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Conserved domains on  [gi|13385298|ref|NP_080103|]
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lon protease homolog 2, peroxisomal isoform 1 [Mus musculus]

Protein Classification

endopeptidase La( domain architecture ID 11422032)

endopeptidase La is an ATP-dependent serine protease that degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long; it binds to DNA in a double-stranded, site-specific manner

CATH:  1.10.8.60
EC:  3.4.21.53
Gene Ontology:  GO:0005524|GO:0016887|GO:0004176|GO:0004252|GO:0043565
MEROPS:  S16
PubMed:  34563541|9115177

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 1-835 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 979.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   1 MS-SVSPIQIPSRLPLLLTHESVLLPGSTMRTSVDTARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDtqDLpp 75
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPD--DL-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  76 lHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEqldRLEEFPNICKSREELGE-LSEQFYRYA 154
Cdd:COG0466  72 -YEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVE---PLEEEEEDDKELEALMRsLKEQFEEYV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 155 vqlvemldmsvpavaklrRLLDNLPREA------------LPDILTSIIRTSNKEKLQILDAVSLEDRFKMTIPLLVRQI 222
Cdd:COG0466 146 ------------------KLNPKIPPELlaalsniedpgrLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEI 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 223 EGLKLLQKTR-KPKQDDDKR---------VIAIR-----------PIRRiphipgtledeeeeednddivmLEKKIRTSS 281
Cdd:COG0466 208 EVLELEKKIRsRVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAK 265

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 282 MPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKRRVLEYLAVRQ 361
Cdd:COG0466 266 LPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRK 345

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 362 LKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLL 441
Cdd:COG0466 346 LKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLL 425

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 442 DEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPPALLDRMEIIQVPGYTQEEKIEI 521
Cdd:COG0466 426 DEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEI 505

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 522 AHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRKFGAICRAVAVKVAEGQHKeakldrsdvadgegck 601
Cdd:COG0466 506 AKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK---------------- 569

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 602 ehvledakpesisdtadlalppemPILIDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEG 681
Cdd:COG0466 570 ------------------------KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKG 625

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 682 QLTLTGQLGDVMKESAHLAISWLRSNAKKYHLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLV 761
Cdd:COG0466 626 KLTLTGQLGDVMKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPV 700

                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13385298 762 RSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLNAAF 835
Cdd:COG0466 701 RSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 1-835 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 979.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   1 MS-SVSPIQIPSRLPLLLTHESVLLPGSTMRTSVDTARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDtqDLpp 75
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPD--DL-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  76 lHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEqldRLEEFPNICKSREELGE-LSEQFYRYA 154
Cdd:COG0466  72 -YEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVE---PLEEEEEDDKELEALMRsLKEQFEEYV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 155 vqlvemldmsvpavaklrRLLDNLPREA------------LPDILTSIIRTSNKEKLQILDAVSLEDRFKMTIPLLVRQI 222
Cdd:COG0466 146 ------------------KLNPKIPPELlaalsniedpgrLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEI 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 223 EGLKLLQKTR-KPKQDDDKR---------VIAIR-----------PIRRiphipgtledeeeeednddivmLEKKIRTSS 281
Cdd:COG0466 208 EVLELEKKIRsRVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAK 265

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 282 MPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKRRVLEYLAVRQ 361
Cdd:COG0466 266 LPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRK 345

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 362 LKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLL 441
Cdd:COG0466 346 LKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLL 425

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 442 DEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPPALLDRMEIIQVPGYTQEEKIEI 521
Cdd:COG0466 426 DEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEI 505

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 522 AHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRKFGAICRAVAVKVAEGQHKeakldrsdvadgegck 601
Cdd:COG0466 506 AKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK---------------- 569

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 602 ehvledakpesisdtadlalppemPILIDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEG 681
Cdd:COG0466 570 ------------------------KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKG 625

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 682 QLTLTGQLGDVMKESAHLAISWLRSNAKKYHLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLV 761
Cdd:COG0466 626 KLTLTGQLGDVMKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPV 700

                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13385298 762 RSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLNAAF 835
Cdd:COG0466 701 RSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 14-835 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: 810.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    14 PLLLTHESVLLPGSTMRTSVDTARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDTQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    93 WPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEQLDRlEEFPnicKSREELGELSEQFYRYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKE-EPFD---KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   173 RLLDNLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEDRFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   248 IRRIPHIPGTledeeEEEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   328 DRLDIRAARILLDNDHYAMEKLKRRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   488 IATANTTATIPPALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   568 FGAICRAVAVKVAEGQHKEAkldrsdvadgegckehvledAKPESISDTADLalppempilidshaLKDILGPPLYELEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   648 SERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYHLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747

                         810       820
                  ....*....|....*....|....*...
gi 13385298   808 LEEIPSNVRQDLSFVTASCLDEVLNAAF 835
Cdd:TIGR00763 748 LEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 273-835 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 540.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  273 LEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKRR 352
Cdd:PRK10787 254 LKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDR 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  353 VLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV 432
Cdd:PRK10787 334 ILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKV 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  433 GVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPPALLDRMEIIQVPG 512
Cdd:PRK10787 414 GVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSG 492

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  513 YTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRKFGAICRAVAvkvaegqhKEAKLDRS 592
Cdd:PRK10787 493 YTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV--------KQLLLDKS 564

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  593 dvadgegcKEHvledakpesisdtadlalppempILIDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFV 672
Cdd:PRK10787 565 --------LKH-----------------------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTI 613

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  673 EASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYHLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCL 752
Cdd:PRK10787 614 ETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTAL 688

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  753 ASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLN 832
Cdd:PRK10787 689 VSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLT 768


                 ...
gi 13385298  833 AAF 835
Cdd:PRK10787 769 LAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 332-513 6.42e-121

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 362.65  E-value: 6.42e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 332 IRAARILLDNDHYAMEKLKRRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 13385298 492 NTTATIPPALLDRMEIIQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 629-837 5.37e-97

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: 301.46  E-value: 5.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   629 IDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNA 708
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   709 KKYHLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVL 788
Cdd:pfam05362  82 EELGI-----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 13385298   789 AAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLNAAFDG 837
Cdd:pfam05362 157 AAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 367-505 9.51e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 9.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13385298    438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPPALLDRM 505
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, ...
 1-835 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 979.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   1 MS-SVSPIQIPSRLPLLLTHESVLLPGSTMRTSVDTARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDtqDLpp 75
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPD--DL-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  76 lHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEqldRLEEFPNICKSREELGE-LSEQFYRYA 154
Cdd:COG0466  72 -YEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVE---PLEEEEEDDKELEALMRsLKEQFEEYV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 155 vqlvemldmsvpavaklrRLLDNLPREA------------LPDILTSIIRTSNKEKLQILDAVSLEDRFKMTIPLLVRQI 222
Cdd:COG0466 146 ------------------KLNPKIPPELlaalsniedpgrLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEI 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 223 EGLKLLQKTR-KPKQDDDKR---------VIAIR-----------PIRRiphipgtledeeeeednddivmLEKKIRTSS 281
Cdd:COG0466 208 EVLELEKKIRsRVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAK 265

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 282 MPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKRRVLEYLAVRQ 361
Cdd:COG0466 266 LPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRK 345

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 362 LKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLL 441
Cdd:COG0466 346 LKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLL 425

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 442 DEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPPALLDRMEIIQVPGYTQEEKIEI 521
Cdd:COG0466 426 DEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEI 505

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 522 AHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRKFGAICRAVAVKVAEGQHKeakldrsdvadgegck 601
Cdd:COG0466 506 AKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK---------------- 569

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 602 ehvledakpesisdtadlalppemPILIDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEG 681
Cdd:COG0466 570 ------------------------KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKG 625

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 682 QLTLTGQLGDVMKESAHLAISWLRSNAKKYHLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLV 761
Cdd:COG0466 626 KLTLTGQLGDVMKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPV 700

                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13385298 762 RSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLNAAF 835
Cdd:COG0466 701 RSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 14-835 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: 810.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    14 PLLLTHESVLLPGSTMRTSVDTARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDTQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    93 WPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEQLDRlEEFPnicKSREELGELSEQFYRYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKE-EPFD---KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   173 RLLDNLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEDRFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   248 IRRIPHIPGTledeeEEEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   328 DRLDIRAARILLDNDHYAMEKLKRRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   488 IATANTTATIPPALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   568 FGAICRAVAVKVAEGQHKEAkldrsdvadgegckehvledAKPESISDTADLalppempilidshaLKDILGPPLYELEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   648 SERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYHLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747

                         810       820
                  ....*....|....*....|....*...
gi 13385298   808 LEEIPSNVRQDLSFVTASCLDEVLNAAF 835
Cdd:TIGR00763 748 LEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 273-835 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 540.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  273 LEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKRR 352
Cdd:PRK10787 254 LKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDR 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  353 VLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV 432
Cdd:PRK10787 334 ILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKV 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  433 GVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPPALLDRMEIIQVPG 512
Cdd:PRK10787 414 GVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSG 492

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  513 YTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRKFGAICRAVAvkvaegqhKEAKLDRS 592
Cdd:PRK10787 493 YTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV--------KQLLLDKS 564

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  593 dvadgegcKEHvledakpesisdtadlalppempILIDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFV 672
Cdd:PRK10787 565 --------LKH-----------------------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTI 613

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  673 EASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYHLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCL 752
Cdd:PRK10787 614 ETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTAL 688

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  753 ASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLN 832
Cdd:PRK10787 689 VSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLT 768


                 ...
gi 13385298  833 AAF 835
Cdd:PRK10787 769 LAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 332-513 6.42e-121

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 362.65  E-value: 6.42e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 332 IRAARILLDNDHYAMEKLKRRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 13385298 492 NTTATIPPALLDRMEIIQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 629-837 5.37e-97

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: 301.46  E-value: 5.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   629 IDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNA 708
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   709 KKYHLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVL 788
Cdd:pfam05362  82 EELGI-----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 13385298   789 AAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLNAAFDG 837
Cdd:pfam05362 157 AAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 13-220 4.22e-27

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: 109.35  E-value: 4.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    13 LPLLLTHESVLLPGSTMRTSVDTARNLQLVRSRLLKGtslQSTILGVIPNTpDPASDTQDLPPLHRIGTAALAVQVVGSn 92
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQK-DAEDEEPTPDDLYEVGTVAKIVQILKL- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    93 wPKPHYTLLITGLCRFQIVQVL-KEKPYPVAEVEQLDrleefpnicKSREELGELSEQFYRYAVQ-LVEMLDMSVPAVAK 170
Cdd:pfam02190  77 -PDGTYKVLVEGLERVRIVELVkKEEPYLRAEVEDLP---------EDSDELSEALKALVKELIEkLRRLLKLLLPLELL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 13385298   171 LRRLLDNLPrEALPDILTSIIRTSNKEKLQILDAVSLEDRFKMTIPLLVR 220
Cdd:pfam02190 147 LKIKDIENP-GRLADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 371-513 5.11e-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: 106.52  E-value: 5.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   371 LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 449
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385298   450 SLQG-------DPAAALLEVLDPEQNHNftdhylnvafdlSQVLFIATANTTATIPPALLDRMEIIQVPGY 513
Cdd:pfam00004  72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
723-810 1.02e-15

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 76.94  E-value: 1.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 723 LDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQ 802
Cdd:COG1750  91 LSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPK 170


                ....*...
gi 13385298 803 RNEKDLEE 810
Cdd:COG1750 171 GQAILTGY 178
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 345-504 2.58e-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: 2.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 345 AMEKLKRRVLEYLAVRQL--KNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSdirghrRTYVGSMP 422
Cdd:cd19481   1 LKASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 423 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhnftdhylnvafdLSQVLFIATANTT 494
Cdd:cd19481  75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139

                       170
                ....*....|
gi 13385298 495 ATIPPALLDR 504
Cdd:cd19481 140 DLLDPALLRP 149
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 337-532 3.62e-15

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: 78.41  E-value: 3.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 337 ILLDNdhyAMEKLKRRVLEYLAVRQLKNNLKGPI---LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG0464 160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 414 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDpaaallevldpeqnhnfTDHYLNVAFD---------LS 483
Cdd:COG0464 231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEV-----------------GDGVGRRVVNtlltemeelRS 290

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13385298 484 QVLFIATANTTATIPPALLDRM-EIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0464 291 DVVVIAATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD 340
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 352-513 1.51e-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: 62.93  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 352 RVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTL---GREFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 428
Cdd:cd00009   3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 429 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhnfTDHYLNVAFDLSQVLFIATANTTATIPPALLDRMEII 508
Cdd:cd00009  79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146


                ....*
gi 13385298 509 QVPGY 513
Cdd:cd00009 147 IVIPL 151
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 366-546 3.51e-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: 59.03  E-value: 3.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 366 LKGPILcFVGPPGVGKTSVGRSVAKTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 436
Cdd:COG0714  30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 437 ----PVF----LLDEVDKlgkslqGDPA--AALLEVLdpeQNHNFT-DhylNVAFDLSQVLF-IATANT-----TATIPP 499
Cdd:COG0714  88 frpgPLFanvlLADEINR------APPKtqSALLEAM---EERQVTiP---GGTYKLPEPFLvIATQNPieqegTYPLPE 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13385298 500 ALLDRMEI-IQVpGY-TQEEKIEIAHRHLIPKQLE-QHGLTPQQIQIPQH 546
Cdd:COG0714 156 AQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELLALQE 204
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 371-505 2.82e-08

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 53.07  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   371 LCFVGPPGVGKTSVGRSVAK-TLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 448
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385298   449 KSLQGdpaaALLEVLDPEQNHNFTDHYLnVAFDLSQVLFIATANT----TATIPPALLDRM 505
Cdd:pfam07728  80 PDVLN----SLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
345-526 5.41e-08

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 54.89  E-value: 5.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 345 AMEKLKRrVLEYLAVRQL--KNNLKGP--ILcFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirghrrtYVGS 420
Cdd:COG1223  10 AKKKLKL-IIKELRRRENlrKFGLWPPrkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 421 MPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHnftdhylnvafdlsqVL 486
Cdd:COG1223  79 TARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSG---------------SV 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 13385298 487 FIATANTTATIPPALLDRM-EIIQVPGYTQEEKIEIAHRHL 526
Cdd:COG1223 138 VIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNL 178
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 358-508 1.01e-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: 49.87  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 358 AVRQLKNNLKGP-----ILCFVGPPGVGKTSVGRSVAKTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 430
Cdd:cd19499  26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 431 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATANttaTIPPAL 501
Cdd:cd19499 100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRTV-DFKNTIIIMTSN---HFRPEF 168


                ....*..
gi 13385298 502 LDRMEII 508
Cdd:cd19499 169 LNRIDEI 175
aroK PRK00131
shikimate kinase; Reviewed
 366-396 2.35e-06

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 48.65  E-value: 2.35e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 13385298  366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREF 396
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
44 PHA02544
clamp loader, small subunit; Provisional
 369-522 3.72e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 49.60  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  369 PILCFVGP-PGVGKTSVGRSVAKTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGVNNPVFLLDEVDKL 447
Cdd:PHA02544  43 PNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTGGGKVIIIDEFDRL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  448 G-----KSLQGdpaaaLLEvldpeqnhnftdhylnvAFDlSQVLFIATANTTATIPPALLDRMEIIQVPGYTQEEKIEIA 522
Cdd:PHA02544 113 GladaqRHLRS-----FME-----------------AYS-KNCSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM 169
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 373-524 7.78e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.31  E-value: 7.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  373 FVGPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 448
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  449 KSLQgDpaaALLEVLdpEQNHnftdhylnvafdlsqVLFIATanTTA----TIPPALLDRMEIIQVPGYTQEEKIEIAHR 524
Cdd:PRK13342 106 KAQQ-D---ALLPHV--EDGT---------------ITLIGA--TTEnpsfEVNPALLSRAQVFELKPLSEEDIEQLLKR 162
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 321-596 7.84e-06

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 49.46  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   321 PWNKSTT--------DRLDIRAARILLD-----NDHYAMEKLKRRVLEY-----LAVRQLKNNLKGPI----LCFVGPPG 378
Cdd:TIGR03922 243 PWDPSSApsraefvdPAAAERKAKLLAEaeaelAEQIGLERVKRQVAALksstaMALARAERGLPVAQtsnhMLFAGPPG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   379 VGKTSVGRSVAKTLGrefhriALGGVCDQSDIRGHRRTYVGSMPGRiiNGLKTV----GVNNPVFLLDEVDKLGKSL--Q 452
Cdd:TIGR03922 323 TGKTTIARVVAKIYC------GLGVLRKPLVREVSRADLIGQYIGE--SEAKTNeiidSALGGVLFLDEAYTLVETGygQ 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   453 GDP--AAALLEVLDPEQNHNFTDHYLNVAF--DLSQVLfiatanttaTIPPALLDRM-EIIQVPGYTQEEKIEIAHRHLI 527
Cdd:TIGR03922 395 KDPfgLEAIDTLLARMENDRDRLVVIGAGYrkDLDKFL---------EVNEGLRSRFtRVIEFPSYSPDELVEIARRMAT 465

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13385298   528 PKQ--LEQhglTPQQIQIPQHTTLAIITRYTrEAGV--RSLD-RKFGAICRAVaVKVAEgQHKEAKLDRSDVAD 596
Cdd:TIGR03922 466 ERDsvLDD---AAADALLEAATTLAQDTTPD-ANGDlrRGLDiAGNGRFVRNV-VERAE-EERDFRLDHSDRLD 533
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 367-505 9.51e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 9.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298    367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13385298    438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPPALLDRM 505
Cdd:smart00382  81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRR 137
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 373-528 1.54e-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: 46.03  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   373 FVGPPGVGKTSVGRSVAKTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGVN-NP--VF 439
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVRrKPysIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   440 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHNFTDHY-LNVAFDlsQVLFIATANTTATIPpalLDRMEIIQVPGY--TQE 516
Cdd:pfam07724  80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQgRTVDFK--NTLFIMTGNFGSEKI---SDASRLGDSPDYelLKE 147

                         170
                  ....*....|..
gi 13385298   517 EKIEIAHRHLIP 528
Cdd:pfam07724 148 EVMDLLKKGFIP 159
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
741-833 7.22e-05

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 45.96  E-value: 7.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 741 GPSAGvTIVTcLA--------SLFSGRlvrsDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEip 812
Cdd:COG3480 240 GPSAG-LMFA-LGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAVG-- 311

                        90       100
                ....*....|....*....|.
gi 13385298 813 sNVRQDLSFVTASCLDEVLNA 833
Cdd:COG3480 312 -TIPTGLKVVPVDTLDDALDA 331
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 371-397 7.33e-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: 7.33e-05
                        10        20
                ....*....|....*....|....*..
gi 13385298 371 LCFVGPPGVGKTSVGRSVAKTLGREFH 397
Cdd:COG0703   1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
292-390 8.10e-05

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 45.63  E-value: 8.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 292 KEIKRLKKMPQSMpeyaLTRNYLELMVELPWNKSTTDRL-----DIRAARILLDN--DHYAMEKLKRRVLEYLAvRQLKN 364
Cdd:COG1419  81 RELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEKlpEDLSAEEAWRALLEALA-RRLPV 155

                        90       100       110
                ....*....|....*....|....*....|.
gi 13385298 365 NL-----KGPILCFVGPPGVGKTSvgrSVAK 390
Cdd:COG1419 156 AEdplldEGGVIALVGPTGVGKTT---TIAK 183
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 374-396 9.35e-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: 9.35e-05
                        10        20
                ....*....|....*....|...
gi 13385298 374 VGPPGVGKTSVGRSVAKTLGREF 396
Cdd:cd00464   5 IGMMGAGKTTVGRLLAKALGLPF 27
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 375-543 2.55e-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: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 375 GPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIR------GHRRTYvgsmpgriinGLKTVgvnnpVFlLDEVDK 446
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIRevieeaRERRAY----------GRRTI-----LF-VDEIHR 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 447 LGKSLQgDpaaALLEVLdpEQNHnftdhylnvafdlsqVLFIA--TANTTATIPPALLDRMEIIQVPGYTQEEKIEIAHR 524
Cdd:COG2256 117 FNKAQQ-D---ALLPHV--EDGT---------------ITLIGatTENPSFEVNSALLSRCRVFVLKPLSEEDLEQLLER 175

                       170
                ....*....|....*....
gi 13385298 525 HLipkQLEQHGLTPQQIQI 543
Cdd:COG2256 176 AL---ADDERGLGGYKLEL 191
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 740-843 3.60e-04

Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 44.17  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298 740 DGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKV-----LAAHRaGL--KQ-IIIPQRNEKDLeei 811
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLtgKQgVIIPAANVKNL--- 667

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13385298 812 psnvrqdlsfvtasCL-DEVLNAAFDGGF---PVKT 843
Cdd:COG1067 668 --------------MLrDEVVEAVKAGQFhiyAVEH 689
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 373-492 6.17e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 43.67  E-value: 6.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  373 FVGPPGVGKTSVGRSVAKTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 443
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 13385298  444 VDKlgksLQGDPAAALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATAN 492
Cdd:PRK11034 566 IEK----AHPDVFNLLLQVMD---NGTLTDNNGRKA-DFRNVVLVMTTN 606
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 375-504 2.90e-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: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298   375 GPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 444
Cdd:pfam07726   6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13385298   445 DKLGKSLQgdpaAALLEVLdpeQNHNFTdhYLNVAFDLSQVLF-IATANT-----TATIPPALLDR 504
Cdd:pfam07726  72 NRAPPKTQ----SALLEAM---QERQVT--IDGETHPLPEPFFvLATQNPieqegTYPLPEAQLDR 128
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 366-413 4.79e-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: 38.94  E-value: 4.79e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 13385298 366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIAlggVCDQSDIRGH 413
Cdd:COG4088   2 DSPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVA---LLHSDDFRRF 46
flhF PRK05703
flagellar biosynthesis protein FlhF;
229-390 7.51e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 39.49  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  229 QKTRKPKQDDD--KRVIAIRPIRRIPHIPGTLEDEEEEEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSM-- 304
Cdd:PRK05703  65 EEKRKPAKSILslQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELDELRDELKELkn 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385298  305 ----------------PEYALTRNYLELMvELpwNKSTTDRLdiraARILLDNDHYAMEKLKRRVLEYLAvRQLKNNLK- 367
Cdd:PRK05703 145 lledqlsglrqveripPEFAELYKRLKRS-GL--SPEIAEKL----LKLLLEHMPPRERTAWRYLLELLA-NMIPVRVEd 216

                        170       180
                 ....*....|....*....|....*..
gi 13385298  368 ----GPILCFVGPPGVGKTSvgrSVAK 390
Cdd:PRK05703 217 ilkqGGVVALVGPTGVGKTT---TLAK 240
 
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.
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