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Conserved domains on  [gi|493924021|ref|WP_006868924|]
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endopeptidase La [Gordonia namibiensis]

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, ...
7-767 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1046.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   7 LPVLFVPDVVVLPGMVVPIPL-DDAAQATVDAARASESGKLLVA--------PRLDDRYpTYGVVASIVQVGRIPGGGLA 77
Cdd:COG0466   14 LPLLPLRDVVVFPGMVIPLFVgREKSIKALEEAMEGDKLIGLVAqkdaevedPGPDDLY-EVGTVAKILQLLKLPDGTVK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  78 AVVKGEKRAQIGTGTPGHGAaLWVEATEVEDQEVTDE-----VRTLAGEYKKLVlaMLQRREAWQLIDAVNKMSDPSNLA 152
Cdd:COG0466   93 VLVEGLQRARIKEFVQEEPY-LEAEVEPLEEEEEDDKelealMRSLKEQFEEYV--KLNPKIPPELLAALSNIEDPGRLA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 153 DTSGYASWLTDEQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKELGEDEP 232
Cdd:COG0466  170 DFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 233 EGAD--DYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREILDADHHG 310
Cdd:COG0466  250 GEDEieELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYG 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 311 LDDVKDRIVEYLAVRARRAErglqvvggrGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRGHRRT 390
Cdd:COG0466  330 LEKVKERILEYLAVRKLKKK---------LKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 391 YVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRdhyldldldlsdvlflATANVIEN 470
Cdd:COG0466  401 YIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSdhylevpfdlskvmfiATANSLDT 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 471 IPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAKALRKAA 550
Cdd:COG0466  481 IPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 551 TNLAQGTATaPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGDVMKE 630
Cdd:COG0466  561 KKIAEGKKK-KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKE 639
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 631 SAQIALSYVRAHAEQLGVDPELLNRT-IHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGRVLPI 709
Cdd:COG0466  640 SAQAALSYVRSRAEELGIDPDFFEKYdIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPI 719
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493924021 710 GGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALEPA 767
Cdd:COG0466  720 GGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
7-767 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1046.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   7 LPVLFVPDVVVLPGMVVPIPL-DDAAQATVDAARASESGKLLVA--------PRLDDRYpTYGVVASIVQVGRIPGGGLA 77
Cdd:COG0466   14 LPLLPLRDVVVFPGMVIPLFVgREKSIKALEEAMEGDKLIGLVAqkdaevedPGPDDLY-EVGTVAKILQLLKLPDGTVK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  78 AVVKGEKRAQIGTGTPGHGAaLWVEATEVEDQEVTDE-----VRTLAGEYKKLVlaMLQRREAWQLIDAVNKMSDPSNLA 152
Cdd:COG0466   93 VLVEGLQRARIKEFVQEEPY-LEAEVEPLEEEEEDDKelealMRSLKEQFEEYV--KLNPKIPPELLAALSNIEDPGRLA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 153 DTSGYASWLTDEQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKELGEDEP 232
Cdd:COG0466  170 DFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 233 EGAD--DYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREILDADHHG 310
Cdd:COG0466  250 GEDEieELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYG 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 311 LDDVKDRIVEYLAVRARRAErglqvvggrGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRGHRRT 390
Cdd:COG0466  330 LEKVKERILEYLAVRKLKKK---------LKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 391 YVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRdhyldldldlsdvlflATANVIEN 470
Cdd:COG0466  401 YIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSdhylevpfdlskvmfiATANSLDT 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 471 IPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAKALRKAA 550
Cdd:COG0466  481 IPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 551 TNLAQGTATaPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGDVMKE 630
Cdd:COG0466  561 KKIAEGKKK-KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKE 639
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 631 SAQIALSYVRAHAEQLGVDPELLNRT-IHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGRVLPI 709
Cdd:COG0466  640 SAQAALSYVRSRAEELGIDPDFFEKYdIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPI 719
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493924021 710 GGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALEPA 767
Cdd:COG0466  720 GGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
8-764 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: 825.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021    8 PVLFVPDVVVLPGMVVPIPL-DDAAQATVDAARASESGKLLVA---------PRLDDRYPTyGVVASIVQ---VGRIPGG 74
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVgREKSIKLIKEALRLKQPYLGLFlqkdddneePEEDDIYSV-GVVAQILEmlpLPSSGTA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   75 GLAAVVKGEKRAQIGTGTPGHGAaLWVEATEVEDQEV---TDEVRTLAGEYKKLVLAMLQRREAWQ----LIDAVNKMSD 147
Cdd:TIGR00763  80 TYKVVVEGLRRIRIKELSDKGGY-LVVRVDNLKEEPFdkdDEEIKALTREIKETFRELISLSKLFReqpaLLSALEDIDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  148 PSNLADTSGYASWLTD-EQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKE 226
Cdd:TIGR00763 159 PGRLADFVAASLQLKEkDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  227 LGE--DEPEGADDYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREIL 304
Cdd:TIGR00763 239 LGIekDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEIL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  305 DADHHGLDDVKDRIVEYLAVRARRaerglqvvgGRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEI 384
Cdd:TIGR00763 319 DEDHYGLKKVKERILEYLAVQKLR---------GKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEI 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  385 RGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVLFLAT 464
Cdd:TIGR00763 390 RGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIAT 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  465 ANVIENIPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAK 544
Cdd:TIGR00763 470 ANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEK 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  545 ALRKAATNLA-----QGTATAPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLK 619
Cdd:TIGR00763 550 ICRKAAVKLVeqgekKKSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLE 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  620 LTGQLGDVMKESAQIALSYVRAHAEQLGVDPELLNRT-IHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTG 698
Cdd:TIGR00763 630 LTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKAdIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTG 709
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493924021  699 EVTLNGRVLPIGGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQAL 764
Cdd:TIGR00763 710 EITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
2-775 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 627.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   2 SQTYSLPVLFVPDVVVLPGMVVPIPLD-DAAQATVDAARASESGKLLVA--------PRLDDRYpTYGVVASIVQVGRIP 72
Cdd:PRK10787   6 SERIEIPVLPLRDVVVYPHMVIPLFVGrEKSIRCLEAAMDHDKKIMLVAqkeastdePGVNDLF-TVGTVASILQMLKLP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  73 GGGLAAVVKGEKRAQIGT----GTPGHGAALWVEATEVEDQEVTDEVRTLAGEYKKLVlaMLQRREAWQLIDAVNKMSDP 148
Cdd:PRK10787  85 DGTVKVLVEGLQRARISAlsdnGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYI--KLNKKIPPEVLTSLNSIDDP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 149 SNLADTSGYASWLTDEQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKELG 228
Cdd:PRK10787 163 ARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 229 E--DEPEGADDYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREILDA 306
Cdd:PRK10787 243 EmdDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 307 DHHGLDDVKDRIVEYLAVRARRAerglqvvggRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRG 386
Cdd:PRK10787 323 DHYGLERVKDRILEYLAVQSRVN---------KIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 387 HRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVLFLATAN 466
Cdd:PRK10787 394 HRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSN 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 467 VIeNIPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAKAL 546
Cdd:PRK10787 474 SM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLC 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 547 RKAATNLAQGTATAPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGD 626
Cdd:PRK10787 553 RKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGE 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 627 VMKESAQIALSYVRAHAEQLGVDPELL-NRTIHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGR 705
Cdd:PRK10787 633 VMQESIQAALTVVRARAEKLGINPDFYeKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQ 712
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493924021 706 VLPIGGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALE--PAAGEQVSAA 775
Cdd:PRK10787 713 VLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQnePSGMQVVTAK 784
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
563-766 1.66e-105

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: 321.50  E-value: 1.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  563 TIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGDVMKESAQIALSYVRAH 642
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  643 AEQLGVDPELL-NRTIHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGRVLPIGGVKQKLLAAQR 721
Cdd:pfam05362  81 AEELGIDPDFFeKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 493924021  722 NGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALEP 766
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
297-487 7.55e-97

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: 298.32  E-value: 7.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 297 IKGAREILDADHHGLDDVKDRIVEYLAVRARRaerglqvvgGRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALG 376
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLK---------GSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 377 GVRDESEIRGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDL 456
Cdd:cd19500   72 GVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDL 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 493924021 457 SDVLFLATANVIENIPSALLDRMELVTLDGY 487
Cdd:cd19500  152 SKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
341-420 6.37e-04

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: 40.82  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   341 SGAVMVLAGPPGVGKTSLGESVARALGRKFVRV--------ALGGVRDESEIRGHRRTYVGALPGRIVRAIGEA-GSMNP 411
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALArKLKPD 80

                   ....*....
gi 493924021   412 VVLLDEIDK 420
Cdd:smart00382  81 VLILDEITS 89
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
7-767 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1046.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   7 LPVLFVPDVVVLPGMVVPIPL-DDAAQATVDAARASESGKLLVA--------PRLDDRYpTYGVVASIVQVGRIPGGGLA 77
Cdd:COG0466   14 LPLLPLRDVVVFPGMVIPLFVgREKSIKALEEAMEGDKLIGLVAqkdaevedPGPDDLY-EVGTVAKILQLLKLPDGTVK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  78 AVVKGEKRAQIGTGTPGHGAaLWVEATEVEDQEVTDE-----VRTLAGEYKKLVlaMLQRREAWQLIDAVNKMSDPSNLA 152
Cdd:COG0466   93 VLVEGLQRARIKEFVQEEPY-LEAEVEPLEEEEEDDKelealMRSLKEQFEEYV--KLNPKIPPELLAALSNIEDPGRLA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 153 DTSGYASWLTDEQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKELGEDEP 232
Cdd:COG0466  170 DFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEKDD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 233 EGAD--DYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREILDADHHG 310
Cdd:COG0466  250 GEDEieELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYG 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 311 LDDVKDRIVEYLAVRARRAErglqvvggrGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRGHRRT 390
Cdd:COG0466  330 LEKVKERILEYLAVRKLKKK---------LKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 391 YVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRdhyldldldlsdvlflATANVIEN 470
Cdd:COG0466  401 YIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSdhylevpfdlskvmfiATANSLDT 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 471 IPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAKALRKAA 550
Cdd:COG0466  481 IPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 551 TNLAQGTATaPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGDVMKE 630
Cdd:COG0466  561 KKIAEGKKK-KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKE 639
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 631 SAQIALSYVRAHAEQLGVDPELLNRT-IHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGRVLPI 709
Cdd:COG0466  640 SAQAALSYVRSRAEELGIDPDFFEKYdIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPI 719
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493924021 710 GGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALEPA 767
Cdd:COG0466  720 GGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
8-764 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: 825.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021    8 PVLFVPDVVVLPGMVVPIPL-DDAAQATVDAARASESGKLLVA---------PRLDDRYPTyGVVASIVQ---VGRIPGG 74
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVgREKSIKLIKEALRLKQPYLGLFlqkdddneePEEDDIYSV-GVVAQILEmlpLPSSGTA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   75 GLAAVVKGEKRAQIGTGTPGHGAaLWVEATEVEDQEV---TDEVRTLAGEYKKLVLAMLQRREAWQ----LIDAVNKMSD 147
Cdd:TIGR00763  80 TYKVVVEGLRRIRIKELSDKGGY-LVVRVDNLKEEPFdkdDEEIKALTREIKETFRELISLSKLFReqpaLLSALEDIDE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  148 PSNLADTSGYASWLTD-EQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKE 226
Cdd:TIGR00763 159 PGRLADFVAASLQLKEkDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  227 LGE--DEPEGADDYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREIL 304
Cdd:TIGR00763 239 LGIekDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEIL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  305 DADHHGLDDVKDRIVEYLAVRARRaerglqvvgGRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEI 384
Cdd:TIGR00763 319 DEDHYGLKKVKERILEYLAVQKLR---------GKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEI 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  385 RGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVLFLAT 464
Cdd:TIGR00763 390 RGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIAT 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  465 ANVIENIPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAK 544
Cdd:TIGR00763 470 ANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEK 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  545 ALRKAATNLA-----QGTATAPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLK 619
Cdd:TIGR00763 550 ICRKAAVKLVeqgekKKSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLE 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  620 LTGQLGDVMKESAQIALSYVRAHAEQLGVDPELLNRT-IHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTG 698
Cdd:TIGR00763 630 LTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKAdIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTG 709
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493924021  699 EVTLNGRVLPIGGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQAL 764
Cdd:TIGR00763 710 EITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
2-775 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 627.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   2 SQTYSLPVLFVPDVVVLPGMVVPIPLD-DAAQATVDAARASESGKLLVA--------PRLDDRYpTYGVVASIVQVGRIP 72
Cdd:PRK10787   6 SERIEIPVLPLRDVVVYPHMVIPLFVGrEKSIRCLEAAMDHDKKIMLVAqkeastdePGVNDLF-TVGTVASILQMLKLP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  73 GGGLAAVVKGEKRAQIGT----GTPGHGAALWVEATEVEDQEVTDEVRTLAGEYKKLVlaMLQRREAWQLIDAVNKMSDP 148
Cdd:PRK10787  85 DGTVKVLVEGLQRARISAlsdnGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYI--KLNKKIPPEVLTSLNSIDDP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 149 SNLADTSGYASWLTDEQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKELG 228
Cdd:PRK10787 163 ARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 229 E--DEPEGADDYRSRIEEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWNTRTEDSTDIKGAREILDA 306
Cdd:PRK10787 243 EmdDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 307 DHHGLDDVKDRIVEYLAVRARRAerglqvvggRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRG 386
Cdd:PRK10787 323 DHYGLERVKDRILEYLAVQSRVN---------KIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 387 HRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDLSDVLFLATAN 466
Cdd:PRK10787 394 HRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSN 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 467 VIeNIPSALLDRMELVTLDGYTEDDKVAIARDYLLPRQAERAALTTDEVSVTDAALREIAANYTREPGVRQFERLLAKAL 546
Cdd:PRK10787 474 SM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLC 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 547 RKAATNLAQGTATAPVTIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGD 626
Cdd:PRK10787 553 RKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGE 632
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 627 VMKESAQIALSYVRAHAEQLGVDPELL-NRTIHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGR 705
Cdd:PRK10787 633 VMQESIQAALTVVRARAEKLGINPDFYeKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQ 712
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493924021 706 VLPIGGVKQKLLAAQRNGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALE--PAAGEQVSAA 775
Cdd:PRK10787 713 VLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQnePSGMQVVTAK 784
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
563-766 1.66e-105

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: 321.50  E-value: 1.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  563 TIDEPDLRDYLGRPRFTPESAERTAVPGVATGLAVTGMGGDVLFIEVNATDGEPGLKLTGQLGDVMKESAQIALSYVRAH 642
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  643 AEQLGVDPELL-NRTIHVHVPAGAVPKDGPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGRVLPIGGVKQKLLAAQR 721
Cdd:pfam05362  81 AEELGIDPDFFeKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 493924021  722 NGLKTVFIPQRNSPDLDDVPAEVLDALDVRPMTDVAEIVAQALEP 766
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
297-487 7.55e-97

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: 298.32  E-value: 7.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 297 IKGAREILDADHHGLDDVKDRIVEYLAVRARRaerglqvvgGRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALG 376
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLK---------GSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 377 GVRDESEIRGHRRTYVGALPGRIVRAIGEAGSMNPVVLLDEIDKVGSDYRGDPAAALLEVLDPAQNHTFRDHYLDLDLDL 456
Cdd:cd19500   72 GVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDL 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 493924021 457 SDVLFLATANVIENIPSALLDRMELVTLDGY 487
Cdd:cd19500  152 SKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
7-185 7.25e-23

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: 97.02  E-value: 7.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021    7 LPVLFVPDVVVLPGMVVPIPLDDAA-QATVDAARASESGKLLVA----------PRLDDRYPtYGVVASIVQVGRIPGGG 75
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRsIAAIEAALNKDKLYGVLLvsqkdaedeePTPDDLYE-VGTVAKIVQILKLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   76 LAAVVKGEKRAQI---GTGTPGHGAALwVEATEVEDQEVTDEVRTLAGEYKKLVLAMLQRREAWQLIDAVNKMSDPSNLA 152
Cdd:pfam02190  81 YKVLVEGLERVRIvelVKKEEPYLRAE-VEDLPEDSDELSEALKALVKELIEKLRRLLKLLLPLELLLKIKDIENPGRLA 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 493924021  153 DTSGYASWLTDEQKRELLETPDTAARLRLLIEW 185
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLEL 192
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
345-480 7.32e-22

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: 91.89  E-value: 7.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  345 MVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDeseirghrrTYVGALPGRIVRAIGEAGSMNP-VVLLDEIDKVGS 423
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493924021  424 D-------YRGDPAAALLEVLDPAQNHTFRdhyldldldlsdVLFLATANVIENIPSALLDRME 480
Cdd:pfam00004  72 SrgsggdsESRRVVNQLLTELDGFTSSNSK------------VIVIAATNRPDKLDPALLGRFD 123
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
595-760 1.95e-16

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 78.87  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 595 LAVTG-MGGDVLFIEVNAT---DGEPGLKLTGQLGDVMKESAQIAlSYVrahAEQL-GVDPELLNRTIHVHVPAGAVpkD 669
Cdd:COG1750   35 PAVSGtGEGVVINITVTVTypgSGRVYVSTSPLTGPDTQASARIA-ALV---ASLLaGVDLSSYDVYISIESDSPIV--G 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 670 GPSAGVTMVTALVSMATGRRVRAEVGMTGEVTLNGRVLPIGGVKQKLLAAQRNGLKTVFIP--QRNSPDLDDVPAEVLDA 747
Cdd:COG1750  109 GPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPkgQAILTGYNTQVGETVDL 188
                        170       180
                 ....*....|....*....|.
gi 493924021 748 --------LDVRPMTDVAEIV 760
Cdd:COG1750  189 veygkelgVKVIEVSTIADAL 209
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
163-550 1.50e-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: 76.49  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 163 DEQKRELLETPDTAARLRLLIEWTGDHLAESEVSEKIAEDVRAGMDKQQKEFLLRQQLAAIRKELGEDEPEGADDYRSRI 242
Cdd:COG0464   22 ALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 243 EEAELPEKVREAALREVGKLERASDQSPETGWIRTWLDTVLDLPWntrtedstDIKGAREILDADHHGLDDVKD---RIV 319
Cdd:COG0464  102 LLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEE--------ELLELREAILDDLGGLEEVKEelrELV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 320 EYLAVRAR-RAERGLQVVGGrgsgavMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDEseirghrrtYVGALPGR 398
Cdd:COG0464  174 ALPLKRPElREEYGLPPPRG------LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------YVGETEKN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 399 IVRAIGEAGSMNPVVLL-DEIDKVGSDyRGDPA--------AALLEVLDpaqNHTFRdhyldldldlsdVLFLATANVIE 469
Cdd:COG0464  239 LREVFDKARGLAPCVLFiDEADALAGK-RGEVGdgvgrrvvNTLLTEME---ELRSD------------VVVIAATNRPD 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 470 NIPSALLDRM-ELVTLDGYTEDDKVAIARDYLLPRQAEraalttdevsvTDAALREIAA---NYTrepgVRQFERLLAKA 545
Cdd:COG0464  303 LLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD-----------EDVDLEELAEateGLS----GADIRNVVRRA 367

                 ....*
gi 493924021 546 LRKAA 550
Cdd:COG0464  368 ALQAL 372
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
314-442 7.33e-12

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: 64.23  E-value: 7.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 314 VKDRIVEYLAVRaRRAERGLQVVGGRGSGavMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDEseirghrrtYVG 393
Cdd:cd19481    1 LKASLREAVEAP-RRGSRLRRYGLGLPKG--ILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK---------YVG 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493924021 394 ALPGRIVRAIGEAGSMNP-VVLLDEIDKVGSDyRGDPA---------AALLEVLDPAQN 442
Cdd:cd19481   69 ESEKNLRKIFERARRLAPcILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS 126
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
310-428 2.77e-08

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 56.17  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 310 GLDDVKDRIVEYLAVRARRAER----GLQVVGGrgsgavMVLAGPPGVGKTSLGESVARALGRKFVRVALggvrdeSEIr 385
Cdd:COG1222   82 GLDEQIEEIREAVELPLKNPELfrkyGIEPPKG------VLLYGPPGTGKTLLAKAVAGELGAPFIRVRG------SEL- 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493924021 386 ghRRTYVGAlPGRIVRAIGE-AGSMNP-VVLLDEIDKVGSDyRGD 428
Cdd:COG1222  149 --VSKYIGE-GARNVREVFElAREKAPsIIFIDEIDAIAAR-RTD 189
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
316-549 7.63e-08

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 54.12  E-value: 7.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 316 DRIVEYLAVRARRAERGLQVVGGrgsgavMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDEseirghrrtYVGAL 395
Cdd:COG1223   15 KLIIKELRRRENLRKFGLWPPRK------ILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 396 PGRIVRAIGEAGSMNPVVLLDEIDKVGSDyRGDPAA---------ALLEVLDPAQNHTFrdhyldldldlsdvlFLATAN 466
Cdd:COG1223   80 ARNLRKLFDFARRAPCVIFFDEFDAIAKD-RGDQNDvgevkrvvnALLQELDGLPSGSV---------------VIAATN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 467 VIENIPSALLDRMELV-TLDGYTEDDKVAIARDYLLPRQAEraalttdevsvTDAALREIAANYTREPGvRQFERLLAKA 545
Cdd:COG1223  144 HPELLDSALWRRFDEViEFPLPDKEERKEILELNLKKFPLP-----------FELDLKKLAKKLEGLSG-ADIEKVLKTA 211

                 ....
gi 493924021 546 LRKA 549
Cdd:COG1223  212 LKKA 215
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
339-438 1.37e-07

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: 51.38  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 339 RGSGAVMVLAGPPGVGKTSLGESVARALGRK---FVRVALGGVRDESEIRGHRRTYVGALPGRIVRAigeagSMNPVVLL 415
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELFRPgapFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK-----AKPGVLFI 90
                         90       100
                 ....*....|....*....|...
gi 493924021 416 DEIDKVgsdyRGDPAAALLEVLD 438
Cdd:cd00009   91 DEIDSL----SRGAQNALLRVLE 109
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
345-438 1.78e-07

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: 50.75  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  345 MVLAGPPGVGKTSLGESVARAL-GRKFVRVALGGVRDESEIRGHRRTYVGAL---PGRIVRAIGEAGsmnpVVLLDEIDK 420
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGAswvDGPLVRAAREGE----IAVLDEINR 77
                          90
                  ....*....|....*...
gi 493924021  421 VGSDYrgdpAAALLEVLD 438
Cdd:pfam07728  78 ANPDV----LNSLLSLLD 91
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
347-438 1.07e-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: 49.50  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  347 LAGPPGVGKTSLGESVARALG---RKFVRValggvrDESEIrgHRRTYV----GALPGRIVRAIG----EAGSMNP--VV 413
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGYEEGgqltEAVRRKPysIV 79
                          90       100
                  ....*....|....*....|....*.
gi 493924021  414 LLDEIDKVGSD-YRgdpaaALLEVLD 438
Cdd:pfam07724  80 LIDEIEKAHPGvQN-----DLLQILE 100
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
310-446 1.65e-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: 51.38  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  310 GLDDVKDRIVEY---LAVRARRAERGLQVVGgrgSGAVMVLAGPPGVGKTslgeSVARALGRKFvrVALGGVRDESEIRG 386
Cdd:TIGR03922 280 GLERVKRQVAALkssTAMALARAERGLPVAQ---TSNHMLFAGPPGTGKT----TIARVVAKIY--CGLGVLRKPLVREV 350
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493924021  387 HRRTYVGalpgrivRAIGEA---------GSMNPVVLLDEIDKVGSDYRGDP----AAALLEVLDPAQNHTFR 446
Cdd:TIGR03922 351 SRADLIG-------QYIGESeaktneiidSALGGVLFLDEAYTLVETGYGQKdpfgLEAIDTLLARMENDRDR 416
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
349-525 1.75e-06

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: 50.55  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 349 GPPGVGKTSLGESVARALGRKFVRV----------ALGgvrdeSEI--RGHRRTYVgaLPGRIVRaigeagsmnPVVLLD 416
Cdd:COG0714   38 GVPGVGKTTLAKALARALGLPFIRIqftpdllpsdILG-----TYIydQQTGEFEF--RPGPLFA---------NVLLAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 417 EIDkvgsdyRGDPA--AALLEVLDPAQ----NHTFRdhyldldlDLSDVLFLATANVIENI-----PSALLDRMELVTLD 485
Cdd:COG0714  102 EIN------RAPPKtqSALLEAMEERQvtipGGTYK--------LPEPFLVIATQNPIEQEgtyplPEAQLDRFLLKLYI 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493924021 486 GY-TEDDKVAIARDYLLPRQAE-RAALTTDEVSVTDAALREI 525
Cdd:COG0714  168 GYpDAEEEREILRRHTGRHLAEvEPVLSPEELLALQELVRQV 209
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
129-437 2.15e-06

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 50.92  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 129 MLQRREAWQLIDAVNKMSDPSNLADTSGYASWLTDEQKRELLETPDTAARLRLLIEWTGDHLAEsEVSEKIAEDVRAGMD 208
Cdd:COG1401   10 FLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAA-LEVVVLLLDLEKVEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 209 KQQKEFLLRQQLAAIRKELGEDEPEGADDYRSRIEEAELPEKVREAALREVGKLERASDQsPETGWIRTWLDTVLDLPWN 288
Cdd:COG1401   89 NEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERA-ALETEVLEALEAELEELLA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 289 TRTEDSTDIKGAREILDADHHGLDDVKDRIVEYLAVRARRAERGLQVVGGRGSGAVMVLAGPPGVGKTSLGESVARALG- 367
Cdd:COG1401  168 APEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGg 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 368 ---RKFVRVAlggVR----DESEIRGHR-RTYVGAL---PGRIVRAIGEAgSMNP----VVLLDEIDkvgsdyRGDPAAA 432
Cdd:COG1401  248 ednGRIEFVQ---FHpswsYEDFLLGYRpSLDEGKYeptPGIFLRFCLKA-EKNPdkpyVLIIDEIN------RANVEKY 317

                 ....*
gi 493924021 433 LLEVL 437
Cdd:COG1401  318 FGELL 322
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
345-418 1.59e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.16  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 345 MVLAGPPGVGKTSLGESVARALGRKFVRV--ALGGVRDeseirghrrtyvgalpgrIVRAIGEAGSM-----NPVVLLDE 417
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALsaVTSGVKD------------------LREVIEEARQRrsagrRTILFIDE 100

                 .
gi 493924021 418 I 418
Cdd:PRK13342 101 I 101
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
607-733 1.67e-05

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 44.75  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  607 IEVNATDGEPGLKLTGQLGDVMKESAQIalsyVRAHAEQLGVDPELLNRTIHVhVPAGaVPKDGPSAGVTMVTALVSMAT 686
Cdd:pfam13541   1 VEVDVSKGLPAFTIVGLPDTAVKESKER----VRAALKNSGFEFPPKRITVNL-APAD-LKKEGSSFDLPIAIGILAAQG 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 493924021  687 GRRVRAEVGMTGEVTLNGRVLPIGGVKQKLLAAQRNGLKTVFIPQRN 733
Cdd:pfam13541  75 QIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
316-438 2.29e-05

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: 45.63  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 316 DRIVEYLAVRARRAERGLQvvGGRGSGAVMVLAGPPGVGKTSLGESVARAL---GRKFVRValggvrDESE-IRGHRRTY 391
Cdd:cd19499   17 DEAVKAVSDAIRRARAGLS--DPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRI------DMSEyMEKHSVSR 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493924021 392 VGALPGRIV--RAIG---EAGSMNP--VVLLDEIDKVGSDYRGdpaaALLEVLD 438
Cdd:cd19499   89 LIGAPPGYVgyTEGGqltEAVRRKPysVVLLDEIEKAHPDVQN----LLLQVLD 138
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
670-733 3.10e-05

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 46.73  E-value: 3.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493924021 670 GPSAGvTMVT-ALVSMAT------GRRVRAevgmTGEVTLNGRVLPIGGVKQKLLAAQRNGLKTVFIPQRN 733
Cdd:COG3480  240 GPSAG-LMFAlGIYDQLTpgdltgGKKIAG----TGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN 305
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
345-418 5.24e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 46.59  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 345 MVLAGPPGVGKTSLGESVARALGRKFVRV--ALGGVRDeseIRghrrtyvgalpgrivRAIGEA-----GSMNPVVLLDE 417
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTSGVKD---IR---------------EVIEEArerraYGRRTILFVDE 113

                 .
gi 493924021 418 I 418
Cdd:COG2256  114 I 114
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
310-423 9.46e-05

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 43.55  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 310 GLDDVKDRIVEYLAVRARRAERGLQ--VVGGRGsgavMVLAGPPGVGKTSLGESVARALGRKFVRVA----LGGVRDESE 383
Cdd:cd19518    4 GMDSTLKELCELLIHPILPPEYFQHlgVEPPRG----VLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESE 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 493924021 384 irghrrtyvgalpGRIVRAIGEAGSMNP-VVLLDEIDKVGS 423
Cdd:cd19518   80 -------------EKIRELFDQAISNAPcIVFIDEIDAITP 107
PRK04195 PRK04195
replication factor C large subunit; Provisional
346-442 5.95e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.99  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 346 VLAGPPGVGKTSLGESVARALGRKFVRValggvrDESEirghRRTYvgalpGRIVRAIGEAGSMNP-------VVLLDEI 418
Cdd:PRK04195  43 LLYGPPGVGKTSLAHALANDYGWEVIEL------NASD----QRTA-----DVIERVAGEAATSGSlfgarrkLILLDEV 107
                         90       100
                 ....*....|....*....|....*.
gi 493924021 419 D--KVGSDYRGdpAAALLEVLDPAQN 442
Cdd:PRK04195 108 DgiHGNEDRGG--ARAILELIKKAKQ 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
341-420 6.37e-04

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: 40.82  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021   341 SGAVMVLAGPPGVGKTSLGESVARALGRKFVRV--------ALGGVRDESEIRGHRRTYVGALPGRIVRAIGEA-GSMNP 411
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALArKLKPD 80

                   ....*....
gi 493924021   412 VVLLDEIDK 420
Cdd:smart00382  81 VLILDEITS 89
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
310-426 8.18e-04

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 40.80  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 310 GLDDVKDRIVEYLAVRARRAErglQVVGGRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGV----RDESEir 385
Cdd:cd19509    3 GLDDAKEALKEAVILPSLRPD---LFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLvskwVGESE-- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 493924021 386 ghrrtyvgalpgRIVRAIGE-AGSMNP-VVLLDEIDKVGSDYR 426
Cdd:cd19509   78 ------------KIVRALFAlARELQPsIIFIDEIDSLLSERG 108
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
346-371 9.38e-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: 40.62  E-value: 9.38e-04
                         10        20
                 ....*....|....*....|....*.
gi 493924021 346 VLAGPPGVGKTSLGESVARALGRKFV 371
Cdd:cd00464    3 VLIGMMGAGKTTVGRLLAKALGLPFV 28
Sms COG1066
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ...
671-764 9.73e-04

DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];


Pssm-ID: 440685 [Multi-domain]  Cd Length: 453  Bit Score: 42.34  E-value: 9.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 671 PSAGVTMVTALVSMATGRRVRA------EVGMTGEVtlngRvlPIGGVKQKLLAAQRNGLKTVFIPQRNSPDLDDvpaev 744
Cdd:COG1066  366 PAADLAVALAIASSFRDRPLPPdtvffgEVGLTGEI----R--PVSRIEQRLKEAAKLGFKRAIVPKGNKKKLKP----- 434
                         90       100
                 ....*....|....*....|
gi 493924021 745 lDALDVRPMTDVAEIVAQAL 764
Cdd:COG1066  435 -KGIEIIGVSTLEEALEALF 453
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
346-371 1.24e-03

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 40.11  E-value: 1.24e-03
                         10        20
                 ....*....|....*....|....*.
gi 493924021 346 VLAGPPGVGKTSLGESVARALGRKFV 371
Cdd:COG0703    2 VLIGMMGAGKSTVGRLLAKRLGLPFV 27
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
346-423 1.29e-03

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 40.40  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 346 VLAGPPGVGKTSLGESVARALGRKFVRVAlggvrdESEIrghRRTYVGALPgRIVRAIGE-AGSMNP-VVLLDEIDKVGS 423
Cdd:cd19502   41 LLYGPPGTGKTLLAKAVANHTDATFIRVV------GSEL---VQKYIGEGA-RLVRELFEmAREKAPsIIFIDEIDAIGA 110
aroK PRK00131
shikimate kinase; Reviewed
346-371 1.65e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 40.17  E-value: 1.65e-03
                         10        20
                 ....*....|....*....|....*.
gi 493924021 346 VLAGPPGVGKTSLGESVARALGRKFV 371
Cdd:PRK00131   8 VLIGFMGAGKSTIGRLLAKRLGYDFI 33
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
306-422 2.60e-03

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 39.52  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 306 ADHHGLDDVKD---RIVEYLavraRRAERgLQVVGGRGSGAVMvLAGPPGVGKTSLGESVARALGRKFVRVAlGGVRDEs 382
Cdd:cd19501    4 KDVAGCEEAKEelkEVVEFL----KNPEK-FTKLGAKIPKGVL-LVGPPGTGKTLLAKAVAGEAGVPFFSIS-GSDFVE- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493924021 383 eirghrrTYVGALPGRiVRAIGEAGSMNP--VVLLDEIDKVG 422
Cdd:cd19501   76 -------MFVGVGASR-VRDLFEQAKKNApcIVFIDEIDAVG 109
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
310-476 2.68e-03

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 39.27  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 310 GLDDVKDriveYLAVRAR----RAER-GLQVVGGrgsgavMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDEsei 384
Cdd:cd19507    4 GLDNLKD----WLKKRKAafskQASAyGLPTPKG------LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 385 rghrrtYVGALPGRIVRAIGEAGSMNPVVLL-DEIDKV--GSDYRGDPA------AALLEVLDPAQNHTFrdhyldldld 455
Cdd:cd19507   71 ------LVGESESRLRQMIQTAEAIAPCVLWiDEIEKGfsNADSKGDSGtssrvlGTFLTWLQEKKKPVF---------- 134
                        170       180
                 ....*....|....*....|.
gi 493924021 456 lsdvlFLATANVIENIPSALL 476
Cdd:cd19507  135 -----VVATANNVQSLPPELL 150
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
310-419 3.12e-03

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 39.20  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 310 GLDDVKDRIVEYLAVRARRAE--RGLQVVGGRGsgavMVLAGPPGVGKTSLGESVARALGRKFVrvalggVRDESEIRGh 387
Cdd:cd19503    4 GLDEQIASLKELIELPLKYPElfRALGLKPPRG----VLLHGPPGTGKTLLARAVANEAGANFL------SISGPSIVS- 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 493924021 388 rrTYVGALPGRIVRAIGEAGSMNP-VVLLDEID 419
Cdd:cd19503   73 --KYLGESEKNLREIFEEARSHAPsIIFIDEID 103
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
339-442 4.06e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.02  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  339 RGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRG-----HRRTYVGALPGRIVRAIGEAGSMNPVV 413
Cdd:pfam13191  21 SGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPllealTREGLLRQLLDELESSLLEAWRAALLE 100
                          90       100
                  ....*....|....*....|....*....
gi 493924021  414 LLDEIDKVGSDYRGDPAAALLEVLDPAQN 442
Cdd:pfam13191 101 ALAPVPELPGDLAERLLDLLLRLLDLLAR 129
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
302-366 4.33e-03

PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.


Pssm-ID: 214810  Cd Length: 361  Bit Score: 39.97  E-value: 4.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493924021   302 EILDADHHGLDDVKDRIVEYLavraRRAERGLQVvggrgSGAVMVLAGPPGVGKTSLGESVARAL 366
Cdd:smart00763  47 RFFDHDFFGMEEAIERFVNYF----KSAAQGLEE-----RKQILYLLGPVGGGKSSLVECLKRGL 102
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
306-422 4.87e-03

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 40.40  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 306 ADHHGLDDVKDRI---VEYLAVRARraergLQVVGGR-GSGAVMVlaGPPGVGKTSLGESVARALGRKFVRVAlggVRDE 381
Cdd:PRK10733 152 ADVAGCDEAKEEVaelVEYLREPSR-----FQKLGGKiPKGVLMV--GPPGTGKTLLAKAIAGEAKVPFFTIS---GSDF 221
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493924021 382 SEIrghrrtYVGALPGRIVRAIGEAGSMNP-VVLLDEIDKVG 422
Cdd:PRK10733 222 VEM------FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVG 257
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
341-396 5.64e-03

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


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 38.55  E-value: 5.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493924021 341 SGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGvRDESeirghRRTYVGALP 396
Cdd:COG4088    3 SPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLH-SDDF-----RRFLVNESF 52
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
310-384 5.74e-03

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 39.60  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021  310 GLDDvkDRIVEYLA------VRARRAErGL---QVVGGRGSGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGvrd 380
Cdd:pfam06068  12 GLDE--DGEARYVSgglvgqEKAREAA-GViveMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTPFTSISG--- 85

                  ....
gi 493924021  381 eSEI 384
Cdd:pfam06068  86 -SEV 88
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
346-438 7.93e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.82  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 346 VLAGPPGVGKTSLGESVARALGRKFVRValggvrDESEIrGHRRT---YVGALPGRIVRAIG----EAGSMNP--VVLLD 416
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVGFDQGglltDAVIKHPhaVLLLD 564
                         90       100
                 ....*....|....*....|..
gi 493924021 417 EIDKVGSDYRGdpaaALLEVLD 438
Cdd:PRK11034 565 EIEKAHPDVFN----LLLQVMD 582
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
341-419 9.58e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.61  E-value: 9.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493924021 341 SGAVMVLAGPPGVGKTSLGESVARALGRKFVRVALGGVRDESEIRGHRRTYVGALPG-------RIvrAIGEAGSMNP-V 412
Cdd:cd00267   24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrqRV--ALARALLLNPdL 101

                 ....*..
gi 493924021 413 VLLDEID 419
Cdd:cd00267  102 LLLDEPT 108
 
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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