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Conserved domains on  [gi|56693217|ref|NP_001008573|]
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lon protease homolog 2, peroxisomal [Danio rerio]

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
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, ...
1-823 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1003.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   1 MS-SNSGIQIPSRLPLLCTHDGVLLPGSTMRVSVDTARNMQLVKsRLLKGTSLkstiIGVIPnTRDPEHDSDELPSLHSI 79
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVA-QKDAEVEDPGPDDLYEV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  80 GTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDkleqytEGDPADGELGELSQRFYQAAVQLVg 159
Cdd:COG0466  75 GTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE------EEEEDDKELEALMRSLKEQFEEYV- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 160 MLDMSVP--VVAKLRRLLDSlpkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIEGLKLLQKTR-KLRP 236
Cdd:COG0466 146 KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 237 DDDKR----VL-----SIRK--GGVFPGRQfsldeevededsdDTALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMP 305
Cdd:COG0466 223 QMEKSqreyYLreqlkAIQKelGEKDDGED-------------EIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSA 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 306 EYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVG 385
Cdd:COG0466 290 EATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLG 369
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 386 RSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDP 465
Cdd:COG0466 370 KSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDP 449
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 466 EQNHSFTDHYLNVPFDLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQ 545
Cdd:COG0466 450 EQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISD 529
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 546 DTTLQIISKYTREAGVRSLERKIGAVCRAVAVKVAEGQKVsrseapteqhaeqntdskvedsgiaappemPIVIDHVALK 625
Cdd:COG0466 530 EALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK------------------------------KVTITPKNLE 579
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 626 DILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLND 705
Cdd:COG0466 580 KYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDP 659
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 706 gsaDLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKR 785
Cdd:COG0466 660 ---DFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKT 736
                       810       820       830
                ....*....|....*....|....*....|....*...
gi 56693217 786 IIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:COG0466 737 VILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
1-823 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1003.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   1 MS-SNSGIQIPSRLPLLCTHDGVLLPGSTMRVSVDTARNMQLVKsRLLKGTSLkstiIGVIPnTRDPEHDSDELPSLHSI 79
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVA-QKDAEVEDPGPDDLYEV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  80 GTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDkleqytEGDPADGELGELSQRFYQAAVQLVg 159
Cdd:COG0466  75 GTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE------EEEEDDKELEALMRSLKEQFEEYV- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 160 MLDMSVP--VVAKLRRLLDSlpkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIEGLKLLQKTR-KLRP 236
Cdd:COG0466 146 KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 237 DDDKR----VL-----SIRK--GGVFPGRQfsldeevededsdDTALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMP 305
Cdd:COG0466 223 QMEKSqreyYLreqlkAIQKelGEKDDGED-------------EIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSA 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 306 EYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVG 385
Cdd:COG0466 290 EATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLG 369
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 386 RSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDP 465
Cdd:COG0466 370 KSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDP 449
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 466 EQNHSFTDHYLNVPFDLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQ 545
Cdd:COG0466 450 EQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISD 529
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 546 DTTLQIISKYTREAGVRSLERKIGAVCRAVAVKVAEGQKVsrseapteqhaeqntdskvedsgiaappemPIVIDHVALK 625
Cdd:COG0466 530 EALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK------------------------------KVTITPKNLE 579
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 626 DILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLND 705
Cdd:COG0466 580 KYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDP 659
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 706 gsaDLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKR 785
Cdd:COG0466 660 ---DFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKT 736
                       810       820       830
                ....*....|....*....|....*....|....*...
gi 56693217 786 IIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:COG0466 737 VILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
14-823 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: 850.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    14 PLLCTHDGVLLPGSTMRVSVDTARNMQLVKsrllKGTSLKSTIIGVIpNTRDPEHDSDELPSLHSIGTAGLAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLF-LQKDDDNEEPEEDDIYSVGVVAQILEMLPLpS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    93 WPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEQytegDPADGELGELSQRFYQAAVQLVGMLDMSVPVVAKLR 172
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPF----DKDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   173 RLLDSLPKETLPDVLAAMIRTSNKEKLQ-VLDAVDLEERFKKALPLLTRQIEGLKLLQK-TRKLRPDDDKR--------- 241
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEKMEKTqreyylreq 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   242 VLSIRKG-GVFPGRQFSLdeevededsddtALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMPEYALTRNYLEMMVEL 320
Cdd:TIGR00763 232 LKAIKKElGIEKDDKDEL------------EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   321 PWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIA 400
Cdd:TIGR00763 300 PWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFS 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   401 LGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPF 480
Cdd:TIGR00763 380 LGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPF 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   481 DLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQDTTLQIISKYTREAG 560
Cdd:TIGR00763 460 DLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAG 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   561 VRSLERKIGAVCRAVAVKVAEGQKVSRSEApteqhaeqntdskvedsgiaappeMPIVIDHVALKDILGPPLFEMEVSER 640
Cdd:TIGR00763 540 VRNLERQIEKICRKAAVKLVEQGEKKKSEA------------------------ESVVITPDNLKKYLGKPVFTYERAYE 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   641 LTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLNDgsaDLLEGTDIHLHF 720
Cdd:TIGR00763 596 VTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP---NFFEKADIHLHV 672
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   721 PAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEKDLEEIP 800
Cdd:TIGR00763 673 PEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELP 752
                         810       820
                  ....*....|....*....|...
gi 56693217   801 ANVRADLDFVLAGTLDEVLNAAF 823
Cdd:TIGR00763 753 ENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
67-823 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 559.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   67 EHDSDE--LPSLHSIGTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEqytegdpADGELG 144
Cdd:PRK10787  57 EASTDEpgVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPT-------IDEREQ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  145 ELSQRfyQAAVQLVGMLDMSVPVVAKLRRLLDSLPKET-LPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIE 223
Cdd:PRK10787 128 EVLVR--TAISQFEGYIKLNKKIPPEVLTSLNSIDDPArLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEID 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  224 glkLLQKTRKLRpdddKRVlsiRKGGVFPGRQFSLDEEVEDEDSDDTAL---------LERKVKAAAMPEAALRVCLKEL 294
Cdd:PRK10787 206 ---LLQVEKRIR----NRV---KKQMEKSQREYYLNEQMKAIQKELGEMddapdeneaLKRKIDAAKMPKEAKEKAEAEL 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  295 RRLKKMPQSMPEYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFV 374
Cdd:PRK10787 276 QKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLV 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  375 GPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGD 454
Cdd:PRK10787 356 GPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGD 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  455 PAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATANTTaTIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQH 534
Cdd:PRK10787 436 PASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERN 514
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  535 GLTPQQLQIPQDTTLQIISKYTREAGVRSLERKIGAVCRAvAVKVAEGQKvsrseapTEQHAEQNTDSkvedsgiaappe 614
Cdd:PRK10787 515 ALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQLLLDK-------SLKHIEINGDN------------ 574
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  615 mpividhvaLKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWL 694
Cdd:PRK10787 575 ---------LHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVV 645
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  695 RSNAKTYLLNdgsADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDK 774
Cdd:PRK10787 646 RARAEKLGIN---PDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEK 722
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*....
gi 56693217  775 VLAAHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:PRK10787 723 LLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
332-513 5.75e-123

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: 367.65  E-value: 5.75e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 332 IRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATA 491
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                       170       180
                ....*....|....*....|..
gi 56693217 492 NTTATIPPALLDRMEVLQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
618-825 5.94e-95

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: 295.69  E-value: 5.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   618 VIDHVALKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSN 697
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   698 AKTYllnDGSADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLA 777
Cdd:pfam05362  81 AEEL---GIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 56693217   778 AHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAFDG 825
Cdd:pfam05362 158 AHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
367-505 7.13e-07

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: 49.68  E-value: 7.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    367 KGPILCFVGPPGVGKTSVGRSIARTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693217    438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHSFTDHYLNVPfdlsqvlFIATANTTATIPPALLDRM 505
Cdd:smart00382  81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLT-------VILTTNDEKDLGPALLRRR 137
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
1-823 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1003.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   1 MS-SNSGIQIPSRLPLLCTHDGVLLPGSTMRVSVDTARNMQLVKsRLLKGTSLkstiIGVIPnTRDPEHDSDELPSLHSI 79
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVA-QKDAEVEDPGPDDLYEV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  80 GTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDkleqytEGDPADGELGELSQRFYQAAVQLVg 159
Cdd:COG0466  75 GTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE------EEEEDDKELEALMRSLKEQFEEYV- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 160 MLDMSVP--VVAKLRRLLDSlpkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIEGLKLLQKTR-KLRP 236
Cdd:COG0466 146 KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 237 DDDKR----VL-----SIRK--GGVFPGRQfsldeevededsdDTALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMP 305
Cdd:COG0466 223 QMEKSqreyYLreqlkAIQKelGEKDDGED-------------EIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSA 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 306 EYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVG 385
Cdd:COG0466 290 EATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLG 369
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 386 RSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDP 465
Cdd:COG0466 370 KSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDP 449
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 466 EQNHSFTDHYLNVPFDLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQ 545
Cdd:COG0466 450 EQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISD 529
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 546 DTTLQIISKYTREAGVRSLERKIGAVCRAVAVKVAEGQKVsrseapteqhaeqntdskvedsgiaappemPIVIDHVALK 625
Cdd:COG0466 530 EALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK------------------------------KVTITPKNLE 579
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 626 DILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLND 705
Cdd:COG0466 580 KYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDP 659
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 706 gsaDLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKR 785
Cdd:COG0466 660 ---DFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKT 736
                       810       820       830
                ....*....|....*....|....*....|....*...
gi 56693217 786 IIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:COG0466 737 VILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
14-823 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: 850.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    14 PLLCTHDGVLLPGSTMRVSVDTARNMQLVKsrllKGTSLKSTIIGVIpNTRDPEHDSDELPSLHSIGTAGLAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLF-LQKDDDNEEPEEDDIYSVGVVAQILEMLPLpS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    93 WPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEQytegDPADGELGELSQRFYQAAVQLVGMLDMSVPVVAKLR 172
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPF----DKDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   173 RLLDSLPKETLPDVLAAMIRTSNKEKLQ-VLDAVDLEERFKKALPLLTRQIEGLKLLQK-TRKLRPDDDKR--------- 241
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEKMEKTqreyylreq 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   242 VLSIRKG-GVFPGRQFSLdeevededsddtALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMPEYALTRNYLEMMVEL 320
Cdd:TIGR00763 232 LKAIKKElGIEKDDKDEL------------EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   321 PWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIA 400
Cdd:TIGR00763 300 PWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFS 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   401 LGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPF 480
Cdd:TIGR00763 380 LGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPF 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   481 DLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQDTTLQIISKYTREAG 560
Cdd:TIGR00763 460 DLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAG 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   561 VRSLERKIGAVCRAVAVKVAEGQKVSRSEApteqhaeqntdskvedsgiaappeMPIVIDHVALKDILGPPLFEMEVSER 640
Cdd:TIGR00763 540 VRNLERQIEKICRKAAVKLVEQGEKKKSEA------------------------ESVVITPDNLKKYLGKPVFTYERAYE 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   641 LTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLNDgsaDLLEGTDIHLHF 720
Cdd:TIGR00763 596 VTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP---NFFEKADIHLHV 672
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   721 PAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEKDLEEIP 800
Cdd:TIGR00763 673 PEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELP 752
                         810       820
                  ....*....|....*....|...
gi 56693217   801 ANVRADLDFVLAGTLDEVLNAAF 823
Cdd:TIGR00763 753 ENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
67-823 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 559.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   67 EHDSDE--LPSLHSIGTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEqytegdpADGELG 144
Cdd:PRK10787  57 EASTDEpgVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPT-------IDEREQ 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  145 ELSQRfyQAAVQLVGMLDMSVPVVAKLRRLLDSLPKET-LPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIE 223
Cdd:PRK10787 128 EVLVR--TAISQFEGYIKLNKKIPPEVLTSLNSIDDPArLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEID 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  224 glkLLQKTRKLRpdddKRVlsiRKGGVFPGRQFSLDEEVEDEDSDDTAL---------LERKVKAAAMPEAALRVCLKEL 294
Cdd:PRK10787 206 ---LLQVEKRIR----NRV---KKQMEKSQREYYLNEQMKAIQKELGEMddapdeneaLKRKIDAAKMPKEAKEKAEAEL 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  295 RRLKKMPQSMPEYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFV 374
Cdd:PRK10787 276 QKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLV 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  375 GPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGD 454
Cdd:PRK10787 356 GPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGD 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  455 PAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATANTTaTIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQH 534
Cdd:PRK10787 436 PASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERN 514
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  535 GLTPQQLQIPQDTTLQIISKYTREAGVRSLERKIGAVCRAvAVKVAEGQKvsrseapTEQHAEQNTDSkvedsgiaappe 614
Cdd:PRK10787 515 ALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQLLLDK-------SLKHIEINGDN------------ 574
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  615 mpividhvaLKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWL 694
Cdd:PRK10787 575 ---------LHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVV 645
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  695 RSNAKTYLLNdgsADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDK 774
Cdd:PRK10787 646 RARAEKLGIN---PDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEK 722
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*....
gi 56693217  775 VLAAHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:PRK10787 723 LLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
332-513 5.75e-123

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: 367.65  E-value: 5.75e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 332 IRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATA 491
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                       170       180
                ....*....|....*....|..
gi 56693217 492 NTTATIPPALLDRMEVLQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
618-825 5.94e-95

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: 295.69  E-value: 5.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   618 VIDHVALKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSN 697
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   698 AKTYllnDGSADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLA 777
Cdd:pfam05362  81 AEEL---GIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 56693217   778 AHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAFDG 825
Cdd:pfam05362 158 AHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
13-220 1.29e-26

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: 107.81  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    13 LPLLCTHDGVLLPGSTMRVSVDTARNMQLVKSRLLKGtslKSTIIGVIPNtRDPEHDSDELPSLHSIGTAGLAVQVVGSn 92
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQ-KDAEDEEPTPDDLYEVGTVAKIVQILKL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    93 wPKPHYTLLITGLCRFRV-SQLLRERPFPVAEVEQLDkleqytegDPADGELGELSQRFYQAAVQLVGMLDMSVPVVAKL 171
Cdd:pfam02190  77 -PDGTYKVLVEGLERVRIvELVKKEEPYLRAEVEDLP--------EDSDELSEALKALVKELIEKLRRLLKLLLPLELLL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 56693217   172 RRLLDSLPkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTR 220
Cdd:pfam02190 148 KIKDIENP-GRLADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
371-513 3.67e-26

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 104.21  E-value: 3.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   371 LCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 449
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56693217   450 SLQG-------DPAAALLEVLDPEQNHSftdhylnvpfdlSQVLFIATANTTATIPPALLDRMEVLQVPGY 513
Cdd:pfam00004  72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
715-798 2.24e-15

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 75.79  E-value: 2.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 715 DIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEK 794
Cdd:COG1750  95 DVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAI 174

                ....
gi 56693217 795 DLEE 798
Cdd:COG1750 175 LTGY 178
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
349-504 5.33e-15

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 73.09  E-value: 5.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 349 LKKRVLEYLAVRQLKSTL------KGPILCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSdirghrRTYVGSMP 422
Cdd:cd19481   1 LKASLREAVEAPRRGSRLrryglgLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 423 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhsftdhylnvpfdLSQVLFIATANTT 494
Cdd:cd19481  75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139
                       170
                ....*....|
gi 56693217 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 6.12e-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: 74.56  E-value: 6.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 337 VLLDNdhyAMEKLKKRVLEYLAVRQLKSTLKGPI---LCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG0464 160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 414 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDPA-------AALLEVLDpeqnhsftdhylNVPFDlsqV 485
Cdd:COG0464 231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEVGDgvgrrvvNTLLTEME------------ELRSD---V 292
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 56693217 486 LFIATANTTATIPPALLDRM-EVLQVPGYTQEEKVEIAHRHLIPHQLE 532
Cdd:COG0464 293 VVIAATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD 340
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
352-506 3.05e-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: 62.16  E-value: 3.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 352 RVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTL---GREFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 428
Cdd:cd00009   3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693217 429 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhsfTDHYLNVPFDLSQVLFIATANTTATIPPALLDRME 506
Cdd:cd00009  79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLD 144
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
366-551 5.85e-11

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 64.42  E-value: 5.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 366 LKGPILcFVGPPGVGKTSVGRSIARTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 436
Cdd:COG0714  30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 437 ----PVF----LLDEVDKlgkslqGDPA--AALLEVLdpeQNHSFT----DHYLNVPFdlsqvLFIATANT-----TATI 497
Cdd:COG0714  88 frpgPLFanvlLADEINR------APPKtqSALLEAM---EERQVTipggTYKLPEPF-----LVIATQNPieqegTYPL 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56693217 498 PPALLDRMEV-LQVpGY-TQEEKVEIAHRHLIPHQLE-QHGLTPQQLQIPQDTTLQI 551
Cdd:COG0714 154 PEAQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELLALQELVRQV 209
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
371-505 5.54e-09

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: 55.38  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   371 LCFVGPPGVGKTSVGRSIA-RTLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 448
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56693217   449 KSLQGdpaaALLEVLDPEQNHSFTDHYLnVPFDLSQVLFIATANT----TATIPPALLDRM 505
Cdd:pfam07728  80 PDVLN----SLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
341-532 5.22e-08

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 54.89  E-value: 5.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 341 NDHYAMEKLK---KRVLEYLAVRQ-LKSTLKGP---ILcFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG1223   2 DDVVGQEEAKkklKLIIKELRRREnLRKFGLWPprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 414 rrtYVGSMPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHSftdhylnvp 479
Cdd:COG1223  75 ---YLGETARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSGS--------- 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 56693217 480 fdlsqvLFIATANTTATIPPALLDRM-EVLQVPGYTQEEKVEIAHRHLIPHQLE 532
Cdd:COG1223 137 ------VVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNLKKFPLP 184
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
367-505 7.13e-07

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: 49.68  E-value: 7.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217    367 KGPILCFVGPPGVGKTSVGRSIARTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693217    438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHSFTDHYLNVPfdlsqvlFIATANTTATIPPALLDRM 505
Cdd:smart00382  81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLT-------VILTTNDEKDLGPALLRRR 137
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
373-524 7.42e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 7.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  373 FVGPPGVGKTSVGRSIARTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 448
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  449 KSLQgDpaaALLEVLdpEQNHsftdhylnvpfdlsqVLFIATanTTA----TIPPALLDRMEVLQVPGYTQEEKVEIAHR 524
Cdd:PRK13342 106 KAQQ-D---ALLPHV--EDGT---------------ITLIGA--TTEnpsfEVNPALLSRAQVFELKPLSEEDIEQLLKR 162
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
358-506 1.22e-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: 49.48  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 358 AVRQLKSTLKGP-----ILCFVGPPGVGKTSVGRSIARTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 430
Cdd:cd19499  26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 431 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHSFTDHYLNVpFDLSQVLFIATANttaTIPPAL 501
Cdd:cd19499 100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSN---HFRPEF 168

                ....*
gi 56693217 502 LDRME 506
Cdd:cd19499 169 LNRID 173
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
375-552 6.89e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 49.28  E-value: 6.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 375 GPPGVGKTSVGRSIARTLGREFHRI--ALGGVcdqSDIR------GHRRTYvgsmpgriinGLKTVgvnnpVFlLDEVDK 446
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIRevieeaRERRAY----------GRRTI-----LF-VDEIHR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 447 LGKSLQgDpaaALLEVLdpEQNHsftdhylnvpfdlsqVLFIA--TANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHR 524
Cdd:COG2256 117 FNKAQQ-D---ALLPHV--EDGT---------------ITLIGatTENPSFEVNSALLSRCRVFVLKPLSEEDLEQLLER 175
                       170       180
                ....*....|....*....|....*...
gi 56693217 525 HLiphQLEQHGLTPQQLQIPQDTTLQII 552
Cdd:COG2256 176 AL---ADDERGLGGYKLELDDEALEALA 200
44 PHA02544
clamp loader, small subunit; Provisional
363-522 8.05e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 48.83  E-value: 8.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  363 KSTLKG-------PILCFVGP-PGVGKTSVGRSIARTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGV 434
Cdd:PHA02544  30 KETFKSivkkgriPNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  435 NNPVFLLDEVDKLGkslqgdpaaaLLEVldpeQNH--SFTDHYlnvpfdLSQVLFIATANTTATIPPALLDRMEVLQVPG 512
Cdd:PHA02544 100 GGKVIIIDEFDRLG----------LADA----QRHlrSFMEAY------SKNCSFIITANNKNGIIEPLRSRCRVIDFGV 159
                        170
                 ....*....|
gi 56693217  513 YTQEEKVEIA 522
Cdd:PHA02544 160 PTKEEQIEMM 169
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
373-528 8.61e-06

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: 46.80  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   373 FVGPPGVGKTSVGRSIARTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGV-NNP--VF 439
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVrRKPysIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   440 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHSFTDHYlNVPFDLSQVLFIATANTTATIPpalLDRMEVLQVPGY--TQEE 517
Cdd:pfam07724  80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNFGSEKI---SDASRLGDSPDYelLKEE 148
                         170
                  ....*....|.
gi 56693217   518 KVEIAHRHLIP 528
Cdd:pfam07724 149 VMDLLKKGFIP 159
aroK PRK00131
shikimate kinase; Reviewed
366-396 9.44e-06

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 46.72  E-value: 9.44e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 56693217  366 LKGPILCFVGPPGVGKTSVGRSIARTLGREF 396
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
729-821 1.41e-05

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 48.27  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 729 GPSAGvTIVTcLA--------SLLSGRlvrsDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEKDLEEip 800
Cdd:COG3480 240 GPSAG-LMFA-LGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAVG-- 311
                        90       100
                ....*....|....*....|.
gi 56693217 801 aNVRADLDFVLAGTLDEVLNA 821
Cdd:COG3480 312 -TIPTGLKVVPVDTLDDALDA 331
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
371-397 8.55e-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: 8.55e-05
                        10        20
                ....*....|....*....|....*..
gi 56693217 371 LCFVGPPGVGKTSVGRSIARTLGREFH 397
Cdd:COG0703   1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
374-396 2.17e-04

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: 42.54  E-value: 2.17e-04
                        10        20
                ....*....|....*....|...
gi 56693217 374 VGPPGVGKTSVGRSIARTLGREF 396
Cdd:cd00464   5 IGMMGAGKTTVGRLLAKALGLPF 27
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
291-382 6.52e-04

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 42.93  E-value: 6.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 291 LKELRRLKKMPQSMpeyaLTRNYLEMMVELPWSKSTTDCL-----DIRAARVLLD------NDHYAMEKLKKRVLEYLAV 359
Cdd:COG1419  80 RRELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEklpedlSAEEAWRALLEALARRLPV 155
                        90       100
                ....*....|....*....|...
gi 56693217 360 RQLKSTLKGPILCFVGPPGVGKT 382
Cdd:COG1419 156 AEDPLLDEGGVIALVGPTGVGKT 178
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
375-504 1.31e-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: 39.46  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217   375 GPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 444
Cdd:pfam07726   6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56693217   445 DKLGKSLQgdpaAALLEVLdpeQNHSFTdhYLNVPFDLSQVLF-IATANT-----TATIPPALLDR 504
Cdd:pfam07726  72 NRAPPKTQ----SALLEAM---QERQVT--IDGETHPLPEPFFvLATQNPieqegTYPLPEAQLDR 128
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
728-796 2.76e-03

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 41.47  E-value: 2.76e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693217 728 DGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKV-----LAAHRaNLKR---IIIPKRNEKDL 796
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLTGkqgVIIPAANVKNL 667
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
373-492 3.12e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 41.36  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  373 FVGPPGVGKTSVGRSIARTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 443
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 56693217  444 VDKlgksLQGDPAAALLEVLDpeqNHSFTDHYlNVPFDLSQVLFIATAN 492
Cdd:PRK11034 566 IEK----AHPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 606
PRK13341 PRK13341
AAA family ATPase;
371-460 3.74e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217  371 LCFVGPPGVGKTSVGRSIARTLGREFHRI--ALGGVcdqSDIR------GHRRTYvgsmpgriiNGLKTvgvnnpVFLLD 442
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIANHTRAHFSSLnaVLAGV---KDLRaevdraKERLER---------HGKRT------ILFID 116
                         90
                 ....*....|....*...
gi 56693217  443 EVDKLGKSLQgdpaAALL 460
Cdd:PRK13341 117 EVHRFNKAQQ----DALL 130
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
366-413 5.03e-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: 5.03e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 56693217 366 LKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIAlggVCDQSDIRGH 413
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.
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