|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
12-795 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1321.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 12 DESPKLPEELPVLPLRDVVVYPYVILPLSVSREKSIRAVDTALVENRMILLLSQKQVEMDNPRPEDLYQVGTAALIMRVL 91
Cdd:COG0466 5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 92 KLPDGRIRALVQGLQRVRVEYFTETENLFKARVEPLAEPELKSPdlEQDALMRSVKQTLEKAVALGKTLPQEVLVIAGNL 171
Cdd:COG0466 85 KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDK--ELEALMRSLKEQFEEYVKLNPKIPPELLAALSNI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 172 DNPGRLADLVASNLDLKLQQTQEVLEIAHPGLRLKRVNELLMREIQLLEVQQKITMEARGEMDKSQREYYLRQQLKAIQQ 251
Cdd:COG0466 163 EDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 252 ELGEGSELSEEIAAFRDKLAKMKVPDEPLVEIERNLKKLERMHPDSSETAVTRTYLEWMTELPWGQVTEDNLDLKQAKTV 331
Cdd:COG0466 243 ELGEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 332 LDEDHFGLSKIKDRLLEFLAVRKLKPDLRGTILCFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDESEIRGHRRTYV 411
Cdd:COG0466 323 LDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 412 GAMPGRIVQALHQIKSMNPVIMLDEVDKIGRDMRGDPSAALLEVLDPEQNHTFRDHYLNVPLDLSQVLFLANANELEPIH 491
Cdd:COG0466 403 GAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIP 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 492 PAFRDRMEIIYLSSYTLEEKVGIAEQHLIPKQMEKHGVTRKQVAIPRKALKAIITGYTREAGLRQLERELGAVCRKVARR 571
Cdd:COG0466 483 APLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 572 VAEKTlRKKLTLDEKSIHELLGPVKLLQDERLKAPRVGVVTGLAWTSVGGDVLFVEALKMPGKGLLILTGQLGDVMKESA 651
Cdd:COG0466 563 IAEGK-KKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 652 QAALSYIRSRGDAFQIDPEVFQKQDIHIHFPEGAIPKDGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAIGG 731
Cdd:COG0466 642 QAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGG 721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2490891619 732 LKEKSLAALRLGIKDILIPHANQKDLEEIDPELRKQLRFHPVKHVEEVFEHALVGWKRPEALKP 795
Cdd:COG0466 722 LKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPKKE 785
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
22-784 |
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: 988.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 22 PVLPLRDVVVYPYVILPLSVSREKSIRAVDTALV-ENRMILLLSQKQVEMDNPRPEDLYQVGTAALIMRVLKLPD---GR 97
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRlKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 98 IRALVQGLQRVRVEYFTETENLFKARVEPLAEPELKSPDLEQDALMRSVKQTLEKAVALGKTLPQEV--LVIAGNLDNPG 175
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPFDKDDEEIKALTREIKETFRELISLSKLFREQPalLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 176 RLADLVASNLDLK-LQQTQEVLEIAHPGLRLKRVNELLMREIQLLEVQQKITMEARGEMDKSQREYYLRQQLKAIQQELG 254
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 255 EGSELSEEIAAFRDKLAKMKVPDEPLVEIERNLKKLERMHPDSSETAVTRTYLEWMTELPWGQVTEDNLDLKQAKTVLDE 334
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 335 DHFGLSKIKDRLLEFLAVRKLKPDLRGTILCFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDESEIRGHRRTYVGAM 414
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 415 PGRIVQALHQIKSMNPVIMLDEVDKIGRDMRGDPSAALLEVLDPEQNHTFRDHYLNVPLDLSQVLFLANANELEPIHPAF 494
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 495 RDRMEIIYLSSYTLEEKVGIAEQHLIPKQMEKHGVTRKQVAIPRKALKAIITGYTREAGLRQLERELGAVCRKVARRVAE 574
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 575 KTLRKK-----LTLDEKSIHELLGPVKLLQDERLKAPRVGVVTGLAWTSVGGDVLFVEALKMPGKGLLILTGQLGDVMKE 649
Cdd:TIGR00763 561 QGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 650 SAQAALSYIRSRGDAFQIDPEVFQKQDIHIHFPEGAIPKDGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAI 729
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2490891619 730 GGLKEKSLAALRLGIKDILIPHANQKDLEEIDPELRKQLRFHPVKHVEEVFEHAL 784
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
11-784 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 775.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 11 PDESPKLpeELPVLPLRDVVVYPYVILPLSVSREKSIRAVDTALVENRMILLLSQKQVEMDNPRPEDLYQVGTAALIMRV 90
Cdd:PRK10787 3 PERSERI--EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 91 LKLPDGRIRALVQGLQRVRVEYFTETENLFKARVEPLAEPELKspDLEQDALMRSVKQTLEKAVALGKTLPQEVLVIAGN 170
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTID--EREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 171 LDNPGRLADLVASNLDLKLQQTQEVLEIAHPGLRLKRVNELLMREIQLLEVQQKITMEARGEMDKSQREYYLRQQLKAIQ 250
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 251 QELGEGSELSEEIAAFRDKLAKMKVPDEPLVEIERNLKKLERMHPDSSETAVTRTYLEWMTELPWGQVTEDNLDLKQAKT 330
Cdd:PRK10787 239 KELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 331 VLDEDHFGLSKIKDRLLEFLAVRKLKPDLRGTILCFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDESEIRGHRRTY 410
Cdd:PRK10787 319 ILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 411 VGAMPGRIVQALHQIKSMNPVIMLDEVDKIGRDMRGDPSAALLEVLDPEQNHTFRDHYLNVPLDLSQVLFLANANELEPI 490
Cdd:PRK10787 399 IGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 491 HPAFrDRMEIIYLSSYTLEEKVGIAEQHLIPKQMEKHGVTRKQVAIPRKALKAIITGYTREAGLRQLERELGAVCRKVAR 570
Cdd:PRK10787 479 APLL-DRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 571 RVAEKTLRKKLTLDEKSIHELLGPVKLLQDERLKAPRVGVVTGLAWTSVGGDVLFVEALKMPGKGLLILTGQLGDVMKES 650
Cdd:PRK10787 558 QLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQES 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 651 AQAALSYIRSRGDAFQIDPEVFQKQDIHIHFPEGAIPKDGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAIG 730
Cdd:PRK10787 638 IQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIG 717
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2490891619 731 GLKEKSLAALRLGIKDILIPHANQKDLEEIDPELRKQLRFHPVKHVEEVFEHAL 784
Cdd:PRK10787 718 GLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
325-506 |
2.48e-118 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 354.56 E-value: 2.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 325 LKQAKTVLDEDHFGLSKIKDRLLEFLAVRKLKPDLRGTILCFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDESEIR 404
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 405 GHRRTYVGAMPGRIVQALHQIKSMNPVIMLDEVDKIGRDMRGDPSAALLEVLDPEQNHTFRDHYLNVPLDLSQVLFLANA 484
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 2490891619 485 NELEPIHPAFRDRMEIIYLSSY 506
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
582-786 |
3.19e-103 |
|
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: 316.49 E-value: 3.19e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 582 TLDEKSIHELLGPVKLLQDERLKAPRVGVVTGLAWTSVGGDVLFVEALKMPGKGLLILTGQLGDVMKESAQAALSYIRSR 661
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 662 GDAFQIDPEVFQKQDIHIHFPEGAIPKDGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAIGGLKEKSLAALR 741
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2490891619 742 LGIKDILIPHANQKDLEEIDPELRKQLRFHPVKHVEEVFEHALVG 786
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
20-212 |
2.08e-48 |
|
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: 169.82 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 20 ELPVLPLRDVVVYPYVILPLSVSREKSIRAVDTALVENR--MILLLSQKQVEMDNPRPEDLYQVGTAALIMRVLKLPDGR 97
Cdd:pfam02190 1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKlyGVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 98 IRALVQGLQRVRVEYFTETENLF-KARVEPLAEPELKSpdleQDALMRSVKQTLEKAVALGKTL-PQEVLVIAGNLDNPG 175
Cdd:pfam02190 81 YKVLVEGLERVRIVELVKKEEPYlRAEVEDLPEDSDEL----SEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPG 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 2490891619 176 RLADLVASNLDLKLQQTQEVLEIAHPGLRLKRVNELL 212
Cdd:pfam02190 157 RLADLVAAILPLSPEEKQELLETLDVKERLEKVLELL 193
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
364-506 |
4.19e-26 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 103.83 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 364 LCFVGPPGVGKTSLGKSIARALGRKYARISLGGVhdeseirghRRTYVGAMPGRIVQALHQIKSMNP-VIMLDEVDKIGR 442
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSEL---------VSKYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490891619 443 D-------MRGDPSAALLEVLDPEQNHTfrdhylnvpldlSQVLFLANANELEPIHPAFRDRMEIIYLSSY 506
Cdd:pfam00004 72 SrgsggdsESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
|
|
| LON/PUA |
COG2802 |
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ... |
17-215 |
4.37e-23 |
|
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 442054 [Multi-domain] Cd Length: 194 Bit Score: 97.64 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 17 LPEELPVLPLrDVVVYPYVILPLSVSREKSIRAVDTALVENR---MILLLSQKQVEmdnpRPEDLYQVGTAALIMRVLKL 93
Cdd:COG2802 3 LPMELPLFPL-GAVLFPGGRLPLHIFEPRYLDMVRDCLAGDRpfgVVLIREGREVG----GPPPLYDVGTLARITDFEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 94 PDGRIRALVQGLQRVRVEYFTETENLF-KARVEPLAEPELKSPDLEQDALMRSVKQTLEKAVALGKtlpqevLVIAGNLD 172
Cdd:COG2802 78 EDGRLDITLRGVQRFRILEELQEDDPYrVAEVEWLPDEPDLPVPEELEALRERLLRLLRRYPELAG------LEADPDLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2490891619 173 NPGRLADLVASNLDLKLQQTQEVLEIAHPGLRLKRVNELLMRE 215
Cdd:COG2802 152 DPEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
342-503 |
2.57e-15 |
|
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: 73.86 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 342 IKDRLLEFLAVRKLKPDLR------GTILCFVGPPGVGKTSLGKSIARALGRKYARISLggvhdeSEIRGHRRTYVGAMP 415
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRryglglPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKL------SSLLSKYVGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 416 GRIVQALHQIKsmNPVIMLDEVDKIGRD--------MRGDPSAALLEVLDPEQNhtfrdhylnvpldLSQVLFLANANEL 487
Cdd:cd19481 75 RKIFERARRLA--PCILFIDEIDAIGRKrdssgesgELRRVLNQLLTELDGVNS-------------RSKVLVIAATNRP 139
|
170
....*....|....*....
gi 2490891619 488 EPIHPAFRDR---MEIIYL 503
Cdd:cd19481 140 DLLDPALLRPgrfDEVIEF 158
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
177-526 |
3.34e-14 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 75.33 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 177 LADLVASNLDLKLQQTQEVLEIAHPGLRLKRVNELLMREIQLLEVQQKITMEARGEMDKSQREYYLRQQLKAIQQELGEG 256
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 257 SELSEEIAAFRDKLAKMKVPDEPLVEIERNLKKLERMHPDSSETAVTRTYLEWMTELPWGQVTEDNLDLKQAKTVLDEDh 336
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 337 FGLSKIKDRLLEFLAVRKLKPDLRGTI-------LCFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDEseirghrrt 409
Cdd:COG0464 160 GGLEEVKEELRELVALPLKRPELREEYglppprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 410 YVGAMPGRIVQALHQIKSMNP-VIMLDEVDKI--GRDMRGDPSA-----ALLEVLDpeqNHTFRdhylnvpldlsqVLFL 481
Cdd:COG0464 231 YVGETEKNLREVFDKARGLAPcVLFIDEADALagKRGEVGDGVGrrvvnTLLTEME---ELRSD------------VVVI 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2490891619 482 ANANELEPIHPAFRDRM-EIIYLSSYTLEEKVGIAEQHLIPKQMEK 526
Cdd:COG0464 296 AATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDE 341
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
676-759 |
3.42e-14 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 72.32 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 676 DIHIHFPEGAIPKDGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAIGGLKEKSLAALRLGIKDILIPHANQK 755
Cdd:COG1750 95 DVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAI 174
|
....
gi 2490891619 756 DLEE 759
Cdd:COG1750 175 LTGY 178
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
343-501 |
2.92e-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: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 343 KDRLLEFLAVRKLKPDLRGTILCFVGPPGVGKTSLGKSIARALGRKYARI------SLGGVHDESEIRGHRRTYVGAMPG 416
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylnasDLLEGLVVAELFGHFLVRLLFELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 417 RivqalhqiKSMNPVIMLDEVDKIGRDMrgdpSAALLEVLdpeqnHTFRDHYLNVplDLSQVLFLANANELEPIHPAFRD 496
Cdd:cd00009 81 E--------KAKPGVLFIDEIDSLSRGA----QNALLRVL-----ETLNDLRIDR--ENVRVIGATNRPLLGDLDRALYD 141
|
....*
gi 2490891619 497 RMEII 501
Cdd:cd00009 142 RLDIR 146
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
334-519 |
8.62e-11 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 62.98 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 334 EDHFGLSKIKDRLLEFLAVRKLKPDLRG-------TILcFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDEseirgh 406
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKELRRRENLRKfglwpprKIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 407 rrtYVGAMPGRIVQALHQIKSMNPVIMLDEVDKIGRDmRGDPSA---------ALLEVLDPEQNHtfrdhylnvpldlsq 477
Cdd:COG1223 75 ---YLGETARNLRKLFDFARRAPCVIFFDEFDAIAKD-RGDQNDvgevkrvvnALLQELDGLPSG--------------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2490891619 478 VLFLANANELEPIHPAFRDRM-EIIYLSSYTLEEKVGIAEQHL 519
Cdd:COG1223 136 SVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNL 178
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
689-781 |
1.64e-09 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 61.50 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 689 DGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAIGGLKEK-----SLAALR--LGIKDILIPHANQKDLeEID 761
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKiegffDVCKARglTGKQGVIIPAANVKNL-MLR 670
|
90 100
....*....|....*....|....*
gi 2490891619 762 PELR---KQLRFH--PVKHVEEVFE 781
Cdd:COG1067 671 DEVVeavKAGQFHiyAVEHVDEAIE 695
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
364-498 |
2.25e-08 |
|
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: 53.45 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 364 LCFVGPPGVGKTSLGKSIARAL-GRKYARISLGGVHDESEIRGHRRTYVGAM---PGRIVQALhQIKSmnpVIMLDEVDK 439
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGAswvDGPLVRAA-REGE---IAVLDEINR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490891619 440 IGRDMRGdpsaALLEVLDPEQNHTF-RDHYLNVPLDLSQVLFLANAN--ELEPIHPAFRDRM 498
Cdd:pfam07728 78 ANPDVLN----SLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLdrGLNELSPALRSRF 135
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
364-502 |
7.45e-07 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 49.87 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 364 LCFVGPPGVGKTSLGKSIARAL---GRKYARISLGGV---HDESEIRGHRRTYVGA-MPGRIVQALHQiksmNP--VIML 434
Cdd:cd19499 44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYmekHSVSRLIGAPPGYVGYtEGGQLTEAVRR----KPysVVLL 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2490891619 435 DEVDKIGRDMRGdpsaALLEVLDpeqNHTFRDHYLNVpLDLSQVLFLANANELEpihPAFRDRM-EIIY 502
Cdd:cd19499 120 DEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSNHFR---PEFLNRIdEIVV 177
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
284-580 |
1.15e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 51.16 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 284 ERNLKKLERMHPDSSETAVTRTYLEwmTELPWGQVTEDNLDLKQAKTVLDEDHFGLSKIKDRLLEFLAVRKLKPDL---- 359
Cdd:COG1222 30 ALLLQPVKALELLEEAPALLLNDAN--LTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELfrky 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 360 ----RGTILcFVGPPGVGKTSLGKSIARALGRKYARISLggvhdeSEIrghRRTYVGAmPGRIVQALHQ-IKSMNP-VIM 433
Cdd:COG1222 108 giepPKGVL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG------SEL---VSKYIGE-GARNVREVFElAREKAPsIIF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 434 LDEVDKIGRdMRGDPS---------AALLEVLDpeqnhTFRdhylnvplDLSQVLFLANANELEPIHPAFR-----DRme 499
Cdd:COG1222 177 IDEIDAIAA-RRTDDGtsgevqrtvNQLLAELD-----GFE--------SRGDVLIIAATNRPDLLDPALLrpgrfDR-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 500 IIYLSSYTLEEKVGIAEQHLIPKQMEKhGVTRKQVAiprKALK----AIITGYTREAGLRQLERELGAVCRKVARRVAEK 575
Cdd:COG1222 241 VIEVPLPDEEAREEILKIHLRDMPLAD-DVDLDKLA---KLTEgfsgADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEK 316
|
....*
gi 2490891619 576 TLRKK 580
Cdd:COG1222 317 VKKKT 321
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-497 |
4.01e-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: 47.37 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 360 RGTILCFVGPPGVGKTSLGKSIARALGRKYARI-------SLGGVHDESEIRGHRRTYVGAMPGRIVQALHQI--KSMNP 430
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490891619 431 VIMLDEVDKIGRDMrgdpSAALLEVLDPEQNHTFRDHYLNVPldlsqvLFLANANELEPIHPAFRDR 497
Cdd:smart00382 81 VLILDEITSLLDAE----QEALLLLLEELRLLLLLKSEKNLT------VILTTNDEKDLGPALLRRR 137
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
686-753 |
1.07e-05 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 45.52 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2490891619 686 IPKDGPSAGLAIATVLLSVLKDVPVRNTLAMTGEIDLRGEALAIGGLKEKSLAALRLGIKDILIPHAN 753
Cdd:pfam13541 54 LKKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
338-457 |
3.41e-05 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 45.09 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 338 GLSKIKDRLLEFLAVRKLKPDL---------RGTILCfvGPPGVGKTSLGKSIARALGRKYARIS----LGGVHDESEir 404
Cdd:cd19518 4 GMDSTLKELCELLIHPILPPEYfqhlgveppRGVLLH--GPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESE-- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490891619 405 ghrrtyvgampGRIVQALHQIKSMNPVIM-LDEVDKIG-------RDMRGDPSAALLEVLD 457
Cdd:cd19518 80 -----------EKIRELFDQAISNAPCIVfIDEIDAITpkresaqREMERRIVSQLLTCMD 129
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
20-66 |
9.40e-05 |
|
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: 42.04 E-value: 9.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2490891619 20 ELPVLPLRDVVVYPYVILPLSVSREKSIRAVDTALV--ENRMILLLSQK 66
Cdd:smart00464 1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRrsQPYVIVFLLQD 49
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
368-497 |
1.43e-04 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 44.39 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 368 GPPGVGKTSLGKSIARALGRKYARI----SLggvhDESEIRGH-------RRTYVgaMPGRIVQalhqiksmnPVIMLDE 436
Cdd:COG0714 38 GVPGVGKTTLAKALARALGLPFIRIqftpDL----LPSDILGTyiydqqtGEFEF--RPGPLFA---------NVLLADE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490891619 437 VDkigrdmRGDP--SAALLEVLD------PEQNHTFRDHYLnvpldlsqVLFLANANELE---PIHPAFRDR 497
Cdd:COG0714 103 IN------RAPPktQSALLEAMEerqvtiPGGTYKLPEPFL--------VIATQNPIEQEgtyPLPEAQLDR 160
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
366-437 |
1.51e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 45.08 E-value: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490891619 366 FVGPPGVGKTSLGKSIARALGRKYARIS--LGGVHDeseIRghrrtyvgampgRIVQALHQIKSM--NPVIMLDEV 437
Cdd:PRK13342 41 LWGPPGTGKTTLARIIAGATDAPFEALSavTSGVKD---LR------------EVIEEARQRRSAgrRTILFIDEI 101
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
338-440 |
1.63e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 43.05 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 338 GLSKIKDRLLEFLAVRKLKPDL---------RGTILcfVGPPGVGKTSLGKSIARALGRKYARISlggvhdeseirGHrr 408
Cdd:cd19503 4 GLDEQIASLKELIELPLKYPELfralglkppRGVLL--HGPPGTGKTLLARAVANEAGANFLSIS-----------GP-- 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 2490891619 409 TYVGAMPGRIVQALHQI----KSMNP-VIMLDEVDKI 440
Cdd:cd19503 69 SIVSKYLGESEKNLREIfeeaRSHAPsIIFIDEIDAL 105
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
361-521 |
1.69e-04 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 42.95 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 361 GTILcFVGPPGVGKTSLGKSIARALG---RKYARIslggvhDESEIrgHRRTYV----GAMPGRIVQA----LHQIKSMN 429
Cdd:pfam07724 4 GSFL-FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGYEeggqLTEAVRRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 430 P--VIMLDEVDKIGRD-MRgdpsaALLEVLDpeqNHTFRDHYlNVPLDLSQVLFLA--NANELEPIHpAFRDRMEIIYLS 504
Cdd:pfam07724 75 PysIVLIDEIEKAHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMtgNFGSEKISD-ASRLGDSPDYEL 144
|
170
....*....|....*..
gi 2490891619 505 syTLEEKVGIAEQHLIP 521
Cdd:pfam07724 145 --LKEEVMDLLKKGFIP 159
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
360-493 |
2.14e-04 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410909 [Multi-domain] Cd Length: 171 Bit Score: 42.60 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 360 RGTILcfVGPPGVGKTSLGKSIARALGRKYARISlGGVHDEseirghrrTYVGAMPGRIVQALHQIKSMNP-VIMLDEVD 438
Cdd:cd19501 38 KGVLL--VGPPGTGKTLLAKAVAGEAGVPFFSIS-GSDFVE--------MFVGVGASRVRDLFEQAKKNAPcIVFIDEID 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2490891619 439 KIGRDmRGDPSAallevldpeQNHTFRDHYLN---VPLD----LSQVLFLANANELEPIHPA 493
Cdd:cd19501 107 AVGRK-RGAGLG---------GGHDEREQTLNqllVEMDgfesNTGVIVIAATNRPDVLDPA 158
|
|
| ftsH |
CHL00176 |
cell division protein; Validated |
366-446 |
2.90e-04 |
|
cell division protein; Validated
Pssm-ID: 214386 [Multi-domain] Cd Length: 638 Bit Score: 44.27 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 366 FVGPPGVGKTSLGKSIARALGRKYarISLGGvhdeSEIrghRRTYVGAMPGRIVQALHQIKSMNPVIM-LDEVDKIGRDm 444
Cdd:CHL00176 221 LVGPPGTGKTLLAKAIAGEAEVPF--FSISG----SEF---VEMFVGVGAARVRDLFKKAKENSPCIVfIDEIDAVGRQ- 290
|
..
gi 2490891619 445 RG 446
Cdd:CHL00176 291 RG 292
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
360-438 |
4.61e-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: 41.46 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 360 RGTILCFVGPPGVGKTSLGKSIARALGRKYARISLGGVHDESEIRGHRRTYVGAMPG---------RIVQALHqikSMNP 430
Cdd:cd00267 24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrqrvALARALL---LNPD 100
|
....*...
gi 2490891619 431 VIMLDEVD 438
Cdd:cd00267 101 LLLLDEPT 108
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
318-442 |
7.14e-04 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 43.10 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 318 VTEDNLDLKQAKTV-LDEDHFGLSKIKDRLLEFLAVRKLKPDLRGTILcFVGPPGVGKTSLGKSIARALGRKYARISLGg 396
Cdd:PRK10733 142 LTEDQIKTTFADVAgCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVL-MVGPPGTGKTLLAKAIAGEAKVPFFTISGS- 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2490891619 397 vhDESEIrghrrtYVGAMPGRIVQALHQIKSMNP-VIMLDEVDKIGR 442
Cdd:PRK10733 220 --DFVEM------FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGR 258
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
368-404 |
7.97e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 42.74 E-value: 7.97e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2490891619 368 GPPGVGKTSLGKSIARALGRKYARIS--LGGVhdeSEIR 404
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALSavTSGV---KDIR 91
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
690-800 |
1.27e-03 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 41.72 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 690 GPSAGLAIAtvlLSVL-----------KDVpvrntlAMTGEIDLRGEALAIGGLKEKSLAALRLGIKDILIPHANQKDLE 758
Cdd:COG3480 240 GPSAGLMFA---LGIYdqltpgdltggKKI------AGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAV 310
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2490891619 759 EIDPElrkQLRFHPVKHVEEvfehALvgwkrpEALKPIRKKR 800
Cdd:COG3480 311 GTIPT---GLKVVPVDTLDD----AL------DALEALRAGG 339
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
334-440 |
1.33e-03 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410933 [Multi-domain] Cd Length: 186 Bit Score: 40.74 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 334 EDHFGLSKIKDRLLEFLAVRKLKPD----LRGT---ILCFvGPPGVGKTSLGKSIARALGRKYARISLGGVHDEseirgh 406
Cdd:cd19525 22 ADIAGLEFAKKTIKEIVVWPMLRPDiftgLRGPpkgILLF-GPPGTGKTLIGKCIASQSGATFFSISASSLTSK------ 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 2490891619 407 rrtYVGAMPgRIVQALHQIKSMN--PVIMLDEVDKI 440
Cdd:cd19525 95 ---WVGEGE-KMVRALFSVARCKqpAVIFIDEIDSL 126
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
204-384 |
2.53e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 41.03 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 204 RLKRVNELlMREIQLLEVQQKITMEARGEMDKSQREYYLRQQLKAIQQELgegSELSEEIAAFRD-------KLAKMKVP 276
Cdd:PRK05703 84 RPSRTNSQ-DALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKEL---DELRDELKELKNlledqlsGLRQVERI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 277 DEPLVEIERNLKKLErMHPDSSEtavtrtylEWMTELPwgqvteDNLDLKQAKTVldedhfglSKIKDRLLEFLAVRKLK 356
Cdd:PRK05703 160 PPEFAELYKRLKRSG-LSPEIAE--------KLLKLLL------EHMPPRERTAW--------RYLLELLANMIPVRVED 216
|
170 180
....*....|....*....|....*....
gi 2490891619 357 PDLRGTILCFVGPPGVGK-TSLGKSIARA 384
Cdd:PRK05703 217 ILKQGGVVALVGPTGVGKtTTLAKLAARY 245
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
364-389 |
3.38e-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: 38.96 E-value: 3.38e-03
10 20
....*....|....*....|....*.
gi 2490891619 364 LCFVGPPGVGKTSLGKSIARALGRKY 389
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPF 26
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
335-440 |
3.87e-03 |
|
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410932 [Multi-domain] Cd Length: 164 Bit Score: 39.06 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 335 DHFGLSKIKDRLLEFLAVRKLKPDL--------RGTILcfVGPPGVGKTSLGKSIARALGRKYARISLGGVHDEseirgh 406
Cdd:cd19524 1 DIAGQDLAKQALQEMVILPSLRPELftglrapaRGLLL--FGPPGNGKTMLAKAVAAESNATFFNISAASLTSK------ 72
|
90 100 110
....*....|....*....|....*....|....*.
gi 2490891619 407 rrtYVGAMPgRIVQALHQI-KSMNP-VIMLDEVDKI 440
Cdd:cd19524 73 ---YVGEGE-KLVRALFAVaRELQPsIIFIDEVDSL 104
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
368-444 |
4.18e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 38.62 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 368 GPPGVGKTSLGKSIARALGRKYarISLGGVHDEsEIrGHRRTYVGAMPG---RIVQALHQIKSMNPVIMldevdkIGRDM 444
Cdd:cd02020 6 GPAGSGKSTVAKLLAKKLGLPY--LDTGGIRTE-EV-GKLASEVAAIPEvrkALDERQRELAKKPGIVL------EGRDI 75
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
351-465 |
5.19e-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: 40.21 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 351 AVRKLKPDLRGTILCFVGPPGVGKTslgkSIARALGRKYAriSLGGVHDESEIRGHRRTYVGAMPGRIVQALHQI--KSM 428
Cdd:TIGR03922 302 AERGLPVAQTSNHMLFAGPPGTGKT----TIARVVAKIYC--GLGVLRKPLVREVSRADLIGQYIGESEAKTNEIidSAL 375
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2490891619 429 NPVIMLDEVDKI--GRDMRGDP--SAALLEVLDPEQNHTFR 465
Cdd:TIGR03922 376 GGVLFLDEAYTLveTGYGQKDPfgLEAIDTLLARMENDRDR 416
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
341-437 |
5.38e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 39.93 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490891619 341 KIKDRLLEFLAVRKlkpdlrgtILCFVGPPGVGKTSLGKSIARALgRKYARISLggvhDESEIRGhrrtYVGAMPGRIVQ 420
Cdd:COG1373 8 KILDKLLKLLDNRK--------AVVITGPRQVGKTTLLKQLAKEL-ENILYINL----DDPRLRA----LAEEDPDDLLE 70
|
90
....*....|....*..
gi 2490891619 421 ALHQIKSMNPVIMLDEV 437
Cdd:COG1373 71 ALKELYPGKTYLFLDEI 87
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
367-389 |
5.70e-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: 38.31 E-value: 5.70e-03
|
| TsaE |
pfam02367 |
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ... |
348-386 |
8.54e-03 |
|
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).
Pssm-ID: 460540 Cd Length: 127 Bit Score: 37.03 E-value: 8.54e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2490891619 348 EFLAvRKLKPdlrGTILCFVGPPGVGKTSLGKSIARALG 386
Cdd:pfam02367 12 KRLA-ALLKP---GDVILLSGDLGAGKTTFTRGLARGLG 46
|
|
| |
