NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034596222|ref|XP_016879245|]
View 

lon protease homolog 2, peroxisomal isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Lon super family cl33893
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 1-552 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0466:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 637.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466     1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYA- 154
Cdd:COG0466    71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYVk 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 155 -------------------------------------VQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR-KPKQDDDK 196
Cdd:COG0466   147 lnpkippellaalsniedpgrladfiashlplkieekQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKEQMEK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 197 R---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVKEIKRLKKM 256
Cdd:COG0466   227 SqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEKELKKLERM 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 257 PQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVG 336
Cdd:COG0466   285 PPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVG 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 337 KTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALL 416
Cdd:COG0466   365 KTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALL 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 417 EVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQ 496
Cdd:COG0466   445 EVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEE 524

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596222 497 IQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDVTE 552
Cdd:COG0466   525 LKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEK 580
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 1-552 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 637.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466     1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYA- 154
Cdd:COG0466    71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYVk 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 155 -------------------------------------VQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR-KPKQDDDK 196
Cdd:COG0466   147 lnpkippellaalsniedpgrladfiashlplkieekQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKEQMEK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 197 R---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVKEIKRLKKM 256
Cdd:COG0466   227 SqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEKELKKLERM 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 257 PQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVG 336
Cdd:COG0466   285 PPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVG 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 337 KTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALL 416
Cdd:COG0466   365 KTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALL 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 417 EVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQ 496
Cdd:COG0466   445 EVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEE 524

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596222 497 IQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDVTE 552
Cdd:COG0466   525 LKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEK 580
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 14-604 6.48e-174

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: 512.61  E-value: 6.48e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--------------------RLEEFPNTCKMREE-------LGE 145
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKeepfdkddeeikaltreikeTFRELISLSKLFREqpallsaLED 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 146 LSEQFY--------------KYAVQILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRPIRRI 207
Cdd:TIGR00763 156 IDEPGRladfvaaslqlkekDELQEVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQLKAI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 208 THISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLD 287
Cdd:TIGR00763 236 KKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLD 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 288 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 367
Cdd:TIGR00763 311 LKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIR 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 368 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 447
Cdd:TIGR00763 391 GHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATA 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 448 NTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAI 527
Cdd:TIGR00763 471 NSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKI 550

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596222 528 CRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEIA 604
Cdd:TIGR00763 551 CRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYERA 593
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 288-469 7.09e-124

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 363.03  E-value: 7.09e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 288 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 367
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 368 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 447
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                         170       180
                  ....*....|....*....|..
gi 1034596222 448 NTTATIPAALLDRMEIIQVPGY 469
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 229-534 1.52e-115

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 362.33  E-value: 1.52e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 229 LEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKR 308
Cdd:PRK10787  254 LKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDR 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 309 VLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV 388
Cdd:PRK10787  334 ILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKV 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 389 GVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPG 468
Cdd:PRK10787  414 GVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSG 492

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596222 469 YTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVK 534
Cdd:PRK10787  493 YTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVK 557
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 327-469 7.64e-27

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: 105.75  E-value: 7.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 327 LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 405
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596222 406 SLQG-------DPAAALLEVLDPEQNHNftdhylnvafdlSQVLFIATANTTATIPAALLDRMEIIQVPGY 469
Cdd:pfam00004  72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 323-461 1.76e-05

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: 45.06  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  323 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 393
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596222  394 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPAALLDRM 461
Cdd:smart00382  81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRR 137
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 1-552 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 637.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466     1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYA- 154
Cdd:COG0466    71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYVk 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 155 -------------------------------------VQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR-KPKQDDDK 196
Cdd:COG0466   147 lnpkippellaalsniedpgrladfiashlplkieekQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKEQMEK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 197 R---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVKEIKRLKKM 256
Cdd:COG0466   227 SqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEKELKKLERM 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 257 PQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVG 336
Cdd:COG0466   285 PPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVG 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 337 KTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALL 416
Cdd:COG0466   365 KTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALL 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 417 EVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQ 496
Cdd:COG0466   445 EVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEE 524

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596222 497 IQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDVTE 552
Cdd:COG0466   525 LKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEK 580
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 14-604 6.48e-174

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: 512.61  E-value: 6.48e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--------------------RLEEFPNTCKMREE-------LGE 145
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKeepfdkddeeikaltreikeTFRELISLSKLFREqpallsaLED 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 146 LSEQFY--------------KYAVQILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRPIRRI 207
Cdd:TIGR00763 156 IDEPGRladfvaaslqlkekDELQEVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQLKAI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 208 THISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLD 287
Cdd:TIGR00763 236 KKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLD 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 288 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 367
Cdd:TIGR00763 311 LKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIR 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 368 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 447
Cdd:TIGR00763 391 GHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATA 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 448 NTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAI 527
Cdd:TIGR00763 471 NSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKI 550

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034596222 528 CRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEIA 604
Cdd:TIGR00763 551 CRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYERA 593
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 288-469 7.09e-124

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 363.03  E-value: 7.09e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 288 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 367
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 368 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 447
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                         170       180
                  ....*....|....*....|..
gi 1034596222 448 NTTATIPAALLDRMEIIQVPGY 469
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 229-534 1.52e-115

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 362.33  E-value: 1.52e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 229 LEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKR 308
Cdd:PRK10787  254 LKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDR 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 309 VLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV 388
Cdd:PRK10787  334 ILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKV 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 389 GVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPG 468
Cdd:PRK10787  414 GVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSG 492

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596222 469 YTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVK 534
Cdd:PRK10787  493 YTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVK 557
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 327-469 7.64e-27

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: 105.75  E-value: 7.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 327 LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 405
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596222 406 SLQG-------DPAAALLEVLDPEQNHNftdhylnvafdlSQVLFIATANTTATIPAALLDRMEIIQVPGY 469
Cdd:pfam00004  72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 13-176 6.80e-15

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: 73.52  E-value: 6.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  13 LPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGtslQSTILGVIPNTpDPASDAQDLPPLHRIGTAALAVQVVGSn 92
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQK-DAEDEEPTPDDLYEVGTVAKIVQILKL- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  93 wPKPHYTLLITGLCRFQIVQVL-KEKPYPIAEVEQL-----DRLEEFPNTCK-MREELGELSEQFYKYAV---------- 155
Cdd:pfam02190  77 -PDGTYKVLVEGLERVRIVELVkKEEPYLRAEVEDLpedsdELSEALKALVKeLIEKLRRLLKLLLPLELllkikdienp 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034596222 156 -------------------QILDAVSLEERFKMTIPLLVR 176
Cdd:pfam02190 156 grladlvaailplspeekqELLETLDVKERLEKVLELLNR 195
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 293-488 1.61e-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: 75.72  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 293 ILLDNdhyAMEKLKKRVLEYLAVRQLKNNLKGPI---LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 369
Cdd:COG0464   160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 370 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDpaaallevldpeqnhnfTDHYLNVAFD---------LS 439
Cdd:COG0464   231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEV-----------------GDGVGRRVVNtlltemeelRS 290

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034596222 440 QVLFIATANTTATIPAALLDRM-EIIQVPGYTQEEKIEIAHRHLIPKQLE 488
Cdd:COG0464   291 DVVVIAATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD 340
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 301-460 2.92e-14

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: 70.77  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 301 AMEKLKKRVLEYLAVRQL--KNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSdirghrRTYVGSMP 378
Cdd:cd19481     1 LKASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 379 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhnftdhylnvafdLSQVLFIATANTT 450
Cdd:cd19481    75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139

                         170
                  ....*....|
gi 1034596222 451 ATIPAALLDR 460
Cdd:cd19481   140 DLLDPALLRP 149
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 308-469 5.13e-11

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: 61.01  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 308 RVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGR---EFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 384
Cdd:cd00009     3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 385 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhnfTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEII 464
Cdd:cd00009    79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146


                  ....*
gi 1034596222 465 QVPGY 469
Cdd:cd00009   147 IVIPL 151
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 322-526 5.47e-10

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 60.57  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 322 LKGPILcFVGPPGVGKTSVGRSVAKTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 392
Cdd:COG0714    30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 393 ----PVF----LLDEVDKlgkslqGDPA--AALLEVLdpeQNHNFT-DhylNVAFDLSQVLF-IATANT-----TATIPA 455
Cdd:COG0714    88 frpgPLFanvlLADEINR------APPKtqSALLEAM---EERQVTiP---GGTYKLPEPFLvIATQNPieqegTYPLPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 456 ALLDRMEI-IQVpGY-TQEEKIEIAHRHLIPKQLE-QHGLTPQQI-----QIPQVTTLDIITRY-------TREAGvrsl 520
Cdd:COG0714   156 AQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELlalqeLVRQVHVSEAVLDYivdlvraTREHP---- 230


                  ....*.
gi 1034596222 521 DRKLGA 526
Cdd:COG0714   231 DLRKGP 236
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 327-461 3.74e-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: 52.29  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 327 LCFVGPPGVGKTSVGRSVAK-TLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 404
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596222 405 KSLQGdpaaALLEVLDPEQNHNFTDHYLnVAFDLSQVLFIATANT----TATIPAALLDRM 461
Cdd:pfam07728  80 PDVLN----SLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
297-482 2.07e-07

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 52.19  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 297 NDHYAMEKLK---KRVLEYLAVRQL--KNNLKGP--ILcFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 369
Cdd:COG1223     2 DDVVGQEEAKkklKLIIKELRRRENlrKFGLWPPrkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 370 rrtYVGSMPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHnftdhylnva 435
Cdd:COG1223    75 ---YLGETARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSG---------- 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034596222 436 fdlsqVLFIATANTTATIPAALLDRM-EIIQVPGYTQEEKIEIAHRHL 482
Cdd:COG1223   136 -----SVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNL 178
aroK PRK00131
shikimate kinase; Reviewed
 322-352 1.89e-06

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 48.26  E-value: 1.89e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034596222 322 LKGPILCFVGPPGVGKTSVGRSVAKTLGREF 352
Cdd:PRK00131    2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 314-464 9.21e-06

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: 46.40  E-value: 9.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 314 AVRQLKNNLKGP-----ILCFVGPPGVGKTSVGRSVAKTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 386
Cdd:cd19499    26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 387 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATANttaTIPAAL 457
Cdd:cd19499   100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRTV-DFKNTIIIMTSN---HFRPEF 168


                  ....*..
gi 1034596222 458 LDRMEII 464
Cdd:cd19499   169 LNRIDEI 175
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 329-480 1.16e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.16  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 329 FVGPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 404
Cdd:PRK13342   41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 405 KSLQgDpaaALLEVLdpEQNHnftdhylnvafdlsqVLFIATanTTA----TIPAALLDRMEIIQVPGYTQEEKIEIAHR 480
Cdd:PRK13342  106 KAQQ-D---ALLPHV--EDGT---------------ITLIGA--TTEnpsfEVNPALLSRAQVFELKPLSEEDIEQLLKR 162
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 329-484 1.37e-05

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: 45.65  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 329 FVGPPGVGKTSVGRSVAKTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGV-NNP--VF 395
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVrRKPysIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 396 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHNFTDHY-LNVAFDlsQVLFIATANTTATIPaalLDRMEIIQVPGY--TQE 472
Cdd:pfam07724  80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQgRTVDFK--NTLFIMTGNFGSEKI---SDASRLGDSPDYelLKE 147

                         170
                  ....*....|..
gi 1034596222 473 EKIEIAHRHLIP 484
Cdd:pfam07724 148 EVMDLLKKGFIP 159
44 PHA02544
clamp loader, small subunit; Provisional
 325-478 1.41e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 47.29  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 325 PILCFVGP-PGVGKTSVGRSVAKTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGVNNPVFLLDEVDKL 403
Cdd:PHA02544   43 PNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTGGGKVIIIDEFDRL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 404 G-----KSLQGdpaaaLLEvldpeqnhnftdhylnvAFDlSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIA 478
Cdd:PHA02544  113 GladaqRHLRS-----FME-----------------AYS-KNCSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM 169
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 323-461 1.76e-05

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: 45.06  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222  323 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 393
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034596222  394 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPAALLDRM 461
Cdd:smart00382  81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRR 137
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 327-353 5.49e-05

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 43.96  E-value: 5.49e-05
                          10        20
                  ....*....|....*....|....*..
gi 1034596222 327 LCFVGPPGVGKTSVGRSVAKTLGREFH 353
Cdd:COG0703     1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 330-352 7.60e-05

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: 43.31  E-value: 7.60e-05
                          10        20
                  ....*....|....*....|...
gi 1034596222 330 VGPPGVGKTSVGRSVAKTLGREF 352
Cdd:cd00464     5 IGMMGAGKTTVGRLLAKALGLPF 27
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
248-346 1.04e-04

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 44.86  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 248 KEIKRLKKMPQSMpeyaLTRNYLELMVELPWNKSTTDRL-----DIRAARILLDN--DHYAMEKLKKRVLEYLAvRQLKN 320
Cdd:COG1419    81 RELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEKlpEDLSAEEAWRALLEALA-RRLPV 155

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034596222 321 NL-----KGPILCFVGPPGVGKTSvgrSVAK 346
Cdd:COG1419   156 AEdplldEGGVIALVGPTGVGKTT---TIAK 183
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 331-367 1.68e-04

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 44.28  E-value: 1.68e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034596222 331 GPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIR 367
Cdd:COG2256    56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR 91
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 329-448 4.21e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 43.29  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 329 FVGPPGVGKTSVGRSVAKTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 399
Cdd:PRK11034  493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034596222 400 VDKlgksLQGDPAAALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATAN 448
Cdd:PRK11034  566 IEK----AHPDVFNLLLQVMD---NGTLTDNNGRKA-DFRNVVLVMTTN 606
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 331-460 2.25e-03

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 38.69  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596222 331 GPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 400
Cdd:pfam07726   6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596222 401 DKLGKSLQgdpaAALLEVLdpeQNHNFTdhYLNVAFDLSQVLF-IATANT-----TATIPAALLDR 460
Cdd:pfam07726  72 NRAPPKTQ----SALLEAM---QERQVT--IDGETHPLPEPFFvLATQNPieqegTYPLPEAQLDR 128
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 322-369 4.16e-03

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 38.55  E-value: 4.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034596222 322 LKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIAlggVCDQSDIRGH 369
Cdd:COG4088     2 DSPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVA---LLHSDDFRRF 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH