|
Name |
Accession |
Description |
Interval |
E-value |
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
10-829 |
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: 1052.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 10 PLLVEEDTFLYPFMIAPIFLQNNAS---IKAVAYAKNNKSLVFIACQKDKLNDNEAPYYDVGVIGSVMREANMPNgRVKL 86
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSiklIKEALRLKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPS-SGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 87 LFNGIAKGRILEPAKE--NEQGFLEAQISPIE--YLEYDKENIQAIVEVLKEKVITLANVSSLF--PPDLIKALEDNDDP 160
Cdd:TIGR00763 80 TYKVVVEGLRRIRIKElsDKGGYLVVRVDNLKeePFDKDDEEIKALTREIKETFRELISLSKLFreQPALLSALEDIDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 161 NRIADLIAAALHLK-KDQAYSLFANNNTEQRLLDLIDIVIEETKTQKLQKEIKSKVHQKMEQTNKEYFLKEQLKQIQKEL 239
Cdd:TIGR00763 160 GRLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 240 GTDKQRDEDLNQYYQKLESIKpfLKEEAFKEIKKQIDRLSRTHADSSDSATLQNYIETMLDVPFGQYGKKALDIKHVREQ 319
Cdd:TIGR00763 240 GIEKDDKDELEKLKEKLEELK--LPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 320 LDKDHYSLKRPKERIVEYFATMQLLEMRRkkkpekkdktkGTILCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDV 399
Cdd:TIGR00763 318 LDEDHYGLKKVKERILEYLAVQKLRGKMK-----------GPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 400 NELRGHRRTYIGSMPGRIVQGLIEAKKMNPVMVLDEIDKVDRSVRGDPASALLEILDPEQNIAFRDHYANFSIDLSQVIF 479
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 480 IATANNIDRIPAPLRDRMEFISVSSYTPSEKEEIAKNYLIPQELEKHALKPSEVDISHECLKLIIEKYTREAGVRDLRRQ 559
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 560 IATIMRKAALKYLEDNPHKKgrtkknedkkgedqksenqkgeNKDFCVSITPNNLKEYLERMVFEIDPIDEENKIGIVNG 639
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK----------------------SEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMG 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 640 LAWTPVGGDVLKIEAVKIRGKGELKLTGSLGDVMKESAIIAFSVVKVLLDNETLKaPKIpseadaenkkkkkvlkvYNAY 719
Cdd:TIGR00763 605 LAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGIS-PNF-----------------FEKA 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 720 DLHLHVPEGATPKDGPSAGIAMASVMASILCDMAIRSEVAMTGELTLSGEVLPIGGLKEKLIAAFKAGIKTALIPIKNyE 799
Cdd:TIGR00763 667 DIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKN-R 745
|
810 820 830
....*....|....*....|....*....|
gi 1261086912 800 RDLDEIPAEVRENLNIVAVKNIAEVLEKTL 829
Cdd:TIGR00763 746 RDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
3-830 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1036.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 3 EDFPKILPLLVEEDTFLYPFMIAPIFLQNNASIKAVAYAKNNKSLVFIACQKDKLNDNEAP--YYDVGVIGSVMREANMP 80
Cdd:COG0466 8 EELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPddLYEVGTVAKILQLLKLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 81 NGRVKLLFNGIAKGRILEPAKENeqGFLEAQISPIEYLEYDKENIQAIVEVLKEKVITLANVSSLFPPDLIKALEDNDDP 160
Cdd:COG0466 88 DGTVKVLVEGLQRARIKEFVQEE--PYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 161 NRIADLIAAALHLKKDQAYSLFANNNTEQRLLDLIDIVIEETKTQKLQKEIKSKVHQKMEQTNKEYFLKEQLKQIQKELG 240
Cdd:COG0466 166 GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 241 TDKQRDEDLNQYYQKLESIKpfLKEEAFKEIKKQIDRLSRTHADSSDSATLQNYIETMLDVPFGQYGKKALDIKHVREQL 320
Cdd:COG0466 246 EKDDGEDEIEELREKIEKAK--LPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 321 DKDHYSLKRPKERIVEYFATMQLL-EMRrkkkpekkdktkGTILCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDV 399
Cdd:COG0466 324 DEDHYGLEKVKERILEYLAVRKLKkKLK------------GPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 400 NELRGHRRTYIGSMPGRIVQGLIEAKKMNPVMVLDEIDKVDRSVRGDPASALLEILDPEQNIAFRDHYANFSIDLSQVIF 479
Cdd:COG0466 392 AEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 480 IATANNIDRIPAPLRDRMEFISVSSYTPSEKEEIAKNYLIPQELEKHALKPSEVDISHECLKLIIEKYTREAGVRDLRRQ 559
Cdd:COG0466 472 IATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLERE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 560 IATIMRKAALKYLEdnphkkgrtkkNEDKKgedqksenqkgenkdfcVSITPNNLKEYLERMVFEIDPIDEENKIGIVNG 639
Cdd:COG0466 552 IAKICRKVAKKIAE-----------GKKKK-----------------VTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTG 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 640 LAWTPVGGDVLKIEAVKIRGKGELKLTGSLGDVMKESAIIAFSVVKVLLDNEtlkapKIPSEadaenkkkkkvlkVYNAY 719
Cdd:COG0466 604 LAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEEL-----GIDPD-------------FFEKY 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 720 DLHLHVPEGATPKDGPSAGIAMASVMASILCDMAIRSEVAMTGELTLSGEVLPIGGLKEKLIAAFKAGIKTALIPIKNyE 799
Cdd:COG0466 666 DIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKEN-E 744
|
810 820 830
....*....|....*....|....*....|.
gi 1261086912 800 RDLDEIPAEVRENLNIVAVKNIAEVLEKTLL 830
Cdd:COG0466 745 KDLEEIPEEVKKGLEFHPVEHIDEVLKIALE 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
9-830 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 606.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 9 LPLLVEEDTFLYPFMIAPIFLQNNASIKAVAYAKNNKSLVFIACQKDKLNDNEA--PYYDVGVIGSVMREANMPNGRVKL 86
Cdd:PRK10787 11 IPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGvnDLFTVGTVASILQMLKLPDGTVKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 87 LFNGIAKGRILEPAKENEQgfLEAQISPIEYLEYDKENIQAIVEVLKEKVITLANVSSLFPPDLIKALEDNDDPNRIADL 166
Cdd:PRK10787 91 LVEGLQRARISALSDNGEH--FSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 167 IAAALHLKKDQAYSLFANNNTEQRLLDLIDIVIEETKTQKLQKEIKSKVHQKMEQTNKEYFLKEQLKQIQKELGTDKQRD 246
Cdd:PRK10787 169 IAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 247 EDLNQYYQKLESIKpfLKEEAFKEIKKQIDRLSRTHADSSDSATLQNYIETMLDVPFGQYGKKALDIKHVREQLDKDHYS 326
Cdd:PRK10787 249 DENEALKRKIDAAK--MPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 327 LKRPKERIVEYFATMQLLEMRRkkkpekkdktkGTILCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDVNELRGHR 406
Cdd:PRK10787 327 LERVKDRILEYLAVQSRVNKIK-----------GPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 407 RTYIGSMPGRIVQGLIEAKKMNPVMVLDEIDKVDRSVRGDPASALLEILDPEQNIAFRDHYANFSIDLSQVIFIATANNI 486
Cdd:PRK10787 396 RTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 487 DrIPAPLRDRMEFISVSSYTPSEKEEIAKNYLIPQELEKHALKPSEVDISHECLKLIIEKYTREAGVRDLRRQIATIMRK 566
Cdd:PRK10787 476 N-IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 567 AALKYLEDNPHKKgrtkknedkkgedqksenqkgenkdfcVSITPNNLKEYLERMVFEIDPIDEENKIGIVNGLAWTPVG 646
Cdd:PRK10787 555 AVKQLLLDKSLKH---------------------------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVG 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 647 GDVLKIEAVKIRGKGELKLTGSLGDVMKESAIIAFSVVKVlldnetlKAPKIPSEADaenkkkkkvlkVYNAYDLHLHVP 726
Cdd:PRK10787 608 GDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRA-------RAEKLGINPD-----------FYEKRDIHVHVP 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 727 EGATPKDGPSAGIAMASVMASILCDMAIRSEVAMTGELTLSGEVLPIGGLKEKLIAAFKAGIKTALIPIKNyERDLDEIP 806
Cdd:PRK10787 670 EGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFEN-KRDLEEIP 748
|
810 820
....*....|....*....|....
gi 1261086912 807 AEVRENLNIVAVKNIAEVLEKTLL 830
Cdd:PRK10787 749 DNVIADLDIHPVKRIEEVLTLALQ 772
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
313-505 |
6.85e-108 |
|
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: 328.36 E-value: 6.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 313 IKHVREQLDKDHYSLKRPKERIVEYFATMQLLEMRRkkkpekkdktkGTILCFYGPPGVGKTSLANSIAKAIERPLVRIA 392
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMK-----------GPILCLVGPPGVGKTSLGKSIARALGRKFVRIS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 393 LGGLEDVNELRGHRRTYIGSMPGRIVQGLIEAKKMNPVMVLDEIDKVDRSVRGDPASALLEILDPEQNIAFRDHYANFSI 472
Cdd:cd19500 70 LGGVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPF 149
|
170 180 190
....*....|....*....|....*....|...
gi 1261086912 473 DLSQVIFIATANNIDRIPAPLRDRMEFISVSSY 505
Cdd:cd19500 150 DLSKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
608-829 |
2.05e-86 |
|
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: 272.96 E-value: 2.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 608 SITPNNLKEYLERMVFEIDPIDEENKIGIVNGLAWTPVGGDVLKIEAVKIRGKGELKLTGSLGDVMKESAIIAFSVVKVL 687
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 688 LDNETLKAPKipseadaenkkkkkvlkvYNAYDLHLHVPEGATPKDGPSAGIAMASVMASILCDMAIRSEVAMTGELTLS 767
Cdd:pfam05362 81 AEELGIDPDF------------------FEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261086912 768 GEVLPIGGLKEKLIAAFKAGIKTALIPIKNyERDLDEIPAEVRENLNIVAVKNIAEVLEKTL 829
Cdd:pfam05362 143 GRVLPIGGLKEKLLAAHRAGIKTVIIPKEN-EKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
363-500 |
1.64e-29 |
|
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: 113.84 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDvnelrghrrTYIGSMPGRIVQGLIEAKKMNP-VMVLDEIDKVDR 441
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261086912 442 S-------VRGDPASALLEILDPEQNiafrdhyanfsiDLSQVIFIATANNIDRIPAPLRDRMEFI 500
Cdd:pfam00004 72 SrgsggdsESRRVVNQLLTELDGFTS------------SNSKVIVIAATNRPDKLDPALLGRFDRI 125
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
9-198 |
2.26e-24 |
|
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: 101.26 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 9 LPLLVEEDTFLYPFMIAPIFLQNNASIKAV--AYAKNNKSLVFIACQKDK--LNDNEAPYYDVGVIGSVMREANMPNGRV 84
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIeaALNKDKLYGVLLVSQKDAedEEPTPDDLYEVGTVAKIVQILKLPDGTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 85 KLLFNGIAKGRILEPAKENEqGFLEAQISPIEYLEydKENIQAIVEVLKEKVITLANVSSLF-PPDLIKALEDNDDPNRI 163
Cdd:pfam02190 82 KVLVEGLERVRIVELVKKEE-PYLRAEVEDLPEDS--DELSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1261086912 164 ADLIAAALHLKKDQAYSLFANNNTEQRLLDLIDIV 198
Cdd:pfam02190 159 ADLVAAILPLSPEEKQELLETLDVKERLEKVLELL 193
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
719-826 |
1.11e-18 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 85.42 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 719 YDLHLHVPEGATPKDGPSAGIAMASVMASILCDMAIRSEVAMTGELTLSGEVLPIGGLKEKLIAAFKAGIKTALIPIKNY 798
Cdd:COG1750 94 YDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQA 173
|
90 100 110
....*....|....*....|....*....|....*..
gi 1261086912 799 E---------RDLDEIPAEVRENLNIVAVKNIAEVLE 826
Cdd:COG1750 174 IltgyntqvgETVDLVEYGKELGVKVIEVSTIADALQ 210
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
363-494 |
1.99e-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: 74.24 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLedVNELRGhrrtYIGSMPGRIVQgliEAKKMNPVMVL-DEIDKV-- 439
Cdd:cd19481 29 ILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSL--LSKYVG----ESEKNLRKIFE---RARRLAPCILFiDEIDAIgr 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261086912 440 DRSVRGDPA------SALLEILDPEQNiafrdhyanfsidLSQVIFIATANNIDRI-PAPLR 494
Cdd:cd19481 100 KRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNRPDLLdPALLR 148
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
363-575 |
3.16e-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: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLedVNElrghrrtYIGSMPGRIVQGLIEAKKMNP-VMVLDEIDKV-- 439
Cdd:COG0464 194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSK-------YVGETEKNLREVFDKARGLAPcVLFIDEADALag 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 440 DRSVRGDPA-----SALLEILDpeqNIAFRdhyanfsidlsqVIFIATANNIDRIPAPLRDRMEF-ISVSSYTPSEKEEI 513
Cdd:COG0464 265 KRGEVGDGVgrrvvNTLLTEME---ELRSD------------VVVIAATNRPDLLDPALLRRFDEiIFFPLPDAEERLEI 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261086912 514 AKNYLIPQELEkhalkpSEVDISHeclkliIEKYTREAGVRDlrrqIATIMRKAALKYLEDN 575
Cdd:COG0464 330 FRIHLRKRPLD------EDVDLEE------LAEATEGLSGAD----IRNVVRRAALQALRLG 375
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
363-500 |
5.80e-12 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 64.09 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKAIERPLVR-IALGGLEDVNELRGHRRtyIGSMPGRIVQGLIEAKKmNPVMVLDEIDKVDR 441
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFRPGAPfLYLNASDLLEGLVVAEL--FGHFLVRLLFELAEKAK-PGVLFIDEIDSLSR 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261086912 442 SVRgdpaSALLEILDPEqniafrdHYANFSIDLSQVIFIATANNIDRIPAPLRDRMEFI 500
Cdd:cd00009 99 GAQ----NALLRVLETL-------NDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
363-501 |
9.74e-11 |
|
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: 61.42 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKAI---ERPLVRIalggleDVNEL-RGHRRTYIGSMPGRIV---QG--LIEAKKMNP--VM 431
Cdd:cd19499 44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRI------DMSEYmEKHSVSRLIGAPPGYVgytEGgqLTEAVRRKPysVV 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 432 VLDEIDKVDRSVRGdpasALLEILDpeqNIAFRDHYANfSIDLSQVIFIATANNIdripaplrdRMEFIS 501
Cdd:cd19499 118 LLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGR-TVDFKNTIIIMTSNHF---------RPEFLN 170
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
363-497 |
1.05e-10 |
|
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: 60.00 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKAIE-RPLVRIALGGLEDVNELRGHRRtyIGSMPGRIVQG-LIEAKKMNPVMVLDEIDKVD 440
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261086912 441 RSVrgdpASALLEILDPEQ----NIAFRDHYANFSidlsqVIFIATANNIDR----IPAPLRDRM 497
Cdd:pfam07728 80 PDV----LNSLLSLLDERRlllpDGGELVKAAPDG-----FRLIATMNPLDRglneLSPALRSRF 135
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
734-826 |
2.40e-09 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 59.82 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 734 GPSAGIAMAsvmasilcdMAIRSE-----------VAMTGELTLSGEVLPIGGLKEKLIAAFKAGIKTALIPIKNYerdl 802
Cdd:COG3480 240 GPSAGLMFA---------LGIYDQltpgdltggkkIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNC---- 306
|
90 100
....*....|....*....|....
gi 1261086912 803 DEIPAEVRENLNIVAVKNIAEVLE 826
Cdd:COG3480 307 AEAVGTIPTGLKVVPVDTLDDALD 330
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
365-589 |
3.37e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 58.36 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDvnelrghrrTYIGSMPGRIVQgLIEAKKMNPVMV-LDEIDKVDRSv 443
Cdd:COG1223 40 FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG---------SYLGETARNLRK-LFDFARRAPCVIfFDEFDAIAKD- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 444 RGDPA---------SALLEILDPEQniafrdhyanfsidlSQVIFIATANNIDRIPAPLRDRMEF-ISVSSYTPSEKEEI 513
Cdd:COG1223 109 RGDQNdvgevkrvvNALLQELDGLP---------------SGSVVIAATNHPELLDSALWRRFDEvIEFPLPDKEERKEI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 514 AKNYL----IPQELEKHALKPSEVDISHEclklIIEKYTREA---GVRDLRRQIATIMRKAALKylednpHKKGRTKKNE 586
Cdd:COG1223 174 LELNLkkfpLPFELDLKKLAKKLEGLSGA----DIEKVLKTAlkkAILEDREKVTKEDLEEALK------QRKERKKEPK 243
|
...
gi 1261086912 587 DKK 589
Cdd:COG1223 244 KEG 246
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-500 |
7.03e-09 |
|
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: 55.46 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 360 GTILCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDVNELRGHRRTYIG-------SMPGRIVQGLIE-AKKMNP-V 430
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIvggkkasGSGELRLRLALAlARKLKPdV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261086912 431 MVLDEIDKVDRSVRgdpaSALLEILDPEQNIAFRDHYANfsidlsqVIFIATANNI-DRIPAPLRDRMEFI 500
Cdd:smart00382 82 LILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEkDLGPALLRRRFDRR 141
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
367-514 |
8.27e-09 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 57.87 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 367 GPPGVGKTSLANSIAKAIERPLVRI----------ALgGLEDVNELRGHRRTyigsMPGRIVQGLIEAkkmnpvmvlDEI 436
Cdd:COG0714 38 GVPGVGKTTLAKALARALGLPFIRIqftpdllpsdIL-GTYIYDQQTGEFEF----RPGPLFANVLLA---------DEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 437 DkvdrsvRGDPA--SALLEILDPEQniafrdhyanFSID-----LSQVIF-IATANNID-----RIPAPLRDR-MEFISV 502
Cdd:COG0714 104 N------RAPPKtqSALLEAMEERQ----------VTIPggtykLPEPFLvIATQNPIEqegtyPLPEAQLDRfLLKLYI 167
|
170
....*....|..
gi 1261086912 503 SsyTPSEKEEIA 514
Cdd:COG0714 168 G--YPDAEEERE 177
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
365-579 |
2.34e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 56.55 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRIALGGLedvnelrghRRTYIGSmPGRIVQGLIE-AKKMNP-VMVLDEIDKVDRS 442
Cdd:COG1222 117 LYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL---------VSKYIGE-GARNVREVFElAREKAPsIIFIDEIDAIAAR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 443 vRGDPAS---------ALLEILDpeqniafrdhyaNFSiDLSQVIFIATANNIDRI-PAPLR----DRMefISVSSYTPS 508
Cdd:COG1222 187 -RTDDGTsgevqrtvnQLLAELD------------GFE-SRGDVLIIAATNRPDLLdPALLRpgrfDRV--IEVPLPDEE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 509 EKEEIAKNYLIPQELEKhalkpsEVDISheclKLI----------IEKYTREAGVRDLRRQIATI----MRKAALKYLED 574
Cdd:COG1222 251 AREEILKIHLRDMPLAD------DVDLD----KLAkltegfsgadLKAIVTEAGMFAIREGRDTVtmedLEKAIEKVKKK 320
|
....*
gi 1261086912 575 NPHKK 579
Cdd:COG1222 321 TETAT 325
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
360-530 |
2.41e-08 |
|
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: 54.12 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 360 GTILcFYGPPGVGKTSLANSIAKAI---ERPLVRI-ALGGLED--VNELrghrrtyIGSMPGRIVQG----LIEAKKMNP 429
Cdd:pfam07724 4 GSFL-FLGPTGVGKTELAKALAELLfgdERALIRIdMSEYMEEhsVSRL-------IGAPPGYVGYEeggqLTEAVRRKP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 430 VMV--LDEIDKVDRSVrgdpASALLEILD-----PEQNIafrdhyanfSIDLSQVIFIATAnNIDripaplrdrMEFISV 502
Cdd:pfam07724 76 YSIvlIDEIEKAHPGV----QNDLLQILEggtltDKQGR---------TVDFKNTLFIMTG-NFG---------SEKISD 132
|
170 180
....*....|....*....|....*...
gi 1261086912 503 SSYTPSEKEEIAKNYLIPQELEKHaLKP 530
Cdd:pfam07724 133 ASRLGDSPDYELLKEEVMDLLKKG-FIP 159
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
365-399 |
2.70e-06 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 50.47 E-value: 2.70e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRI--ALGGLEDV 399
Cdd:PRK13342 41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGVKDL 77
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
365-408 |
7.80e-06 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 49.28 E-value: 7.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRI--ALGGLEDV--------NELRGHRRT 408
Cdd:COG2256 54 LWGPPGTGKTTLARLIANATDAEFVALsaVTSGVKDIrevieearERRAYGRRT 107
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
365-528 |
4.13e-05 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 46.12 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAI------------ERPLVRIALGGLEDVNELrghRRTYIGSMPGR-IVQGLIEAKKMNP-- 429
Cdd:COG0470 23 LHGPPGIGKTTLALALARDLlcenpeggkacgQCHSRLMAAGNHPDLLEL---NPEEKSDQIGIdQIRELGEFLSLTPle 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 430 ----VMVLDEIDKvdrsVRGDPASALLEIL-DPEQNiafrdhyanfsidlsqVIFIATANNIDRIPAPLRDRMEFISVSs 504
Cdd:COG0470 100 ggrkVVIIDEADA----MNEAAANALLKTLeEPPKN----------------TPFILIANDPSRLLPTIRSRCQVIRFR- 158
|
170 180
....*....|....*....|....
gi 1261086912 505 yTPSEKEeiAKNYLIPQELEKHAL 528
Cdd:COG0470 159 -PPSEEE--ALAWLREEGVDEDAL 179
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
362-515 |
5.86e-05 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 46.14 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 362 ILCFYGPPGVGKTSLANSIAKAI--ERPLVRIALGGLEDVnelRGHRRTYIGSMpgrivqGLIEAKKmnpVMVLDEIDK- 438
Cdd:PHA02544 45 MLLHSPSPGTGKTTVAKALCNEVgaEVLFVNGSDCRIDFV---RNRLTRFASTV------SLTGGGK---VIIIDEFDRl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 439 ----VDRSVRGdpasaLLEildpeqniafrdhyaNFSidlSQVIFIATANNIDRIPAPLRDRMEFISVSSYTPSEKEEIA 514
Cdd:PHA02544 113 gladAQRHLRS-----FME---------------AYS---KNCSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM 169
|
.
gi 1261086912 515 K 515
Cdd:PHA02544 170 K 170
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
365-494 |
5.92e-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: 44.32 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRIALGGLedvnelrghrrtyIGSMPG----RIVQGLIEAKKMNP-VMVLDEIDKV 439
Cdd:cd19518 39 LHGPPGCGKTMLANAIAGELKVPFLKISATEI-------------VSGVSGeseeKIRELFDQAISNAPcIVFIDEIDAI 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1261086912 440 drSVRGDPASALLEILDPEQNIAFRDHYANFSIDLSQVIFIATANNIDRIPAPLR 494
Cdd:cd19518 106 --TPKRESAQREMERRIVSQLLTCMDELNNEKTAGGPVLVIGATNRPDSLDPALR 158
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
365-500 |
7.83e-05 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain] Cd Length: 159 Bit Score: 43.81 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKaiERPLVRIALGGLEDVNElrghrrtYIGSMPGRIVQGLIEAKKMNP-VMVLDEIDKV--DR 441
Cdd:cd19511 32 LYGPPGCGKTLLAKALAS--EAGLNFISVKGPELFSK-------YVGESERAVREIFQKARQAAPcIIFFDEIDSLapRR 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261086912 442 SVRGDPA------SALLEILDP-EQniafrdhyanfsidLSQVIFIATANNIDRI-PAPLR----DRMEFI 500
Cdd:cd19511 103 GQSDSSGvtdrvvSQLLTELDGiES--------------LKGVVVIAATNRPDMIdPALLRpgrlDKLIYV 159
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
365-528 |
8.40e-05 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 45.37 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDvnelrghrrtyigsmPGRIVqGLIEAKKMNPVMVLDEIDKVDRSVR 444
Cdd:TIGR00635 35 LYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK---------------PGDLA-AILTNLEEGDVLFIDEIHRLSPAVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 445 gdpasallEILDPeqniAFRDHYANFSI-----------DLSQVIFIATANNIDRIPAPLRDRMEFIS-VSSYTPSEKEE 512
Cdd:TIGR00635 99 --------ELLYP----AMEDFRLDIVIgkgpsarsvrlDLPPFTLVGATTRAGMLTSPLRDRFGIILrLEFYTVEELAE 166
|
170
....*....|....*...
gi 1261086912 513 IAKNY--LIPQELEKHAL 528
Cdd:TIGR00635 167 IVSRSagLLNVEIEPEAA 184
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
365-500 |
1.20e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 45.53 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAI---ERPLVRIA-----------LGGLEDVNELRGHRRTyigsmPGRIVQGLIEAKKmNP- 429
Cdd:COG1401 226 LAGPPGTGKTYLARRLAEALggeDNGRIEFVqfhpswsyedfLLGYRPSLDEGKYEPT-----PGIFLRFCLKAEK-NPd 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 430 ---VMVLDEIDkvdrsvRGDPASALLEIL------DPEQNIAFRDHYANFSIDLS---QVIFIATANNIDR----IPAPL 493
Cdd:COG1401 300 kpyVLIIDEIN------RANVEKYFGELLsllesdKRGEELSIELPYSGEGEEFSippNLYIIGTMNTDDRslalSDKAL 373
|
....*..
gi 1261086912 494 RDRMEFI 500
Cdd:COG1401 374 RRRFTFE 380
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
365-494 |
1.22e-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: 43.43 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLvrIALGGLEDVnelrghrRTYIGSMPGRIVQGLIEAKKMNP-VMVLDEID------ 437
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEAGANF--LSISGPSIV-------SKYLGESEKNLREIFEEARSHAPsIIFIDEIDalapkr 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261086912 438 -KVDRSVRGDPASALLEILDpeqNIAFRDHyanfsidlsqVIFIATANNIDRIPAPLR 494
Cdd:cd19503 110 eEDQREVERRVVAQLLTLMD---GMSSRGK----------VVVIAATNRPDAIDPALR 154
|
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
363-517 |
1.59e-04 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 44.74 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAK------------AIERP--LVRIaLGGLEDvnelrghrrtyigsmpgrivqglieakkmN 428
Cdd:PRK00080 54 VLLYGPPGLGKTTLANIIANemgvniritsgpALEKPgdLAAI-LTNLEE-----------------------------G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 429 PVMVLDEIDKVDRSVrgdpasalLEILDPeqniAFRDhyanFSIDLsqVI---FIATANNID--------------RIPA 491
Cdd:PRK00080 104 DVLFIDEIHRLSPVV--------EEILYP----AMED----FRLDI--MIgkgPAARSIRLDlppftligattragLLTS 165
|
170 180 190
....*....|....*....|....*....|..
gi 1261086912 492 PLRDR------MEFisvssYTPSEKEEIAKNY 517
Cdd:PRK00080 166 PLRDRfgivqrLEF-----YTVEELEKIVKRS 192
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
366-569 |
1.87e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 44.84 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 366 YGPPGVGKTSLANSIAKAIERP------------------------LVRIA--LGGLEDVNElRGHRRtyiGSMPGRIVQ 419
Cdd:COG1474 57 YGPTGTGKTAVAKYVLEELEEEaeergvdvrvvyvncrqastryrvLSRILeeLGSGEDIPS-TGLST---DELFDRLYE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 420 gLIEAKKMNPVMVLDEIDKVDRSVRGDPASALLEILDpeqniafrdhyanfSIDLSQVIFIATANNID-------RIPAP 492
Cdd:COG1474 133 -ALDERDGVLVVVLDEIDYLVDDEGDDLLYQLLRANE--------------ELEGARVGVIGISNDLEflenldpRVKSS 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261086912 493 LRDRMefISVSSYTPSEKEEIAKNYlipqelEKHALKPsEVdISHECLKLIIEKYTREAGvrDLRRQIAtIMRKAAL 569
Cdd:COG1474 198 LGEEE--IVFPPYDADELRDILEDR------AELAFYD-GV-LSDEVIPLIAALAAQEHG--DARKAID-LLRVAGE 261
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
365-445 |
3.40e-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: 42.22 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLvrIALGGLEDVNelrghrrTYIGSMPGRIVQGLIEAKKMNPVMV-LDEIDKVDRSv 443
Cdd:cd19501 42 LVGPPGTGKTLLAKAVAGEAGVPF--FSISGSDFVE-------MFVGVGASRVRDLFEQAKKNAPCIVfIDEIDAVGRK- 111
|
..
gi 1261086912 444 RG 445
Cdd:cd19501 112 RG 113
|
|
| RNA_helicase |
pfam00910 |
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ... |
363-388 |
4.70e-04 |
|
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.
Pssm-ID: 459992 Cd Length: 102 Bit Score: 40.28 E-value: 4.70e-04
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
365-387 |
6.07e-04 |
|
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.
Pssm-ID: 398900 [Multi-domain] Cd Length: 159 Bit Score: 41.33 E-value: 6.07e-04
10 20 30
....*....|....*....|....*....|....*
gi 1261086912 365 FYGPPGVGKTSLANSIAK------------AIERP 387
Cdd:pfam05496 38 LYGPPGLGKTTLANIIANemgvniritsgpAIERP 72
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
308-529 |
7.48e-04 |
|
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: 42.91 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 308 KKALDIKHVREQLDKdHYSLKRPKERIVEYFATMQLLEMRRKKKPEKKDKTKGTIlcFYGPPGVGKTSLANSIAK----- 382
Cdd:TIGR03922 263 RKAKLLAEAEAELAE-QIGLERVKRQVAALKSSTAMALARAERGLPVAQTSNHML--FAGPPGTGKTTIARVVAKiycgl 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 383 -AIERPLVRialggledvnelRGHRRTYIGSMPGRivqgliEAKKMNPVmvldeIDK-VDRSVRGDPASALLEIL----D 456
Cdd:TIGR03922 340 gVLRKPLVR------------EVSRADLIGQYIGE------SEAKTNEI-----IDSaLGGVLFLDEAYTLVETGygqkD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 457 PEQNIAFRDHYANFSIDLSQVIFIAT--ANNIDR---IPAPLRDRM-EFISVSSYTPSEKEEIAKNYLIPQE--LEKHAL 528
Cdd:TIGR03922 397 PFGLEAIDTLLARMENDRDRLVVIGAgyRKDLDKfleVNEGLRSRFtRVIEFPSYSPDELVEIARRMATERDsvLDDAAA 476
|
.
gi 1261086912 529 K 529
Cdd:TIGR03922 477 D 477
|
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
365-498 |
8.71e-04 |
|
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. 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: 410918 [Multi-domain] Cd Length: 153 Bit Score: 40.80 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDVNELRGHrrtyigsmpgrivqgLIEAKKMNPVMVLDEIDkvdrsvr 444
Cdd:cd19510 28 LYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNH---------------LLNTAPKQSIILLEDID------- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261086912 445 gdpASALLEILDPEQNIAFRDHYA-NFSIDLSQV---------IFIATANNIDRI-PAPLRD-RME 498
Cdd:cd19510 86 ---AAFESREHNKKNPSAYGGLSRvTFSGLLNALdgvasseerIVFMTTNHIERLdPALIRPgRVD 148
|
|
| RuvB |
COG2255 |
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ... |
365-513 |
1.02e-03 |
|
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];
Pssm-ID: 441856 [Multi-domain] Cd Length: 337 Bit Score: 41.99 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAK------------AIERP--LVRIaLGGLEDvnelrghrrtyigsmpgrivqglieakkmNPV 430
Cdd:COG2255 59 LYGPPGLGKTTLAHIIANemgvniritsgpAIEKPgdLAAI-LTNLEE-----------------------------GDV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 431 MVLDEIDKVDRSVRgdpasallEILDPeqniAFRDhyanFSIDlsqvIFI-----ATANNID-----------R---IPA 491
Cdd:COG2255 109 LFIDEIHRLSRVVE--------EILYP----AMED----FRLD----IVIgkgpaARSIRLDlppftlvgattRaglLTS 168
|
170 180
....*....|....*....|....*...
gi 1261086912 492 PLRDR------MEFisvssYTPSEKEEI 513
Cdd:COG2255 169 PLRDRfgivlrLEF-----YTVEELAEI 191
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
363-456 |
1.39e-03 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 41.30 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIA-KAIErplvrialggledvnelRGHrRTYIGSMPgRIVQGLIEA-------KKMN-----P 429
Cdd:COG1484 102 LILLGPPGTGKTHLAIALGhEACR-----------------AGY-RVRFTTAP-DLVNELKEAradgrleRLLKrlakvD 162
|
90 100
....*....|....*....|....*....
gi 1261086912 430 VMVLDEI--DKVDRSVRGDpasaLLEILD 456
Cdd:COG1484 163 LLILDELgyLPLDAEGAEL----LFELIS 187
|
|
| IPT |
pfam01745 |
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ... |
366-483 |
1.79e-03 |
|
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes isopentenyladensosine 5'-monophosphate, a cytokinin that induces shoot formation on host plants infected with the Ti plasmid.
Pssm-ID: 366786 Cd Length: 232 Bit Score: 40.84 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 366 YGPPGVGKTSLANSIAKAIERPLV---------RIALG-GLEDVNELRGHRRTYIGSmpGRIVQGLIEAKKMNPVM---V 432
Cdd:pfam01745 7 WGATCTGKTAEAIALAKETGWPVIvldrvqccsQLATGsGRPLPAELQGTRRIYLDN--RPLSEGIIDAEEAHDRLiaeV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1261086912 433 LDEIDKVDRSVRGDPASALLEIL-DPEQNIAFRDHYANFSIDLSQViFIATA 483
Cdd:pfam01745 85 TSHKDEGGVILEGGSISLLKRMAqSPYWNAGFPWHVKRMRLPDRDV-FLAQA 135
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
366-461 |
1.83e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410910 [Multi-domain] Cd Length: 171 Bit Score: 40.01 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 366 YGPPGVGKTSLANSIAKAIERPLVRIAlgGLEDVnelrghrRTYIGSMPgRIVQGLIE-AKKMNPVMV-LDEID-----K 438
Cdd:cd19502 43 YGPPGTGKTLLAKAVANHTDATFIRVV--GSELV-------QKYIGEGA-RLVRELFEmAREKAPSIIfIDEIDaigakR 112
|
90 100 110
....*....|....*....|....*....|.
gi 1261086912 439 VDRSVRGDP--ASALLEIL------DPEQNI 461
Cdd:cd19502 113 FDSGTGGDRevQRTMLELLnqldgfDPRGNI 143
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
360-480 |
3.50e-03 |
|
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: 38.77 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 360 GTILCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDVNELRGHRRTYIGSMPG-------RIvqGLIEAKKMNP-VM 431
Cdd:cd00267 25 GEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrqRV--ALARALLLNPdLL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1261086912 432 VLDEIDK-VDRSVRGDPASALLEILDPEQNIAFRDHYANFSIDLSQVIFI 480
Cdd:cd00267 103 LLDEPTSgLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
367-445 |
5.23e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain] Cd Length: 183 Bit Score: 38.90 E-value: 5.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261086912 367 GPPGVGKTSLANSIAKAIERPLVRIALGGLEDVNelrghrrtYIGSMPGRIVQGLIEAkkmnpVMVLDEIDKVDRSVRG 445
Cdd:cd19498 53 GPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVG--------YVGRDVESIIRDLVEG-----IVFIDEIDKIAKRGGS 118
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
365-484 |
5.82e-03 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 40.21 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 365 FYGPPGVGKTSLANSIAKAIERPLVRIalggleDVNELrGHRRT---YIGSMPGRI--VQG--LIEAKKMNP--VMVLDE 435
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfDQGglLTDAVIKHPhaVLLLDE 565
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1261086912 436 IDKvdrsVRGDPASALLEILDpeqNIAFRDHYANfSIDLSQVIFIATAN 484
Cdd:PRK11034 566 IEK----AHPDVFNLLLQVMD---NGTLTDNNGR-KADFRNVVLVMTTN 606
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
367-445 |
5.87e-03 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 40.02 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 367 GPPGVGKTSLANSIAKAIERPLVRIAlggLEDVNELrghrrtYIGSMPGRIVQGLIEAKKMNPVMV-LDEIDKVDRSvRG 445
Cdd:PRK10733 192 GPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM------FVGVGASRVRDMFEQAKKAAPCIIfIDEIDAVGRQ-RG 261
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
733-826 |
7.45e-03 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 39.93 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 733 DGPSAgiAMASVMA--SILCDMAIRSEVAMTGELTLSGEVLPIGGLKEKlIAAF-----------KAGIktaLIPIKNYe 799
Cdd:COG1067 592 DGDSA--SSAELYAllSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEK-IEGFfdvckargltgKQGV---IIPAANV- 664
|
90 100 110
....*....|....*....|....*....|.
gi 1261086912 800 RDL---DEIPAEVRENL-NIVAVKNIAEVLE 826
Cdd:COG1067 665 KNLmlrDEVVEAVKAGQfHIYAVEHVDEAIE 695
|
|
| RecA-like_PEX6_r2 |
cd19527 |
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ... |
363-500 |
8.21e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. 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: 410935 [Multi-domain] Cd Length: 160 Bit Score: 37.88 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 363 LCFYGPPGVGKTSLANSIAKaiERPLVRIALGGLEDVNelrghrrTYIGSMPGRIVQGLIEAKKMNP-VMVLDEIDKV-- 439
Cdd:cd19527 29 ILLYGPPGTGKTLLAKAIAT--ECSLNFLSVKGPELIN-------MYIGESEANVREVFQKARDAKPcVIFFDELDSLap 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261086912 440 DRSVRGDPASALLEILdpEQNIAFRDhyaNFSIDLSQVIFIATANNIDRI-PAPLR----DRMEFI 500
Cdd:cd19527 100 SRGNSGDSGGVMDRVV--SQLLAELD---GMSSSGQDVFVIGATNRPDLLdPALLRpgrfDKLLYL 160
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
360-456 |
8.21e-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: 37.87 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261086912 360 GTILCFYGPPGVGKTSLANSIAKAIERPLVRIALGGLEDVNELRG-----HRRTYIGSMPGRIVQGLIEAKKMNPVMVLD 434
Cdd:pfam13191 24 PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPllealTREGLLRQLLDELESSLLEAWRAALLEALA 103
|
90 100
....*....|....*....|..
gi 1261086912 435 EIDKVDRSVRGDPASALLEILD 456
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRLLD 125
|
|
| |
