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Conserved domains on  [gi|1804231588|ref|WP_161864573|]
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endopeptidase La [Pseudomonas yangonensis]

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, ...
25-797 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1159.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  25 PAQQFPDKLYIIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFVDTPPDEHGEfdlDSLPEHGTLVRVHH 104
Cdd:COG0466     6 EEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGP---DDLYEVGTVAKILQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 105 VSE-EGGKLQFVAQGLTRVRIRGWLSRRGPYLAEVEYPQAPNDPRDEVKAYGMALINAIKELLPLNPLYSEELKNYLNrf 183
Cdd:COG0466    83 LLKlPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALS-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 184 SPNDPSPLTDFAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLI 263
Cdd:COG0466   161 NIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 264 QQELGiSKDDKSADREEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRA 343
Cdd:COG0466   241 QKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 344 RKVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRR 423
Cdd:COG0466   320 EKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 424 TYIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLD 503
Cdd:COG0466   400 TYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLD 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 504 SIPGPLLDRMEVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKS 583
Cdd:COG0466   480 TIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 584 VVKLLEDPEAKIRIGTKDLEETLGMPVFRNERVL--AGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQLGEVMK 661
Cdd:COG0466   560 AKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEeeDQVGVVTGLAWTEVGGDILFIEATLMPG-KGKLTLTGQLGDVMK 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 662 ESAEIAYSYVSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLP 741
Cdd:COG0466   639 ESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLP 718
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1804231588 742 IGGVREKVIAARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:COG0466   719 IGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
25-797 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1159.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  25 PAQQFPDKLYIIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFVDTPPDEHGEfdlDSLPEHGTLVRVHH 104
Cdd:COG0466     6 EEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGP---DDLYEVGTVAKILQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 105 VSE-EGGKLQFVAQGLTRVRIRGWLSRRGPYLAEVEYPQAPNDPRDEVKAYGMALINAIKELLPLNPLYSEELKNYLNrf 183
Cdd:COG0466    83 LLKlPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALS-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 184 SPNDPSPLTDFAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLI 263
Cdd:COG0466   161 NIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 264 QQELGiSKDDKSADREEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRA 343
Cdd:COG0466   241 QKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 344 RKVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRR 423
Cdd:COG0466   320 EKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 424 TYIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLD 503
Cdd:COG0466   400 TYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLD 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 504 SIPGPLLDRMEVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKS 583
Cdd:COG0466   480 TIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 584 VVKLLEDPEAKIRIGTKDLEETLGMPVFRNERVL--AGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQLGEVMK 661
Cdd:COG0466   560 AKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEeeDQVGVVTGLAWTEVGGDILFIEATLMPG-KGKLTLTGQLGDVMK 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 662 ESAEIAYSYVSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLP 741
Cdd:COG0466   639 ESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLP 718
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1804231588 742 IGGVREKVIAARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:COG0466   719 IGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
35-797 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: 915.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  35 IIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFV-DTPPDEHGEFDLDSLpehGTLVRVHHV----SEEG 109
Cdd:TIGR00763   2 LLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQkDDDNEEPEEDDIYSV---GVVAQILEMlplpSSGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 110 GKLQFVAQGLTRVRIRGWLSRRGPYLAEVEY----PQAPNDPrdEVKAYGMALINAIKELLPLNPLYSEELKNYLNRFSP 185
Cdd:TIGR00763  79 ATYKVVVEGLRRIRIKELSDKGGYLVVRVDNlkeePFDKDDE--EIKALTREIKETFRELISLSKLFREQPALLSALEDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 186 NDPSPLTDFAAALTTAPGH-ELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLIQ 264
Cdd:TIGR00763 157 DEPGRLADFVAASLQLKEKdELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 265 QELGISKDDKSADrEEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRAR 344
Cdd:TIGR00763 237 KELGIEKDDKDEL-EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 345 KVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRT 424
Cdd:TIGR00763 316 EILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 425 YIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLDS 504
Cdd:TIGR00763 396 YVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDT 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 505 IPGPLLDRMEVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKSV 584
Cdd:TIGR00763 476 IPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 585 VKLLEDPEAK------IRIGTKDLEETLGMPVFRNERV--LAGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQL 656
Cdd:TIGR00763 556 VKLVEQGEKKkseaesVVITPDNLKKYLGKPVFTYERAyeVTPPGVVMGLAWTPMGGDTLFIETTKVAG-KGSLELTGQL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 657 GEVMKESAEIAYSYVSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLT 736
Cdd:TIGR00763 635 GDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLR 714
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804231588 737 GQVLPIGGVREKVIAARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:TIGR00763 715 GKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
35-792 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 602.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  35 IIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFVDTPPDEHGEFDLDSLPEHGTLVRVHHVSEegGKLQF 114
Cdd:PRK10787   13 VLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPD--GTVKV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 115 VAQGLTRVRIRGwLSRRGPYL-AEVEYPQAPNDPRDEVKAYGMALINAIKELLPLNPLYSEELKNYLNrfSPNDPSPLTD 193
Cdd:PRK10787   91 LVEGLQRARISA-LSDNGEHFsAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLN--SIDDPARLAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 194 FAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLIQQELGiSKDD 273
Cdd:PRK10787  168 TIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG-EMDD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 274 KSADREEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRARKVLDKHHAG 353
Cdd:PRK10787  247 APDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 354 MDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRTYIGAMPGKL 433
Cdd:PRK10787  327 LERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 434 VQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLDsIPGPLLDRM 513
Cdd:PRK10787  407 IQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDRM 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 514 EVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKSVVKLLEDPEA 593
Cdd:PRK10787  486 EVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSL 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 594 K-IRIGTKDLEETLGMPVFRNERVLAG--VGVITGLAWTSMGGATLPIEATRIHTLNRgFKLTGQLGEVMKESAEIAYSY 670
Cdd:PRK10787  566 KhIEINGDNLHDYLGVQRFDYGRADNEnrVGQVTGLAWTEVGGDLLTIETACVPGKGK-LTYTGSLGEVMQESIQAALTV 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 671 VSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLPIGGVREKVI 750
Cdd:PRK10787  645 VRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLL 724
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|..
gi 1804231588 751 AARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDV 792
Cdd:PRK10787  725 AAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEV 766
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
340-521 1.09e-121

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 363.42  E-value: 1.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 340 LGRARKVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIK 419
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 420 GHRRTYIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTA 499
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                         170       180
                  ....*....|....*....|..
gi 1804231588 500 NTLDSIPGPLLDRMEVIRLSGY 521
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
597-797 1.31e-99

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: 306.86  E-value: 1.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 597 IGTKDLEETLGMPVFRNERV--LAGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQLGEVMKESAEIAYSYVSSH 674
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAekEDQVGVVTGLAWTEVGGDLLTIEAVIMPG-KGKLTLTGQLGDVMKESAQAALSYVRSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 675 LKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLPIGGVREKVIAARR 754
Cdd:pfam05362  81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1804231588 755 QKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
376-512 9.78e-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: 54.69  E-value: 9.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  376 GSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRTYIGAMPGKLV--------QALKEAEVMNP-V 446
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrlrLALALARKLKPdV 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804231588  447 IMLDEIDKMgtsyqGDPASALLEtldpeqNVEFLDHYLDLRLDLSKVLFVCTANTL-DSIPGPLLDR 512
Cdd:smart00382  82 LILDEITSL-----LDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEkDLGPALLRRR 137
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
25-797 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1159.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  25 PAQQFPDKLYIIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFVDTPPDEHGEfdlDSLPEHGTLVRVHH 104
Cdd:COG0466     6 EEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGP---DDLYEVGTVAKILQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 105 VSE-EGGKLQFVAQGLTRVRIRGWLSRRGPYLAEVEYPQAPNDPRDEVKAYGMALINAIKELLPLNPLYSEELKNYLNrf 183
Cdd:COG0466    83 LLKlPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALS-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 184 SPNDPSPLTDFAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLI 263
Cdd:COG0466   161 NIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 264 QQELGiSKDDKSADREEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRA 343
Cdd:COG0466   241 QKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 344 RKVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRR 423
Cdd:COG0466   320 EKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 424 TYIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLD 503
Cdd:COG0466   400 TYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLD 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 504 SIPGPLLDRMEVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKS 583
Cdd:COG0466   480 TIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 584 VVKLLEDPEAKIRIGTKDLEETLGMPVFRNERVL--AGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQLGEVMK 661
Cdd:COG0466   560 AKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEeeDQVGVVTGLAWTEVGGDILFIEATLMPG-KGKLTLTGQLGDVMK 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 662 ESAEIAYSYVSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLP 741
Cdd:COG0466   639 ESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLP 718
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1804231588 742 IGGVREKVIAARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:COG0466   719 IGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
35-797 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: 915.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  35 IIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFV-DTPPDEHGEFDLDSLpehGTLVRVHHV----SEEG 109
Cdd:TIGR00763   2 LLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQkDDDNEEPEEDDIYSV---GVVAQILEMlplpSSGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 110 GKLQFVAQGLTRVRIRGWLSRRGPYLAEVEY----PQAPNDPrdEVKAYGMALINAIKELLPLNPLYSEELKNYLNRFSP 185
Cdd:TIGR00763  79 ATYKVVVEGLRRIRIKELSDKGGYLVVRVDNlkeePFDKDDE--EIKALTREIKETFRELISLSKLFREQPALLSALEDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 186 NDPSPLTDFAAALTTAPGH-ELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLIQ 264
Cdd:TIGR00763 157 DEPGRLADFVAASLQLKEKdELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 265 QELGISKDDKSADrEEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRAR 344
Cdd:TIGR00763 237 KELGIEKDDKDEL-EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 345 KVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRT 424
Cdd:TIGR00763 316 EILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 425 YIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLDS 504
Cdd:TIGR00763 396 YVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDT 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 505 IPGPLLDRMEVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKSV 584
Cdd:TIGR00763 476 IPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 585 VKLLEDPEAK------IRIGTKDLEETLGMPVFRNERV--LAGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQL 656
Cdd:TIGR00763 556 VKLVEQGEKKkseaesVVITPDNLKKYLGKPVFTYERAyeVTPPGVVMGLAWTPMGGDTLFIETTKVAG-KGSLELTGQL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 657 GEVMKESAEIAYSYVSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLT 736
Cdd:TIGR00763 635 GDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLR 714
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804231588 737 GQVLPIGGVREKVIAARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:TIGR00763 715 GKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
35-792 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 602.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  35 IIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCMAVFFVDTPPDEHGEFDLDSLPEHGTLVRVHHVSEegGKLQF 114
Cdd:PRK10787   13 VLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPD--GTVKV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 115 VAQGLTRVRIRGwLSRRGPYL-AEVEYPQAPNDPRDEVKAYGMALINAIKELLPLNPLYSEELKNYLNrfSPNDPSPLTD 193
Cdd:PRK10787   91 LVEGLQRARISA-LSDNGEHFsAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLN--SIDDPARLAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 194 FAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLIQQELGiSKDD 273
Cdd:PRK10787  168 TIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG-EMDD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 274 KSADREEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRARKVLDKHHAG 353
Cdd:PRK10787  247 APDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 354 MDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRTYIGAMPGKL 433
Cdd:PRK10787  327 LERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 434 VQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLDsIPGPLLDRM 513
Cdd:PRK10787  407 IQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDRM 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 514 EVIRLSGYITEEKLAIAKRHLWPKQLEKAGVPKARLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKSVVKLLEDPEA 593
Cdd:PRK10787  486 EVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSL 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 594 K-IRIGTKDLEETLGMPVFRNERVLAG--VGVITGLAWTSMGGATLPIEATRIHTLNRgFKLTGQLGEVMKESAEIAYSY 670
Cdd:PRK10787  566 KhIEINGDNLHDYLGVQRFDYGRADNEnrVGQVTGLAWTEVGGDLLTIETACVPGKGK-LTYTGSLGEVMQESIQAALTV 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 671 VSSHLKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLPIGGVREKVI 750
Cdd:PRK10787  645 VRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLL 724
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|..
gi 1804231588 751 AARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDV 792
Cdd:PRK10787  725 AAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEV 766
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
340-521 1.09e-121

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 363.42  E-value: 1.09e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 340 LGRARKVLDKHHAGMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIK 419
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 420 GHRRTYIGAMPGKLVQALKEAEVMNPVIMLDEIDKMGTSYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTA 499
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                         170       180
                  ....*....|....*....|..
gi 1804231588 500 NTLDSIPGPLLDRMEVIRLSGY 521
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
597-797 1.31e-99

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: 306.86  E-value: 1.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 597 IGTKDLEETLGMPVFRNERV--LAGVGVITGLAWTSMGGATLPIEATRIHTlNRGFKLTGQLGEVMKESAEIAYSYVSSH 674
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAekEDQVGVVTGLAWTEVGGDLLTIEAVIMPG-KGKLTLTGQLGDVMKESAQAALSYVRSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 675 LKQFGGDPSFFDQAFVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLPIGGVREKVIAARR 754
Cdd:pfam05362  81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1804231588 755 QKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYGDVAKVLF 797
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
379-521 1.84e-31

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: 119.24  E-value: 1.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDeaeikghrrTYIGAMPGKLVQALKEAEVMNP-VIMLDEIDKMGT 457
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804231588 458 SYQG-------DPASALLETLDPEQNVEfldhyldlrldlSKVLFVCTANTLDSIPGPLLDRMEVIRLSGY 521
Cdd:pfam00004  72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
35-228 3.78e-25

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: 103.57  E-value: 3.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  35 IIPIHNRPFFPAQVLPVIVNQQPWGRTLTRVGNTEHKCmAVFFVDTPPDEHGEFDLDSLPEHGTLVRVHHVSE-EGGKLQ 113
Cdd:pfam02190   4 LLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLY-GVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKlPDGTYK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 114 FVAQGLTRVRIRGWLSRRGPYL-AEVEY-PQAPNDPRDEVKAYGMALINAIKELLPLNPLYsEELKNYLNrfsPNDPSPL 191
Cdd:pfam02190  83 VLVEGLERVRIVELVKKEEPYLrAEVEDlPEDSDELSEALKALVKELIEKLRRLLKLLLPL-ELLLKIKD---IENPGRL 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1804231588 192 TDFAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRK 228
Cdd:pfam02190 159 ADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
191-578 7.19e-19

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: 89.59  E-value: 7.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 191 LTDFAAALTTAPGHELQEVLDTVPMLKRMEKVLPLLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLIQQELGIS 270
Cdd:COG0464     1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 271 KDDKSADREEFLARLEGKTLSAPAQKRIDEELNKLSILETGSPEYAVTRnyLDWATALPWGIHGQDKLDLGRARKVLDKH 350
Cdd:COG0464    81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEAL--ALAAPLVTYEDIGGLEEELLELREAILDD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 351 HAGMDDIKQRITEFLA-------VGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEaeikghrr 423
Cdd:COG0464   159 LGGLEEVKEELRELVAlplkrpeLREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK-------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 424 tYIGAMPGKLVQALKEAEVMNP-VIMLDEIDKMG---TSYQGDPASALLETLdpeqnVEFLDhylDLRldlSKVLFVCTA 499
Cdd:COG0464   231 -YVGETEKNLREVFDKARGLAPcVLFIDEADALAgkrGEVGDGVGRRVVNTL-----LTEME---ELR---SDVVVIAAT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 500 NTLDSIPGPLLDRM-EVIRLSGYITEEKLAIAKRHLWPKQLEK----AGVPKARLSISDAALRAVIEgYAREAGVRQLEK 574
Cdd:COG0464   299 NRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDEdvdlEELAEATEGLSGADIRNVVR-RAALQALRLGRE 377

                  ....
gi 1804231588 575 QLGK 578
Cdd:COG0464   378 PVTT 381
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
355-512 1.62e-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: 80.40  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 355 DDIKQRITEFLAVGAF--KGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEaeikghrrtYIGAMPGK 432
Cdd:cd19481     3 ASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK---------YVGESEKN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 433 LVQALKEAEVMNP-VIMLDEIDKMG--TSYQGDPA------SALLETLDPEQNvefldhyldlrldLSKVLFVCTANTLD 503
Cdd:cd19481    74 LRKIFERARRLAPcILFIDEIDAIGrkRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNRPD 140

                  ....*....
gi 1804231588 504 SIPGPLLDR 512
Cdd:cd19481   141 LLDPALLRP 149
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
657-790 1.48e-16

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 79.25  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 657 GEVMKESAEIAySYVSSHLKqfGGDPSFFDqafVHLHVPEGATPKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLT 736
Cdd:COG1750    69 GPDTQASARIA-ALVASLLA--GVDLSSYD---VYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPD 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1804231588 737 GQVLPIGGVREKVIAARRQKIFELILPEANRGSYEELPDYLKEGLTVHFAKRYG 790
Cdd:COG1750   143 GSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTGYNTQVGETVDLVEYGKELG 196
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
352-516 3.84e-13

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: 67.56  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITEFLAVGAFKGeiagsiVLLVGPPGVGKTSIGKSIAESLGRPFYRF---SVGGMRDEAEIKGHRRTYIGA 428
Cdd:cd00009     1 VGQEEAIEALREALELPPPKN------LLLYGPPGTGKTTLARAIANELFRPGAPFlylNASDLLEGLVVAELFGHFLVR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 429 MPGKLVQALKeaevmNPVIMLDEIDKMGTSYQgdpasalletldpEQNVEFLDHYLDLRLDLSKVLFVCTAN--TLDSIP 506
Cdd:cd00009    75 LLFELAEKAK-----PGVLFIDEIDSLSRGAQ-------------NALLRVLETLNDLRIDRENVRVIGATNrpLLGDLD 136
                         170
                  ....*....|
gi 1804231588 507 GPLLDRMEVI 516
Cdd:cd00009   137 RALYDRLDIR 146
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
379-510 2.63e-09

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: 56.99  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEaeikghrrtYIGAMPGKLVQALKEAEVMNPVIML-DEIDKM-- 455
Cdd:cd19507    34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG---------LVGESESRLRQMIQTAEAIAPCVLWiDEIEKGfs 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1804231588 456 GTSYQGD--PASALLETldpeqnveFLDHyldLRLDLSKVLFVCTANTLDSIPGPLL 510
Cdd:cd19507   105 NADSKGDsgTSSRVLGT--------FLTW---LQEKKKPVFVVATANNVQSLPPELL 150
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
379-513 3.05e-09

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 55.76  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESL-GRPFyrFSVGGMRD--EAEIKGHRRTYIGAM---PGKLVQALKEAEvmnpVIMLDEI 452
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPV--FYVQLTRDttEEDLFGRRNIDPGGAswvDGPLVRAAREGE----IAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804231588 453 DKMGTSYQGdpasALLETLDPEQ-NVEFLDHYLDLRLDlsKVLFVCTANTLD----SIPGPLLDRM 513
Cdd:pfam07728  76 NRANPDVLN----SLLSLLDERRlLLPDGGELVKAAPD--GFRLIATMNPLDrglnELSPALRSRF 135
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
703-783 5.52e-09

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 58.67  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 703 GPSAGITMASALL------SLARNQApkkgVAMTGELTLTGQVLPIGGVREKVIAARRQ--KIFelILPEANrgsYEELP 774
Cdd:COG3480   240 GPSAGLMFALGIYdqltpgDLTGGKK----IAGTGTIDADGTVGPIGGIDQKVVAARRAgaTIF--LAPASN---CAEAV 310

                  ....*....
gi 1804231588 775 DYLKEGLTV 783
Cdd:COG3480   311 GTIPTGLKV 319
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
353-606 6.99e-09

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 57.20  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 353 GMDDIKQRITEFLA-------VGAFKGEIAGSIvLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEaeikghrrtY 425
Cdd:COG1223     6 GQEEAKKKLKLIIKelrrrenLRKFGLWPPRKI-LFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------Y 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 426 IGAMPGKLVQALKEAEVMNPVIMLDEIDKMGT--SYQGDPA------SALLetldpeQNVEFLDhyldlrldlSKVLFVC 497
Cdd:COG1223    76 LGETARNLRKLFDFARRAPCVIFFDEFDAIAKdrGDQNDVGevkrvvNALL------QELDGLP---------SGSVVIA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 498 TANTLDSIPGPLLDRM-EVIRLSGYITEEKLAIAKRHLWPKQLEKAgvpkarlsISDAALRAVIEGYAReagvRQLEKQL 576
Cdd:COG1223   141 ATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNLKKFPLPFE--------LDLKKLAKKLEGLSG----ADIEKVL 208
                         250       260       270
                  ....*....|....*....|....*....|
gi 1804231588 577 GKLVRKSVvklLEDPEAkirIGTKDLEETL 606
Cdd:COG1223   209 KTALKKAI---LEDREK---VTKEDLEEAL 232
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
376-512 9.78e-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: 54.69  E-value: 9.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588  376 GSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRTYIGAMPGKLV--------QALKEAEVMNP-V 446
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgelrlrLALALARKLKPdV 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804231588  447 IMLDEIDKMgtsyqGDPASALLEtldpeqNVEFLDHYLDLRLDLSKVLFVCTANTL-DSIPGPLLDR 512
Cdd:smart00382  82 LILDEITSL-----LDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEkDLGPALLRRR 137
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
352-458 2.81e-08

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 56.17  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITE-----------FLAVGAF--KGeiagsiVLLVGPPGVGKTSIGKSIAESLGRPFYRfsVGGmrdeAEI 418
Cdd:COG1222    81 GGLDEQIEEIREavelplknpelFRKYGIEppKG------VLLYGPPGTGKTLLAKAVAGELGAPFIR--VRG----SEL 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1804231588 419 kghRRTYIGAMPGKLVQALKEAEVMNP-VIMLDEIDKMGTS 458
Cdd:COG1222   149 ---VSKYIGEGARNVREVFELAREKAPsIIFIDEIDAIAAR 186
ftsH CHL00176
cell division protein; Validated
352-456 1.21e-07

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 55.44  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITE----------FLAVGA--FKGeiagsiVLLVGPPGVGKTSIGKSIAESLGRPFyrFSVGGmrdeAEIk 419
Cdd:CHL00176  186 AGIEEAKEEFEEvvsflkkperFTAVGAkiPKG------VLLVGPPGTGKTLLAKAIAGEAEVPF--FSISG----SEF- 252
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1804231588 420 ghRRTYIGAMPGKLVQALKEAEVMNPVIM-LDEIDKMG 456
Cdd:CHL00176  253 --VEMFVGVGAARVRDLFKKAKENSPCIVfIDEIDAVG 288
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
352-456 1.61e-07

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: 51.85  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITE----------FLAVGAF--KGeiagsiVLLVGPPGVGKTSIGKSIAESLGRPFyrFSVGGmRDEAEIk 419
Cdd:cd19501     7 AGCEEAKEELKEvveflknpekFTKLGAKipKG------VLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM- 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1804231588 420 ghrrtYIGAMPGKLVQALKEAEVMNP-VIMLDEIDKMG 456
Cdd:cd19501    77 -----FVGVGASRVRDLFEQAKKNAPcIVFIDEIDAVG 109
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
352-514 1.93e-07

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: 51.58  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITE-----FLAVGAFKGEIA-GSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGM----RDEAEikgh 421
Cdd:cd19509     2 AGLDDAKEALKEavilpSLRPDLFPGLRGpPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLvskwVGESE---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 422 rrtyigampgKLVQALKE-AEVMNP-VIMLDEIDKMGTSYQGDP--ASALLETldpeqnvEFLDHyLD--LRLDLSKVLF 495
Cdd:cd19509    78 ----------KIVRALFAlARELQPsIIFIDEIDSLLSERGSGEheASRRVKT-------EFLVQ-MDgvLNKPEDRVLV 139
                         170
                  ....*....|....*....
gi 1804231588 496 VCTANTLDSIPGPLLDRME 514
Cdd:cd19509   140 LGATNRPWELDEAFLRRFE 158
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
379-469 6.34e-07

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: 51.71  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYR--FSVGGMrdEAEIKGH-------RRTYIgaMPGKLVQalkeaevmnPVIML 449
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRiqFTPDLL--PSDILGTyiydqqtGEFEF--RPGPLFA---------NVLLA 100
                          90       100
                  ....*....|....*....|..
gi 1804231588 450 DEIDKmgtsyqGDPA--SALLE 469
Cdd:COG0714   101 DEINR------APPKtqSALLE 116
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
352-453 1.18e-06

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: 49.21  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITEFLAVGAFKGEIAGSI-------VLLVGPPGVGKTSIGKSIAESLGRPFYrfsvggMRDEAEIKGhrrT 424
Cdd:cd19503     3 GGLDEQIASLKELIELPLKYPELFRALglkpprgVLLHGPPGTGKTLLARAVANEAGANFL------SISGPSIVS---K 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1804231588 425 YIGAMPGKLVQALKEAEVMNP-VIMLDEID 453
Cdd:cd19503    74 YLGESEKNLREIFEEARSHAPsIIFIDEID 103
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
700-766 3.93e-06

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 46.67  E-value: 3.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804231588 700 PKDGPSAGITMASALLSLARNQAPKKGVAMTGELTLTGQVLPIGGVREKVIAARRQKIFELILPEAN 766
Cdd:pfam13541  55 KKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
353-456 4.32e-06

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: 47.78  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 353 GMDDIKQRITEFLAVGAFKGEIAGSI-------VLLVGPPGVGKTSIGKSIAESLGRPFYRFS----VGGMRDEAEikgh 421
Cdd:cd19518     4 GMDSTLKELCELLIHPILPPEYFQHLgvepprgVLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESE---- 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1804231588 422 rrtyigampGKLVQALKEAEVMNPVIM-LDEIDKMG 456
Cdd:cd19518    80 ---------EKIRELFDQAISNAPCIVfIDEIDAIT 106
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
381-405 4.66e-06

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: 47.43  E-value: 4.66e-06
                          10        20
                  ....*....|....*....|....*
gi 1804231588 381 LVGPPGVGKTSIGKSIAESLGRPFY 405
Cdd:COG0703     3 LIGMMGAGKSTVGRLLAKRLGLPFV 27
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
352-456 6.76e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 49.65  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITEFLAV----GAFKgEIAGSI---VLLVGPPGVGKTSIGKSIAESLGRPFyrFSVGGmRDEAEIkghrrt 424
Cdd:PRK10733  155 AGCDEAKEEVAELVEYlrepSRFQ-KLGGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPF--FTISG-SDFVEM------ 224
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1804231588 425 YIGAMPGKLVQALKEAEVMNP-VIMLDEIDKMG 456
Cdd:PRK10733  225 FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVG 257
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
352-458 7.25e-06

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: 47.29  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITEFLAVGAFKGEIAGSI------VLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHrrty 425
Cdd:cd19525    25 AGLEFAKKTIKEIVVWPMLRPDIFTGLrgppkgILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE---- 100
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1804231588 426 igampgKLVQAL-KEAEVMNP-VIMLDEIDKMGTS 458
Cdd:cd19525   101 ------KMVRALfSVARCKQPaVIFIDEIDSLLSQ 129
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
379-453 8.84e-06

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: 46.66  E-value: 8.84e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFyrFSVGGmrdeAEIKGhrrTYIGAMPGKLVQALKEAEVMNP-VIMLDEID 453
Cdd:cd19519    37 ILLYGPPGTGKTLIARAVANETGAFF--FLING----PEIMS---KLAGESESNLRKAFEEAEKNAPaIIFIDEID 103
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
377-405 9.10e-06

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: 46.39  E-value: 9.10e-06
                          10        20
                  ....*....|....*....|....*....
gi 1804231588 377 SIVLlVGPPGVGKTSIGKSIAESLGRPFY 405
Cdd:cd00464     1 NIVL-IGMMGAGKTTVGRLLAKALGLPFV 28
aroK PRK00131
shikimate kinase; Reviewed
376-404 1.45e-05

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 46.34  E-value: 1.45e-05
                          10        20
                  ....*....|....*....|....*....
gi 1804231588 376 GSIVLLVGPPGVGKTSIGKSIAESLGRPF 404
Cdd:PRK00131    4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
379-452 1.61e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.16  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRFS--VGGMRDeaeikghrrtyigampgkLVQALKEAEVM-----NPVIMLDE 451
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSavTSGVKD------------------LREVIEEARQRrsagrRTILFIDE 100

                  .
gi 1804231588 452 I 452
Cdd:PRK13342  101 I 101
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
347-458 3.10e-05

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 45.45  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 347 LDKHHAGMDDIKQ--------RITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRfsvggmrdeaeI 418
Cdd:cd19498     9 LDKYIIGQDEAKRavaialrnRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIK-----------V 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1804231588 419 KGHRRTYIGAMpGKLVQALKEaEVMNPVIMLDEIDKMGTS 458
Cdd:cd19498    78 EATKFTEVGYV-GRDVESIIR-DLVEGIVFIDEIDKIAKR 115
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
700-796 7.80e-05

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 46.19  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 700 PKDGPS------AGITMASALLSLARNQapkkGVAMTGELTLTGQVLPIGGVREKVIAARRQKIFELILPEANRGSYEel 773
Cdd:COG0606    74 PKEGSRfdlpiaLGILAASGQIPAEALE----DYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAA-- 147
                          90       100
                  ....*....|....*....|...
gi 1804231588 774 pdyLKEGLTVHFAKRYGDVAKVL 796
Cdd:COG0606   148 ---LVPGIEVYGASSLLEVVAFL 167
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
225-452 8.62e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.92  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 225 LLRKEVEVGRLQKELSAEVNKQIGERQREFFLKEQLKLIQQELGISKDDKSADREEFLARLEGKTLSAPAQKRIDEELNK 304
Cdd:COG1401    78 VLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEA 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 305 lSILETGSPEYAVTRNYLDWATALPWGIHGQDKLDLGRARKVLDKHHAgmDDIKQRITEFLAVGAFKGeiagsIVLLVGP 384
Cdd:COG1401   158 -LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLR--EKFEETLEAFLAALKTKK-----NVILAGP 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 385 PGVGKTSIGKSIAESLG------------RP--FYRFSVGGMRDEAEIKGHRRTyigamPGKLVQALKEAEvMNP----V 446
Cdd:COG1401   230 PGTGKTYLARRLAEALGgedngriefvqfHPswSYEDFLLGYRPSLDEGKYEPT-----PGIFLRFCLKAE-KNPdkpyV 303

                  ....*.
gi 1804231588 447 IMLDEI 452
Cdd:COG1401   304 LIIDEI 309
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
379-408 9.30e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 45.82  E-value: 9.30e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRFS 408
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALS 81
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
379-455 1.14e-04

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: 43.43  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGM----RDEAEikghrrtyigampgKLVQALKE-AEVMNP-VIMLDEI 452
Cdd:cd19522    36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLtskyRGESE--------------KLVRLLFEmARFYAPtTIFIDEI 101

                  ...
gi 1804231588 453 DKM 455
Cdd:cd19522   102 DSI 104
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
379-453 1.96e-04

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 44.90  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYrfSVGGmrdeAEIKGhrrTYIGAMPGKLVQALKEAEVMNP-VIMLDEID 453
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFI--SING----PEIMS---KYYGESEERLREIFKEAEENAPsIIFIDEID 281
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
378-515 2.08e-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: 43.20  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 378 IVLLVGPPGVGKTSIGKSIAESLG-RPFYRFSVGGMrdeAEIKGHR--RTYIGAmPGKLVQAL--KEAEVMNP-----VI 447
Cdd:cd19508    54 LVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQL---IEINSHSlfSKWFSE-SGKLVTKMfqKIQELIDDkdalvFV 129
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1804231588 448 MLDEIDKMGTSYQGdpASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLDSIPGPLLDRMEV 515
Cdd:cd19508   130 LIDEVESLAAARSA--SSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFVDRADI 195
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
352-411 2.42e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 44.64  E-value: 2.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1804231588 352 AGMDDIK---QRITEFL-------AVGAF--KGeiagsiVLLVGPPGVGKTSIGKSIA-ESlGRPFyrFSVGG 411
Cdd:COG0465   145 AGVDEAKeelQEIVDFLkdpekftRLGAKipKG------VLLVGPPGTGKTLLAKAVAgEA-GVPF--FSISG 208
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
372-404 3.77e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 43.45  E-value: 3.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1804231588 372 GEIAGSIVLLVGPPGVGKTSIGKSIAESLGR--PF 404
Cdd:pfam06068  46 GKIAGRAVLIAGPPGTGKTALAIAISKELGEdtPF 80
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
376-454 4.62e-04

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: 41.80  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 376 GSIvLLVGPPGVGKTSIGKSIAESLG---RPFYRFSvggMRDEAEIKGHRRTyIGAMPGkLVQA-----LKEAEVMNP-- 445
Cdd:pfam07724   4 GSF-LFLGPTGVGKTELAKALAELLFgdeRALIRID---MSEYMEEHSVSRL-IGAPPG-YVGYeeggqLTEAVRRKPys 77

                  ....*....
gi 1804231588 446 VIMLDEIDK 454
Cdd:pfam07724  78 IVLIDEIEK 86
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
378-406 4.73e-04

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 41.47  E-value: 4.73e-04
                          10        20
                  ....*....|....*....|....*....
gi 1804231588 378 IVLLVGPPGVGKTSIGKSIAESLGRPFYR 406
Cdd:cd02021     1 IIVVMGVSGSGKSTVGKALAERLGAPFID 29
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
352-455 7.56e-04

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: 40.87  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITEFLAVGAFKGEIAGSI--------VLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRD----EAEik 419
Cdd:cd19520     3 GGLDEVITELKELVILPLQRPELFDNSrllqppkgVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDkwygESQ-- 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1804231588 420 ghrrtyigampgKLVQAL-KEAEVMNP-VIMLDEIDKM 455
Cdd:cd19520    81 ------------KLVAAVfSLASKLQPsIIFIDEIDSF 106
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
371-404 7.60e-04

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 42.65  E-value: 7.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1804231588 371 KGEIAGSIVLLVGPPGVGKTSIGKSIAESLGR--PF 404
Cdd:COG1224    59 EGKMAGKGILIVGPPGTGKTALAVAIARELGEdtPF 94
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
383-448 1.41e-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: 39.78  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1804231588 383 GPPGVGKTSIGKSIAESLGRPFYrfSVGGMRDEaEIkGHRRTYIGAMPG---KLVQALKEAEVMNPVIM 448
Cdd:cd02020     6 GPAGSGKSTVAKLLAKKLGLPYL--DTGGIRTE-EV-GKLASEVAAIPEvrkALDERQRELAKKPGIVL 70
AAA_PrkA pfam08298
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
353-415 1.96e-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: 116881  Cd Length: 358  Bit Score: 41.29  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1804231588 353 GMDDIKQRITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESL-GRPFYRFSVGGMRDE 415
Cdd:pfam08298  62 GMEETIERIVNYFRHAAQGLEERKQILYLLGPVGGGKSSLAERLKKLLeLVPIYALKGSPVFES 125
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
352-455 1.98e-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: 39.83  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 352 AGMDDIKQRITEFLAVGAFKGEIAGSI------VLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEaeikghrrtY 425
Cdd:cd19524     3 AGQDLAKQALQEMVILPSLRPELFTGLrapargLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK---------Y 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1804231588 426 IGAMPgKLVQAL-KEAEVMNP-VIMLDEIDKM 455
Cdd:cd19524    74 VGEGE-KLVRALfAVARELQPsIIFIDEVDSL 104
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
379-466 2.30e-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: 39.39  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFyrFSVGGmrdeAEIkghRRTYIGAMPGKLVQALKEAEVMNP-VIMLDEIDKMGT 457
Cdd:cd19530    33 VLLYGPPGCGKTLLAKAVANESGANF--ISVKG----PEL---LNKYVGESERAVRQVFQRARASAPcVIFFDEVDALVP 103

                  ....*....
gi 1804231588 458 SYQGDPASA 466
Cdd:cd19530   104 KRGDGGSWA 112
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
379-472 2.43e-03

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: 39.19  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFyrFSVGGmrdeAEIKGhrrTYIGAMPGKLVQALKEAEVMNP-VIMLDEID---- 453
Cdd:cd19511    30 VLLYGPPGCGKTLLAKALASEAGLNF--ISVKG----PELFS---KYVGESERAVREIFQKARQAAPcIIFFDEIDslap 100
                          90       100
                  ....*....|....*....|...
gi 1804231588 454 KMGTSYQGDPA----SALLETLD 472
Cdd:cd19511   101 RRGQSDSSGVTdrvvSQLLTELD 123
PRK13695 PRK13695
NTPase;
379-455 2.49e-03

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 39.51  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRfsVGGMRDEaEI--KGHR-----------------RTYIGAMP--GKLV--- 434
Cdd:PRK13695    3 IGITGPPGVGKTTLVLKIAELLKEEGYK--VGGFYTE-EVreGGKRigfkiidldtgeegilaRVGFPSRPrvGKYVvnl 79
                          90       100
                  ....*....|....*....|....*....
gi 1804231588 435 --------QALKEAEVMNPVIMLDEIDKM 455
Cdd:PRK13695   80 edlerigiPALERALEEADVIIIDEIGKM 108
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
376-405 2.92e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 39.34  E-value: 2.92e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1804231588 376 GSIVLLVGPPGVGKTSIGKSIAESLGRPFY 405
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERLGWPFI 30
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
380-516 4.01e-03

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: 39.08  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 380 LLVGPPGVGKTSIGKSIAESL---GRPFYRFSVGgmrdEAEIKGHRRTYIGAMPG--------KLVQALKEaevmNP--V 446
Cdd:cd19499    45 LFLGPTGVGKTELAKALAELLfgdEDNLIRIDMS----EYMEKHSVSRLIGAPPGyvgyteggQLTEAVRR----KPysV 116
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 447 IMLDEIDKMGTSYQGdpasALLETLDpeqNVEFLDHYlDLRLDLSKVLFVCTANTLDSipgPLLDRMEVI 516
Cdd:cd19499   117 VLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSNHFRP---EFLNRIDEI 175
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
228-390 4.12e-03

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


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 40.01  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 228 KEVEVGRLQK---ELSAEVNKqigERQREFFLKEQLKLIQQELGISKDDKSADREEFLARLEGKTLSA-------PAQKR 297
Cdd:TIGR03499  32 RKVRKGLFGKkfvEVTAAIDE---EEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAaqaaeplLPEEE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 298 IDEELNKL-SILET---------GSPEYAVTRNYLDWAtalpwGIHGQDKLDLgrARKVLDKHHA--GMDDIKQRITEFL 365
Cdd:TIGR03499 109 LRKELEALrELLERllaglawlqRPPERAKLYERLLEA-----GVSEELAREL--LEKLPEDADAedAWRWLREALEGML 181
                         170       180
                  ....*....|....*....|....*..
gi 1804231588 366 AVGAFKGEIA--GSIVLLVGPPGVGKT 390
Cdd:TIGR03499 182 PVKPEEDPILeqGGVIALVGPTGVGKT 208
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
379-480 4.42e-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: 38.86  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRfsVGGmrdeAEIKghrRTYIGAMPgKLVQALKE-AEVMNP-VIMLDEIDKMG 456
Cdd:cd19502    40 VLLYGPPGTGKTLLAKAVANHTDATFIR--VVG----SELV---QKYIGEGA-RLVRELFEmAREKAPsIIFIDEIDAIG 109
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1804231588 457 TSYQGDPASA-------LLETL------DPEQNVEFL 480
Cdd:cd19502   110 AKRFDSGTGGdrevqrtMLELLnqldgfDPRGNIKVI 146
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
379-457 5.26e-03

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 40.14  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPFYRFsVGgmrdeAEIKghrRTYIGAMPgKLVQAL-KEAEVMNP-VIMLDEIDKMG 456
Cdd:PTZ00361  220 VILYGPPGTGKTLLAKAVANETSATFLRV-VG-----SELI---QKYLGDGP-KLVRELfRVAEENAPsIVFIDEIDAIG 289

                  .
gi 1804231588 457 T 457
Cdd:PTZ00361  290 T 290
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
379-510 6.50e-03

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 38.38  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 379 VLLVGPPGVGKTSIGKSIAESLGRPfyRFSVGGMRDEaEI--KGHR--RTYIGAMPGK---------------------- 432
Cdd:pfam03266   2 IFITGPPGVGKTTLVLKVAELLKSS--GVKVGGFYTP-EVreGGRRigFKIVDLASGEegwlarvgavsgprvgkyvvnv 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 433 ------LVQALKEAEVMNPVIMLDEIDKMGTSYQGdPASALLETLDPEQNV-----EFLDHYL--DLRLDLSKVLFVCTA 499
Cdd:pfam03266  79 esfeeiAVPALRRALEEADLIIIDEIGPMELKSKK-FREAVREVLDSGKPVlavihRRSDSPLleEIRRREDVKIFVVTK 157
                         170
                  ....*....|.
gi 1804231588 500 NTLDSIPGPLL 510
Cdd:pfam03266 158 ENRDALPEEIL 168
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
367-500 7.35e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.82  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 367 VGAFkgeiagsivLLVGPPGVGKTSIGKSIAESLGRPFYRFsvggmrDEAEIkGHRRT---YIGAMPGKL--VQA--LKE 439
Cdd:PRK11034  488 VGSF---------LFAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfDQGglLTD 551
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1804231588 440 AEVMNP--VIMLDEIDKMgtsyQGDPASALLETLDpeqNVEFLDHYlDLRLDLSKVLFVCTAN 500
Cdd:PRK11034  552 AVIKHPhaVLLLDEIEKA----HPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 606
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
344-458 9.19e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 38.74  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804231588 344 RKVLDKHHAGMDDIKQ-----------RITEFLAVGAFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFyrfsvgGM 412
Cdd:cd19497     7 KEHLDKYVIGQERAKKvlsvavynhykRIRNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPF------AI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1804231588 413 RD-----EAeikghrrTYIG----AMPGKLVQA----LKEAEvmNPVIMLDEIDKMGTS 458
Cdd:cd19497    81 ADattltEA-------GYVGedveNILLKLLQAadydVERAQ--RGIVYIDEIDKIARK 130
 
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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