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Conserved domains on  [gi|446320589|ref|WP_000398444|]
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MULTISPECIES: endopeptidase La [Leptospira]

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, ...
19-791 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1095.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  19 SIIPLDSILPPELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLLKDEENEKETSENIYQYGVVAKIL 98
Cdd:COG0466    2 SEEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  99 KKVNLPDNAVNILVNTIRRFKIESFVNKDP-LVARVSYPEEEPgAPKNTTKAMMRTLLVMTRELAQNNPLFTEEMKLTML 177
Cdd:COG0466   82 QLLKLPDGTVKVLVEGLQRARIKEFVQEEPyLEAEVEPLEEEE-EDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 178 NVNEPGKMADFVCSILNLEKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAI 257
Cdd:COG0466  161 NIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 258 QNELGIKDDKfEKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKA 337
Cdd:COG0466  241 QKELGEKDDG-EDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 338 KKTLDKDHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRR 417
Cdd:COG0466  320 EKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRR 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 418 TYIGSMPGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLD 497
Cdd:COG0466  400 TYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 498 SISRILLDRMEIINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKI 577
Cdd:COG0466  480 TIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKV 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 578 AIKIVRKESFPKIIQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEE 657
Cdd:COG0466  560 AKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKE 639
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 658 SSNIALSYIK----NLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAI 733
Cdd:COG0466  640 SAQAALSYVRsraeELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPI 719
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589 734 GGLREKIVAAKRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALLLFDEK 791
Cdd:COG0466  720 GGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
19-791 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1095.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  19 SIIPLDSILPPELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLLKDEENEKETSENIYQYGVVAKIL 98
Cdd:COG0466    2 SEEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  99 KKVNLPDNAVNILVNTIRRFKIESFVNKDP-LVARVSYPEEEPgAPKNTTKAMMRTLLVMTRELAQNNPLFTEEMKLTML 177
Cdd:COG0466   82 QLLKLPDGTVKVLVEGLQRARIKEFVQEEPyLEAEVEPLEEEE-EDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 178 NVNEPGKMADFVCSILNLEKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAI 257
Cdd:COG0466  161 NIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 258 QNELGIKDDKfEKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKA 337
Cdd:COG0466  241 QKELGEKDDG-EDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 338 KKTLDKDHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRR 417
Cdd:COG0466  320 EKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRR 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 418 TYIGSMPGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLD 497
Cdd:COG0466  400 TYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 498 SISRILLDRMEIINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKI 577
Cdd:COG0466  480 TIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKV 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 578 AIKIVRKESFPKIIQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEE 657
Cdd:COG0466  560 AKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKE 639
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 658 SSNIALSYIK----NLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAI 733
Cdd:COG0466  640 SAQAALSYVRsraeELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPI 719
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589 734 GGLREKIVAAKRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALLLFDEK 791
Cdd:COG0466  720 GGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
33-788 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: 889.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589   33 LIPIKSRPVFPGIITPLIVPSGKFAKAVEETVK-GNSFLGLVLLKDEENEKETSENIYQYGVVAKILKKVNLPDN---AV 108
Cdd:TIGR00763   2 LLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRlKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSSgtaTY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  109 NILVNTIRRFKIESFV-NKDPLVARVSYPEEEPGAPKN-TTKAMMRTLLVMTRELAQNNPLFTEEMKLTML--NVNEPGK 184
Cdd:TIGR00763  82 KVVVEGLRRIRIKELSdKGGYLVVRVDNLKEEPFDKDDeEIKALTREIKETFRELISLSKLFREQPALLSAleDIDEPGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  185 MADFVCSILNL-EKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGI 263
Cdd:TIGR00763 162 LADFVAASLQLkEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  264 KDDKfEKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKAKKTLDK 343
Cdd:TIGR00763 242 EKDD-KDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  344 DHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRRTYIGSM 423
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  424 PGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLDSISRIL 503
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  504 LDRMEIINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKIAIKIVR 583
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  584 K------ESFPKIIQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEE 657
Cdd:TIGR00763 561 QgekkksEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  658 SSNIALSYIKNLLYKE----ELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAI 733
Cdd:TIGR00763 641 SAQIALTYVRSIAADLgispNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446320589  734 GGLREKIVAAKRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALLLF 788
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
30-786 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 579.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  30 ELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLLKDEENEKETSENIYQYGVVAKILKKVNLPDNAVN 109
Cdd:PRK10787  10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 110 ILVNTIRRFKIESFV-NKDPLVARVSYpEEEPGAPKNTTKAMMRTLLVMTRELAQNNPLFTEEMKLTMLNVNEPGKMADF 188
Cdd:PRK10787  90 VLVEGLQRARISALSdNGEHFSAKAEY-LESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 189 VCSILNLEKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGIKDDKf 268
Cdd:PRK10787 169 IAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDA- 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 269 EKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKAKKTLDKDHYKL 348
Cdd:PRK10787 248 PDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 349 EDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRRTYIGSMPGKII 428
Cdd:PRK10787 328 ERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 429 SALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLDsISRILLDRME 508
Cdd:PRK10787 408 QKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDRME 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 509 IINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKIAIKIVRKESFP 588
Cdd:PRK10787 487 VIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSLK 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 589 KI-IQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEESSNIALSYIK 667
Cdd:PRK10787 567 HIeINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVR 646
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 668 ----NLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAIGGLREKIVAA 743
Cdd:PRK10787 647 araeKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAA 726
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|...
gi 446320589 744 KRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALL 786
Cdd:PRK10787 727 HRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTL 769
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
334-515 2.51e-118

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: 355.71  E-value: 2.51e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 334 LEKAKKTLDKDHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIK 413
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 414 GHRRTYIGSMPGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATA 493
Cdd:cd19500   81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                        170       180
                 ....*....|....*....|..
gi 446320589 494 NTLDSISRILLDRMEIINLSGY 515
Cdd:cd19500  161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
591-783 3.42e-81

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: 259.48  E-value: 3.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  591 IQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEESSNIALSYI---- 666
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVrsra 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  667 KNLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAIGGLREKIVAAKRV 746
Cdd:pfam05362  82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446320589  747 GIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEV 783
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEV 198
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
369-507 5.38e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 55.84  E-value: 5.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589   369 KGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSV--GGMRDEAEIKGHRRTYIGSMPGKIISALRIT-------KERDC 439
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalarKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589   440 VILLDEIDklsigiqgdpaSALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLDSISRILLDRM 507
Cdd:smart00382  81 VLILDEIT-----------SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
19-791 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1095.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  19 SIIPLDSILPPELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLLKDEENEKETSENIYQYGVVAKIL 98
Cdd:COG0466    2 SEEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  99 KKVNLPDNAVNILVNTIRRFKIESFVNKDP-LVARVSYPEEEPgAPKNTTKAMMRTLLVMTRELAQNNPLFTEEMKLTML 177
Cdd:COG0466   82 QLLKLPDGTVKVLVEGLQRARIKEFVQEEPyLEAEVEPLEEEE-EDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 178 NVNEPGKMADFVCSILNLEKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAI 257
Cdd:COG0466  161 NIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 258 QNELGIKDDKfEKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKA 337
Cdd:COG0466  241 QKELGEKDDG-EDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 338 KKTLDKDHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRR 417
Cdd:COG0466  320 EKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRR 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 418 TYIGSMPGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLD 497
Cdd:COG0466  400 TYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 498 SISRILLDRMEIINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKI 577
Cdd:COG0466  480 TIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKV 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 578 AIKIVRKESFPKIIQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEE 657
Cdd:COG0466  560 AKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKE 639
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 658 SSNIALSYIK----NLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAI 733
Cdd:COG0466  640 SAQAALSYVRsraeELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPI 719
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589 734 GGLREKIVAAKRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALLLFDEK 791
Cdd:COG0466  720 GGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
33-788 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: 889.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589   33 LIPIKSRPVFPGIITPLIVPSGKFAKAVEETVK-GNSFLGLVLLKDEENEKETSENIYQYGVVAKILKKVNLPDN---AV 108
Cdd:TIGR00763   2 LLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRlKQPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSSgtaTY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  109 NILVNTIRRFKIESFV-NKDPLVARVSYPEEEPGAPKN-TTKAMMRTLLVMTRELAQNNPLFTEEMKLTML--NVNEPGK 184
Cdd:TIGR00763  82 KVVVEGLRRIRIKELSdKGGYLVVRVDNLKEEPFDKDDeEIKALTREIKETFRELISLSKLFREQPALLSAleDIDEPGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  185 MADFVCSILNL-EKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGI 263
Cdd:TIGR00763 162 LADFVAASLQLkEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  264 KDDKfEKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKAKKTLDK 343
Cdd:TIGR00763 242 EKDD-KDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  344 DHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRRTYIGSM 423
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  424 PGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLDSISRIL 503
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  504 LDRMEIINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKIAIKIVR 583
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  584 K------ESFPKIIQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEE 657
Cdd:TIGR00763 561 QgekkksEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  658 SSNIALSYIKNLLYKE----ELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAI 733
Cdd:TIGR00763 641 SAQIALTYVRSIAADLgispNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446320589  734 GGLREKIVAAKRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALLLF 788
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
30-786 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 579.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  30 ELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLLKDEENEKETSENIYQYGVVAKILKKVNLPDNAVN 109
Cdd:PRK10787  10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 110 ILVNTIRRFKIESFV-NKDPLVARVSYpEEEPGAPKNTTKAMMRTLLVMTRELAQNNPLFTEEMKLTMLNVNEPGKMADF 188
Cdd:PRK10787  90 VLVEGLQRARISALSdNGEHFSAKAEY-LESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 189 VCSILNLEKEEYQSVIESNILKTRIEKVLLFLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGIKDDKf 268
Cdd:PRK10787 169 IAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDA- 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 269 EKKYEKFLERLKNLNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKAKKTLDKDHYKL 348
Cdd:PRK10787 248 PDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 349 EDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRRTYIGSMPGKII 428
Cdd:PRK10787 328 ERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLI 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 429 SALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLDsISRILLDRME 508
Cdd:PRK10787 408 QKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDRME 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 509 IINLSGYITDEKVQIFQKYLWKKVLYKNGVTPYGIEFDKKAIVALIDSYSRESGVRGLEKVTDKLVRKIAIKIVRKESFP 588
Cdd:PRK10787 487 VIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSLK 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 589 KI-IQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEESSNIALSYIK 667
Cdd:PRK10787 567 HIeINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVR 646
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 668 ----NLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAIGGLREKIVAA 743
Cdd:PRK10787 647 araeKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAA 726
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|...
gi 446320589 744 KRVGIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEVALL 786
Cdd:PRK10787 727 HRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTL 769
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
334-515 2.51e-118

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: 355.71  E-value: 2.51e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 334 LEKAKKTLDKDHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIK 413
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 414 GHRRTYIGSMPGKIISALRITKERDCVILLDEIDKLSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATA 493
Cdd:cd19500   81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                        170       180
                 ....*....|....*....|..
gi 446320589 494 NTLDSISRILLDRMEIINLSGY 515
Cdd:cd19500  161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
591-783 3.42e-81

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: 259.48  E-value: 3.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  591 IQEKDLETFLGVPKFTDERMVRASVPGTALGLAWTSVGGATLLIEALFVKGKGGILLTGMLGKTMEESSNIALSYI---- 666
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVrsra 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  667 KNLLYKEELFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAIGGLREKIVAAKRV 746
Cdd:pfam05362  82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446320589  747 GIHKIIYPKDNLQHLQEIPDYVKKGMYFFPVSRYEEV 783
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEV 198
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
30-222 6.14e-35

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: 131.69  E-value: 6.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589   30 ELFLIPIKSRPVFPGIITPLIVPSGKFAKAVEETVKGNSFLGLVLL--KDEENEKETSENIYQYGVVAKILKKVNLPDNA 107
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVLLVsqKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  108 VNILVNTIRRFKIESFV--NKDPLVARVSYPEEEpgaPKNTTKAMMRTLLVMTRELAQNNPLFTE-EMKLTMLNVNEPGK 184
Cdd:pfam02190  81 YKVLVEGLERVRIVELVkkEEPYLRAEVEDLPED---SDELSEALKALVKELIEKLRRLLKLLLPlELLLKIKDIENPGR 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 446320589  185 MADFVCSILNLEKEEYQSVIESNILKTRIEKVLLFLKK 222
Cdd:pfam02190 158 LADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
373-515 4.88e-29

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 112.30  E-value: 4.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  373 LLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDeaeikghrrTYIGSMPGKIISALRITKE-RDCVILLDEIDKL-- 449
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKlAPCVIFIDEIDALag 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446320589  450 -----SIGIQGDPASALLEVLDPEQNKNfrdhyldlpfdiSNVFFIATANTLDSISRILLDRMEIINLSGY 515
Cdd:pfam00004  72 srgsgGDSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
348-512 3.00e-17

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: 79.63  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 348 LEDVKDRILEFLAVKKL--KNDEKGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAeikghrRTYIGSMPG 425
Cdd:cd19481    2 KASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 426 KIISALRitKERDCVILLDEIDKLSI--GIQGDPA------SALLEVLDPEQNKNfrdhyldlpfdisNVFFIATANTLD 497
Cdd:cd19481   76 KIFERAR--RLAPCILFIDEIDAIGRkrDSSGESGelrrvlNQLLTELDGVNSRS-------------KVLVIAATNRPD 140
                        170
                 ....*....|....*...
gi 446320589 498 SISRILLDR---MEIINL 512
Cdd:cd19481  141 LLDPALLRPgrfDEVIEF 158
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
352-510 8.33e-15

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: 72.56  E-value: 8.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 352 KDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIA---EAMGRKFFRFSVGGMRDEAEIKGHRRTYIgsmpgKII 428
Cdd:cd00009    1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFGHFL-----VRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 429 SALRITKERDCVILLDEIDKLSIGIQgdpaSALLEVLdpeqnknfrDHYLDLPFDISNVFFIATAN--TLDSISRILLDR 506
Cdd:cd00009   76 LFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVL---------ETLNDLRIDRENVRVIGATNrpLLGDLDRALYDR 142

                 ....
gi 446320589 507 MEII 510
Cdd:cd00009  143 LDIR 146
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
282-528 1.07e-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: 76.87  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 282 LNADPEVIEEVTRELDKFSYADPNTGDYNVIRNYLDILESLpwepapvreIDLEKAKKTLdkdhykledvKDRILEFLAV 361
Cdd:COG0464  119 LELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDL---------GGLEEVKEEL----------RELVALPLKR 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 362 KKLKNDEKGTI---LLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEaeikghrrtYIGSMPGKIISALRITKER- 437
Cdd:COG0464  180 PELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------YVGETEKNLREVFDKARGLa 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 438 DCVILLDEIDKL--SIGIQGDPA-----SALLEVLDpeqnkNFRDhyldlpfdisNVFFIATANTLDSISRILLDRM-EI 509
Cdd:COG0464  251 PCVLFIDEADALagKRGEVGDGVgrrvvNTLLTEME-----ELRS----------DVVVIAATNRPDLLDPALLRRFdEI 315
                        250
                 ....*....|....*....
gi 446320589 510 INLSGYITDEKVQIFQKYL 528
Cdd:COG0464  316 IFFPLPDAEERLEIFRIHL 334
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
693-757 1.69e-13

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 70.39  E-value: 1.69e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446320589 693 DGPSAGITMASAILSLALNTKVKSGFGMTGELTLTGEVLAIGGLREKIVAAKRVGIHKIIYPKDN 757
Cdd:COG1750  108 GGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQ 172
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
373-507 1.41e-10

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 60.00  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  373 LLLVGPPGVGKTSIARSIAEAM-GRKFfrFSVGGMRD--EAEIKGHRRTYIGSM---PGKIISALRitkeRDCVILLDEI 446
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPV--FYVQLTRDttEEDLFGRRNIDPGGAswvDGPLVRAAR----EGEIAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446320589  447 DKLSIGIQGdpasALLEVLDPEqnknfRDHYLDLPFDIS----NVFFIATANTLD----SISRILLDRM 507
Cdd:pfam07728  76 NRANPDVLN----SLLSLLDER-----RLLLPDGGELVKaapdGFRLIATMNPLDrglnELSPALRSRF 135
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
373-499 2.03e-10

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 62.49  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFR--FSVGGMrdEAEIKGH-------RRTYIgsMPGKIISAlritkerdcVILL 443
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRiqFTPDLL--PSDILGTyiydqqtGEFEF--RPGPLFAN---------VLLA 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 444 DEIDKLSIGIQgdpaSALLEVLDPEQ----NKNFRdhyLDLPFdisnvFFIATANTLDSI 499
Cdd:COG0714  101 DEINRAPPKTQ----SALLEAMEERQvtipGGTYK---LPEPF-----LVIATQNPIEQE 148
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
373-502 3.66e-09

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: 56.80  E-value: 3.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAM---GRKFFRFSVGgmrdEAEIKGHRRTYIGSMPG--------KIISALRitKERDCVI 441
Cdd:cd19499   44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMS----EYMEKHSVSRLIGAPPGyvgyteggQLTEAVR--RKPYSVV 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446320589 442 LLDEIDKLSIGIQGdpasALLEVLDpeqNKNFRDHYlDLPFDISNVFFIATANTL--DSISRI 502
Cdd:cd19499  118 LLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSNHFrpEFLNRI 172
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
369-507 5.38e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 55.84  E-value: 5.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589   369 KGTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSV--GGMRDEAEIKGHRRTYIGSMPGKIISALRIT-------KERDC 439
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalarKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589   440 VILLDEIDklsigiqgdpaSALLEVLDPEQNKNFRDHYLDLPFDISNVFFIATANTLDSISRILLDRM 507
Cdd:smart00382  81 VLILDEIT-----------SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
323-528 2.60e-08

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 56.55  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 323 PWEPAPVREIDLEKAKKTLDKDHYKLEDVKDRILEFLaVKKLKNDE----------KGtiLLLVGPPGVGKTSIARSIAE 392
Cdd:COG1222   58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAV-ELPLKNPElfrkygieppKG--VLLYGPPGTGKTLLAKAVAG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 393 AMGRKFFRfsVGGmrdeAEIkghRRTYIGSMPGKIISALRITKERD-CVILLDEIDklSIGIQ-GDPAS---------AL 461
Cdd:COG1222  135 ELGAPFIR--VRG----SEL---VSKYIGEGARNVREVFELAREKApSIIFIDEID--AIAARrTDDGTsgevqrtvnQL 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446320589 462 LEVLDPEQNKNfrdhyldlpfdisNVFFIATANTLDSISRILL-----DRMEIINLSGYitDEKVQIFQKYL 528
Cdd:COG1222  204 LAELDGFESRG-------------DVLIIAATNRPDLLDPALLrpgrfDRVIEVPLPDE--EAREEILKIHL 260
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
367-524 3.27e-08

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 53.74  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  367 DEKGTILLLvGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRRTyIGSMPGKI------ISALRITKERDCV 440
Cdd:pfam07724   1 RPIGSFLFL-GPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRL-IGAPPGYVgyeeggQLTEAVRRKPYSI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  441 ILLDEIDKLSIGIQgdpaSALLEVLDpeqNKNFRDHYlDLPFDISNVFFIATAN---TLDSISRILLDRMEIINLSGYIT 517
Cdd:pfam07724  79 VLIDEIEKAHPGVQ----NDLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNfgsEKISDASRLGDSPDYELLKEEVM 150

                  ....*..
gi 446320589  518 DEKVQIF 524
Cdd:pfam07724 151 DLLKKGF 157
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
219-506 3.53e-08

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 56.70  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 219 FLKKEIELVSIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGIKDDKFEKKYEKFLERLKNLNADPEVIEEVTRELDK 298
Cdd:COG1401   77 VVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLE 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 299 FSYADPNTGDYNVIRNYLDILESLPWEPAPVREIDLEKAKKTLDKDHYKL-EDVKDRILEFLAVKKLkndekgtiLLLVG 377
Cdd:COG1401  157 ALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKfEETLEAFLAALKTKKN--------VILAG 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 378 PPGVGKTSIARSIAEAMG---RKFFRF-----------SVGGMRDEAEIKGHRRTyigsmPGKIISALRITKE---RDCV 440
Cdd:COG1401  229 PPGTGKTYLARRLAEALGgedNGRIEFvqfhpswsyedFLLGYRPSLDEGKYEPT-----PGIFLRFCLKAEKnpdKPYV 303
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589 441 ILLDEIDKlsigiqGDPA---SALLEVLDPEQNKNFRDHYLDL-----PFDI-SNVFFIATANTLD---SISRILLDR 506
Cdd:COG1401  304 LIIDEINR------ANVEkyfGELLSLLESDKRGEELSIELPYsgegeEFSIpPNLYIIGTMNTDDrslALSDKALRR 375
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
634-757 3.72e-08

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 52.45  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  634 IEALFVKGKGGILLTGMLGKTMEESSNIALSYIKNLLYKeelFNNRMIHLHVPDGATPKDGPSAGITMASAILSLALNTK 713
Cdd:pfam13541   1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFE---FPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQIP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446320589  714 VKSGFGMTGELTLTGEVLAIGGLREKIVAAKRVGIHKIIYPKDN 757
Cdd:pfam13541  78 VLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
373-576 4.25e-08

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 54.89  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFrfsvggmrdeaEIKGHrrTYIGSMPGKIISALRI----TKERDCVILLDEIDk 448
Cdd:COG1223   38 ILFYGPPGTGKTMLAEALAGELKLPLL-----------TVRLD--SLIGSYLGETARNLRKlfdfARRAPCVIFFDEFD- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 449 lSIGIQ-GDPA---------SALLEVLDpeqnknfrdhylDLPfdiSNVFFIATANTLDSISRILLDRM-EIINLSGYIT 517
Cdd:COG1223  104 -AIAKDrGDQNdvgevkrvvNALLQELD------------GLP---SGSVVIAATNHPELLDSALWRRFdEVIEFPLPDK 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446320589 518 DEKVQIFQKYLWKkvlykngvTPYGIEFDKKAIVALIDSYSResgvRGLEKVTDKLVRK 576
Cdd:COG1223  168 EERKEILELNLKK--------FPLPFELDLKKLAKKLEGLSG----ADIEKVLKTALKK 214
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
373-449 1.84e-07

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: 51.52  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFrfsvggmrdeaEIKGHrrTYIGSMPGKIISALRITKER-----DCVILLDEID 447
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFL-----------SISGP--SIVSKYLGESEKNLREIFEEarshaPSIIFIDEID 103

                 ..
gi 446320589 448 KL 449
Cdd:cd19503  104 AL 105
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
373-446 6.56e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 6.56e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFRFS--VGGMrdeAEIKghrrtyigsmpgKIISALRITKE--RDCVILLDEI 446
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSavTSGV---KDLR------------EVIEEARQRRSagRRTILFIDEI 101
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
343-447 1.51e-06

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: 49.15  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 343 KDHYKLEDVKDRILEFlaVKKLKNDEKGTIL--------LLVGPPGVGKTSIARSIAEAMGRKFfrFSVGGmRDEAEIkg 414
Cdd:cd19501    4 KDVAGCEEAKEELKEV--VEFLKNPEKFTKLgakipkgvLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM-- 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446320589 415 hrrtYIGSMPGKIISALRITKERD-CVILLDEID 447
Cdd:cd19501   77 ----FVGVGASRVRDLFEQAKKNApCIVFIDEID 106
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
368-402 2.89e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.44  E-value: 2.89e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446320589 368 EKGTI--LLLVGPPGVGKTSIARSIAEAMGRKFFRFS 402
Cdd:COG2256   45 EAGRLssMILWGPPGTGKTTLARLIANATDAEFVALS 81
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
694-778 6.11e-06

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 49.04  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 694 GPSAGITMASAIL------SLAlNTKVKSGfgmTGELTLTGEVLAIGGLREKIVAAKRVGIHKIIYPKDNlqhLQEIPDY 767
Cdd:COG3480  240 GPSAGLMFALGIYdqltpgDLT-GGKKIAG---TGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---CAEAVGT 312
                         90
                 ....*....|.
gi 446320589 768 VKKGMYFFPVS 778
Cdd:COG3480  313 IPTGLKVVPVD 323
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
349-577 8.25e-06

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 48.45  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  349 EDVKDRILEFLAVKKLKNDEKGTILLLvGPPGVGKTSIARSIAEAMGRKfFRFSVGGMRDEaeikghrrtyigsmPGKII 428
Cdd:TIGR00635  10 EKVKEQLQLFIEAAKMRQEALDHLLLY-GPPGLGKTTLAHIIANEMGVN-LKITSGPALEK--------------PGDLA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  429 SALRITKERDcVILLDEIDKLSigiqgdpaSALLEVLDPE-----------QNKNFRDHYLDLPfdisnVFFIATANT-L 496
Cdd:TIGR00635  74 AILTNLEEGD-VLFIDEIHRLS--------PAVEELLYPAmedfrldivigKGPSARSVRLDLP-----PFTLVGATTrA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  497 DSISRILLDRMEII-NLSGYITDEKVQIFQKYlwKKVLykngvtpyGIEFDKKAIVALidsySRESgvRGLEKVTDKLVR 575
Cdd:TIGR00635 140 GMLTSPLRDRFGIIlRLEFYTVEELAEIVSRS--AGLL--------NVEIEPEAALEI----ARRS--RGTPRIANRLLR 203

                  ..
gi 446320589  576 KI 577
Cdd:TIGR00635 204 RV 205
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
208-384 1.09e-05

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 48.10  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  208 ILKTRIEKVLLFLKKEIELV-----------SIQREISDQIQDKIDKQQRQFFLREQLKAIQNELGIKDDKFEKKYEKFL 276
Cdd:TIGR03499  28 ILSTRKVRKGLFGKKFVEVTaaideeeaaaaSAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  277 ERLKNLNADPEVIEEVTRELDKFSYAdpntgdyNVIRNYLDILESLPWEPAPVREIdLEKAKKTLDKdhyklEDVKDRIL 356
Cdd:TIGR03499 108 ELRKELEALRELLERLLAGLAWLQRP-------PERAKLYERLLEAGVSEELAREL-LEKLPEDADA-----EDAWRWLR 174
                         170       180       190
                  ....*....|....*....|....*....|....
gi 446320589  357 EFLA----VKKLKND--EKGTILLLVGPPGVGKT 384
Cdd:TIGR03499 175 EALEgmlpVKPEEDPilEQGGVIALVGPTGVGKT 208
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
373-449 3.74e-05

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: 45.04  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGM----RDEAEikghrrtyigsmpgKIISALRIT--KERDCVILLDEI 446
Cdd:cd19509   35 ILLYGPPGTGKTLLARAVASESGSTFFSISASSLvskwVGESE--------------KIVRALFALarELQPSIIFIDEI 100

                 ...
gi 446320589 447 DKL 449
Cdd:cd19509  101 DSL 103
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
373-447 6.05e-05

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 44.32  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFRFS----VGGMRDEAEIKGHR--RTYIGSMPgkiisalritkerdCVILLDEI 446
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESEEKIRElfDQAISNAP--------------CIVFIDEI 102

                 .
gi 446320589 447 D 447
Cdd:cd19518  103 D 103
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
349-447 7.36e-05

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 43.95  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 349 EDVKDRIL------EFLAVKKLKNDEKGtiLLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRD----EAEikghrrt 418
Cdd:cd19520   10 TELKELVIlplqrpELFDNSRLLQPPKG--VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDkwygESQ------- 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446320589 419 yigsmpgKIISAL--RITKERDCVILLDEID 447
Cdd:cd19520   81 -------KLVAAVfsLASKLQPSIIFIDEID 104
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
369-467 8.19e-05

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 45.66  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 369 KGTILLLVGPPGVGKTSIARSIAEAM--GRKFFRFSVGGMR--------DEAEIkgHRR-----TYIGSMPGKIISALRI 433
Cdd:COG3598   12 EGGVTLLAGPPGTGKSFLALQLAAAVaaGGPWLGRRVPPGKvlylaaedDRGEL--RRRlkalgADLGLPFADLDGRLRL 89
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446320589 434 TKERDCVILLDEIDKLSIGIQGDPASALleVLDP 467
Cdd:COG3598   90 LSLAGDLDDTDDLEALERAIEEEGPDLV--VIDP 121
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
221-387 8.37e-05

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 45.63  E-value: 8.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 221 KKEIELVSIQREISDqiqdkidkqqrqffLREQLKAIQNELGIKDDKFEKKYEKFLERLKNLNADPEVIEEvtreldkfs 300
Cdd:COG1419   71 AEEEELEELRRELAE--------------LKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARE--------- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 301 yadpntgdynvirnyldILESLPwepapvREIDLEKAKktldkdhyklEDVKDRILEFLAVKKLKNDEKGTILLLVGPPG 380
Cdd:COG1419  128 -----------------LLEKLP------EDLSAEEAW----------RALLEALARRLPVAEDPLLDEGGVIALVGPTG 174

                 ....*...
gi 446320589 381 VGKT-SIA 387
Cdd:COG1419  175 VGKTtTIA 182
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
349-509 1.67e-04

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. 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: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 43.59  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 349 EDVKDRILEFLAVKKL---KNDEKGTI-----LLLVGPPGVGKTSIARSIAEAMG-RKFFRFSVGGMrdeAEIKGHRR-T 418
Cdd:cd19508   23 SNLKSRLLDYVTTTLLfsdKNVNTNLItwnrlVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQL---IEINSHSLfS 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 419 YIGSMPGKIISAL-----RITKERDCVI--LLDEIDklSIGIQGDPASALLEVLDPEQNKNFRDHYLDLPFDISNVFFIA 491
Cdd:cd19508  100 KWFSESGKLVTKMfqkiqELIDDKDALVfvLIDEVE--SLAAARSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILL 177
                        170
                 ....*....|....*...
gi 446320589 492 TANTLDSISRILLDRMEI 509
Cdd:cd19508  178 TSNLLEKIDVAFVDRADI 195
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
373-449 2.40e-04

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. 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: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 43.05  E-value: 2.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEAEIKGHRrtyigsMPGKIISALRItkERDCVILLDEIDKL 449
Cdd:cd19525   58 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK------MVRALFSVARC--KQPAVIFIDEIDSL 126
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
375-399 2.48e-04

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: 42.42  E-value: 2.48e-04
                         10        20
                 ....*....|....*....|....*
gi 446320589 375 LVGPPGVGKTSIARSIAEAMGRKFF 399
Cdd:COG0703    3 LIGMMGAGKSTVGRLLAKRLGLPFV 27
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
369-499 4.19e-04

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: 41.59  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 369 KGtiLLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEaeikghrrtYIGSMPGKIISALRITKE-RDCVILLDEID 447
Cdd:cd19507   32 KG--LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG---------LVGESESRLRQMIQTAEAiAPCVLWIDEIE 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446320589 448 KL--SIGIQGD--PASALL-EVLDPEQNKnfrdhyldlpfdISNVFFIATANTLDSI 499
Cdd:cd19507  101 KGfsNADSKGDsgTSSRVLgTFLTWLQEK------------KKPVFVVATANNVQSL 145
aroK PRK00131
shikimate kinase; Reviewed
369-399 4.90e-04

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 41.71  E-value: 4.90e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446320589 369 KGTILLLVGPPGVGKTSIARSIAEAMGRKFF 399
Cdd:PRK00131   3 KGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
693-789 4.93e-04

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 43.78  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 693 DGPSAGITMASAILSlAL-NTKVKSGFGMTGELTLTGEVLAIGGLREKI-----VAAKR--VGIHKIIYPKDNLQHL--- 761
Cdd:COG1067  592 DGDSASSAELYALLS-ALsGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARglTGKQGVIIPAANVKNLmlr 670
                         90       100
                 ....*....|....*....|....*....
gi 446320589 762 QEIPDYVKKGMYF-FPVSRYEEVALLLFD 789
Cdd:COG1067  671 DEVVEAVKAGQFHiYAVEHVDEAIELLTG 699
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
374-450 5.68e-04

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 41.11  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 374 LLVGPPGVGKTSIARSIAEAMGRKFfrFSVGGmrdeAEIKGhrrTYIGSMPGKIISALRitKERD---CVILLDEIDKLS 450
Cdd:cd19511   31 LLYGPPGCGKTLLAKALASEAGLNF--ISVKG----PELFS---KYVGESERAVREIFQ--KARQaapCIIFFDEIDSLA 99
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
373-498 6.03e-04

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: 40.62  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  373 LLLVGPPGVGKTSIARSIAEAMGRKFFR--FSVGGMrdEAEIKG-------HRRTYIgsMPGKIISAlritkerdcVILL 443
Cdd:pfam07726   2 VLLEGVPGLAKTLLVRTLARSLGLDFRRiqFTPDLL--PSDITGtevfdqkTREFEF--RPGPVFAN---------VLLA 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446320589  444 DEIDKLSIGIQgdpaSALLEVLDPEQ-NKNFRDHYLDLPFdisnvFFIATANTLDS 498
Cdd:pfam07726  69 DEINRAPPKTQ----SALLEAMQERQvTIDGETHPLPEPF-----FVLATQNPIEQ 115
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
375-399 6.38e-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: 41.00  E-value: 6.38e-04
                         10        20
                 ....*....|....*....|....*
gi 446320589 375 LVGPPGVGKTSIARSIAEAMGRKFF 399
Cdd:cd00464    4 LIGMMGAGKTTVGRLLAKALGLPFV 28
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
374-494 1.18e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.52  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 374 LLVGPPGVGKTSIARSIAEAMGRKFFRFsvggmrDEAEIkGHRRT---YIGSMPGKI------ISALRITKERDCVILLD 444
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdqggLLTDAVIKHPHAVLLLD 564
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446320589 445 EIDKlsigIQGDPASALLEVLDpeqNKNFRDHYlDLPFDISNVFFIATAN 494
Cdd:PRK11034 565 EIEK----AHPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 606
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
368-397 1.21e-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: 40.87  E-value: 1.21e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 446320589 368 EKGTILLLVGPPGVGKTSIARSIAEAMGRK 397
Cdd:COG4088    2 DSPMLLILTGPPGSGKTTFAKALAQRLYAE 31
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
373-450 1.41e-03

first of two ATPase domains of CDC48 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. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 40.11  E-value: 1.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFfrFSVGGmrdeAEIKGhrrTYIGSMPGKIISALRITKERD-CVILLDEIDKLS 450
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFF--FLING----PEIMS---KLAGESESNLRKAFEEAEKNApAIIFIDEIDAIA 106
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
333-411 1.74e-03

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. 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: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 39.97  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 333 DLEKAKKTLDkdhyklEDVKDRILEFLAVKKLKNDEKGtiLLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGM----RD 408
Cdd:cd19522    4 DLEEAKKLLE------EAVVLPMWMPEFFKGIRRPWKG--VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLtskyRG 75

                 ...
gi 446320589 409 EAE 411
Cdd:cd19522   76 ESE 78
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
342-394 1.75e-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: 41.51  E-value: 1.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 446320589   342 DKDHYKLEDVKDRILEFLAVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAM 394
Cdd:smart00763  50 DHDFFGMEEAIERFVNYFKSAAQGLEERKQILYLLGPVGGGKSSLVECLKRGL 102
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
373-504 1.77e-03

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 39.80  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFrfsvggmrdeaEIKGHR--RTYIGSMPGKIISAL-RITKERDCVILLDEIDKL 449
Cdd:cd19527   29 ILLYGPPGTGKTLLAKAIATECSLNFL-----------SVKGPEliNMYIGESEANVREVFqKARDAKPCVIFFDELDSL 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446320589 450 --SIGIQGDPA-------SALLEVLDPEQNKNfrdhyldlpfdiSNVFFIATANTLDSISRILL 504
Cdd:cd19527   98 apSRGNSGDSGgvmdrvvSQLLAELDGMSSSG------------QDVFVIGATNRPDLLDPALL 149
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
373-499 1.78e-03

second 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: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 39.78  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFfrFSVGGmrdeAEIkghRRTYIGSMPGKIISA-LRITKERDCVILLDEIDKLSI 451
Cdd:cd19530   33 VLLYGPPGCGKTLLAKAVANESGANF--ISVKG----PEL---LNKYVGESERAVRQVfQRARASAPCVIFFDEVDALVP 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446320589 452 GIQGDPASALLEVLDPEQNKnfrdhyLDLPFDISNVFFIATANTLDSI 499
Cdd:cd19530  104 KRGDGGSWASERVVNQLLTE------MDGLEERSNVFVIAATNRPDII 145
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
373-450 1.91e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.27  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFfrfsvggmrdeaeikghrRTYIGSM---PGKIISALRITKERDcVILLDEIDKL 449
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNI------------------RITSGPAlekPGDLAAILTNLEEGD-VLFIDEIHRL 114

                 .
gi 446320589 450 S 450
Cdd:PRK00080 115 S 115
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
374-452 2.11e-03

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 40.01  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 374 LLVGPPGVGKTSIARSIAEAMGRKFFRfsVGGmrdeAEIKghrRTYIGSMPGKIISALRITKERD-CVILLDEIDklSIG 452
Cdd:cd19502   41 LLYGPPGTGKTLLAKAVANHTDATFIR--VVG----SELV---QKYIGEGARLVRELFEMAREKApSIIFIDEID--AIG 109
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
348-513 2.16e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.11  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 348 LEDVKDRILEFLAVKKLKNDekgtiLLLVGPPGVGKTSIARSIAEAMG------------RKFFRFSVGGMRD----EAE 411
Cdd:COG0470    1 QEEAWEQLLAAAESGRLPHA-----LLLHGPPGIGKTTLALALARDLLcenpeggkacgqCHSRLMAAGNHPDllelNPE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 412 IKGHRRTyIGSMPgKIISALRIT------KerdcVILLDEIDKLSigiqGDPASALLEVL-DPeqnknfrdhyldlpfdI 484
Cdd:COG0470   76 EKSDQIG-IDQIR-ELGEFLSLTpleggrK----VVIIDEADAMN----EAAANALLKTLeEP----------------P 129
                        170       180
                 ....*....|....*....|....*....
gi 446320589 485 SNVFFIATANTLDSISRILLDRMEIINLS 513
Cdd:COG0470  130 KNTPFILIANDPSRLLPTIRSRCQVIRFR 158
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
370-404 2.50e-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: 39.41  E-value: 2.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446320589  370 GTILLLVGPPGVGKTSIARSIAEAMGRKFFRFSVG 404
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
336-466 2.54e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 40.51  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  336 KAKKTLDK-DHYKLEDVKDRILEFLAvkKLKNDEKGTILLLVGPPGVGKTSIARSIAEA---MGRKFFRFSVGGMRDEAE 411
Cdd:pfam01695  59 PPHKTLEDfDFTFAPGLDQRIVAELA--SLSFIDRAQNVVLLGPPGVGKTHLAIALGVEacrAGYSVRFTSAADLVNQLK 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446320589  412 IKGHRrtyiGSMPGKIISALRITkerdcVILLDEIDKLSIgiqgDPASA--LLEVLD 466
Cdd:pfam01695 137 RAHGD----GKLTRKLQQLLKPD-----VLILDEWGYLPL----DQAEAnlLFQVIS 180
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
377-410 3.48e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 38.62  E-value: 3.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446320589 377 GPPGVGKTSIARSIAEAMGRKFfrFSVGGMRDEA 410
Cdd:cd02020    6 GPAGSGKSTVAKLLAKKLGLPY--LDTGGIRTEE 37
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
373-395 4.86e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|...
gi 446320589  373 LLLVGPPGVGKTSIARSIAEAMG 395
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMG 58
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
355-399 5.07e-03

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 40.41  E-value: 5.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446320589 355 ILEFLavkklKNDEK-----GTI---LLLVGPPGVGKTSIARSIA-EAmGRKFF 399
Cdd:COG0465  157 IVDFL-----KDPEKftrlgAKIpkgVLLVGPPGTGKTLLAKAVAgEA-GVPFF 204
KaiC-like_C cd19487
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
368-411 6.06e-03

C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410895 [Multi-domain]  Cd Length: 219  Bit Score: 39.20  E-value: 6.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446320589 368 EKGTILLLVGPPGVGKTSIARSIAEAMGRK-----FFRF--SVGGMRDEAE 411
Cdd:cd19487   17 ERGTSTLLIGPAGVGKSTLALQFAKAAAARgersvLFSFdeSIGTLFERSE 67
Sigma54_activat pfam00158
Sigma-54 interaction domain;
374-474 6.72e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 38.15  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589  374 LLVGPPGVGKTSIARSIAEAMGRK---FFRFSVGGMRD---EAEIKGHRR-TYIG---SMPGKIISALRITkerdcvILL 443
Cdd:pfam00158  26 LITGESGTGKELFARAIHQLSPRAdgpFVAVNCAAIPEellESELFGHEKgAFTGadsDRKGLFELADGGT------LFL 99
                          90       100       110
                  ....*....|....*....|....*....|.
gi 446320589  444 DEIDKLSIGIQgdpaSALLEVLdpeQNKNFR 474
Cdd:pfam00158 100 DEIGELPLELQ----AKLLRVL---QEGEFE 123
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
373-449 7.30e-03

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 38.29  E-value: 7.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFFRFSVGGMRDEaeikghrrtYIGSMPgKIISAL-RITKERD-CVILLDEIDKL 449
Cdd:cd19524   36 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK---------YVGEGE-KLVRALfAVARELQpSIIFIDEVDSL 104
PRK04195 PRK04195
replication factor C large subunit; Provisional
349-395 7.57e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 39.52  E-value: 7.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446320589 349 EDVKDRILEFlaVKKLKNDEKGTILLLVGPPGVGKTSIARSIAEAMG 395
Cdd:PRK04195  20 EKAKEQLREW--IESWLKGKPKKALLLYGPPGVGKTSLAHALANDYG 64
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
373-398 8.05e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 8.05e-03
                         10        20
                 ....*....|....*....|....*.
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKF 398
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
364-446 8.19e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 39.54  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 364 LKNDEKGTILLLVGPPGVGKTSIARSIAEAMgRKFFRFSVggmrDEAEIkghrRTYIGSMPGKIISALRITKERDCVILL 443
Cdd:COG1373   14 LKLLDNRKAVVITGPRQVGKTTLLKQLAKEL-ENILYINL----DDPRL----RALAEEDPDDLLEALKELYPGKTYLFL 84

                 ...
gi 446320589 444 DEI 446
Cdd:COG1373   85 DEI 87
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
373-463 8.62e-03

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. 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: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446320589 373 LLLVGPPGVGKTSIARSIAEAMGRKFfrFSVGGmrdeAEIKGHrrtYIGSMPGKIISALRITKE-RDCVILLDEIDKLSI 451
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANF--ISVKG----PELLSK---WVGESEKAIREIFRKARQvAPCVIFFDEIDSIAP 100
                         90
                 ....*....|..
gi 446320589 452 GIQGDPASALLE 463
Cdd:cd19529  101 RRGTTGDSGVTE 112
 
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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