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Conserved domains on  [gi|2551685493|ref|WP_302547528|]
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endopeptidase La [Barnesiella intestinihominis]

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, ...
23-796 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1298.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPIGVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDESTTV 102
Cdd:COG0466    14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 103 ILQGKmKRFRIDEITETFPYMRANVSLENEILPDanDKEFEALVSALKDLTFELLKNIGEQAKELVFAIRNIDSAHYLVN 182
Cdd:COG0466    94 LVEGL-QRARIKEFVQEEPYLEAEVEPLEEEEED--DKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLAD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 183 FLGANIPLSATQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEELG-GNMQ 261
Cdd:COG0466   171 FIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGeKDDG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 262 DQDIQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLDKDHYGL 341
Cdd:COG0466   251 EDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGL 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 342 DKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGAMPGRII 421
Cdd:COG0466   331 EKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRII 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 422 QGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNTISQPLLDRME 501
Cdd:COG0466   411 QGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRME 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 502 LIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRKVARLKASGKEYN 581
Cdd:COG0466   491 IIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKK 570
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 582 PTLSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQYIK 661
Cdd:COG0466   571 VTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKG-KLTLTGQLGDVMKESAQAALSYVR 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 662 SHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKILAA 741
Cdd:COG0466   650 SRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAA 729
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2551685493 742 KRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALTDEKVKNAID 796
Cdd:COG0466   730 HRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPKK 784
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
23-796 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1298.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPIGVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDESTTV 102
Cdd:COG0466    14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 103 ILQGKmKRFRIDEITETFPYMRANVSLENEILPDanDKEFEALVSALKDLTFELLKNIGEQAKELVFAIRNIDSAHYLVN 182
Cdd:COG0466    94 LVEGL-QRARIKEFVQEEPYLEAEVEPLEEEEED--DKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLAD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 183 FLGANIPLSATQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEELG-GNMQ 261
Cdd:COG0466   171 FIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGeKDDG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 262 DQDIQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLDKDHYGL 341
Cdd:COG0466   251 EDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGL 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 342 DKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGAMPGRII 421
Cdd:COG0466   331 EKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRII 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 422 QGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNTISQPLLDRME 501
Cdd:COG0466   411 QGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRME 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 502 LIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRKVARLKASGKEYN 581
Cdd:COG0466   491 IIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKK 570
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 582 PTLSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQYIK 661
Cdd:COG0466   571 VTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKG-KLTLTGQLGDVMKESAQAALSYVR 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 662 SHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKILAA 741
Cdd:COG0466   650 SRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAA 729
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2551685493 742 KRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALTDEKVKNAID 796
Cdd:COG0466   730 HRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPKK 784
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
24-786 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: 940.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  24 PILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPI-GVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDEST-- 100
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYlGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSSGTat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 101 -TVILQGkMKRFRIDEITETFPYMRANVSLENEILPDANDKEFEALVSALKDLTFELLK--NIGEQAKELVFAIRNIDSA 177
Cdd:TIGR00763  81 yKVVVEG-LRRIRIKELSDKGGYLVVRVDNLKEEPFDKDDEEIKALTREIKETFRELISlsKLFREQPALLSALEDIDEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 178 HYLVNFLGANIPLSA-TQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEEL 256
Cdd:TIGR00763 160 GRLADFVAASLQLKEkDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKEL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 257 GGNMQDQD-IQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLD 335
Cdd:TIGR00763 240 GIEKDDKDeLEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 336 KDHYGLDKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGA 415
Cdd:TIGR00763 320 EDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 416 MPGRIIQGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNTISQP 495
Cdd:TIGR00763 400 MPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 496 LLDRMELIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRKVARLKA 575
Cdd:TIGR00763 480 LLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 576 SGKEYNPT------LSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVM 649
Cdd:TIGR00763 560 EQGEKKKSeaesvvITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKG-SLELTGQLGDVM 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 650 KESAVIALQYIKSHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVL 729
Cdd:TIGR00763 639 KESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVL 718
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2551685493 730 PVGGIKEKILAAKRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIAL 786
Cdd:TIGR00763 719 PIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
23-788 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 700.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPIGVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDESTTV 102
Cdd:PRK10787   11 IPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 103 ILQGkMKRFRIDEITETFPYMRANVSLENEilPDANDKEFEALVSALKDLTFELLKNIGEQAKELVFAIRNIDSAHYLVN 182
Cdd:PRK10787   91 LVEG-LQRARISALSDNGEHFSAKAEYLES--PTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 183 FLGANIPLSATQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEELGgNMQD 262
Cdd:PRK10787  168 TIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG-EMDD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 263 --QDIQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLDKDHYG 340
Cdd:PRK10787  247 apDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 341 LDKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGAMPGRI 420
Cdd:PRK10787  327 LERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 421 IQGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNtISQPLLDRM 500
Cdd:PRK10787  407 IQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDRM 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 501 ELIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRK-VARLKASGKE 579
Cdd:PRK10787  486 EVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKaVKQLLLDKSL 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 580 YNPTLSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQY 659
Cdd:PRK10787  566 KHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKG-KLTYTGSLGEVMQESIQAALTV 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 660 IKSHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKIL 739
Cdd:PRK10787  645 VRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLL 724
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*....
gi 2551685493 740 AAKRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALTD 788
Cdd:PRK10787  725 AAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQN 773
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
327-508 2.13e-127

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: 378.05  E-value: 2.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 327 LNHVQKQLDKDHYGLDKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIR 406
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 407 GHRRTYIGAMPGRIIQGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATA 486
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                         170       180
                  ....*....|....*....|..
gi 2551685493 487 NNLNTISQPLLDRMELIDISGY 508
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
587-787 1.04e-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: 307.24  E-value: 1.04e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 587 DDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQYIKSHASL 666
Cdd:pfam05362   5 KNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKG-KLTLTGQLGDVMKESAQAALSYVRSRAEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 667 LGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKILAAKRAGI 746
Cdd:pfam05362  84 LGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGI 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2551685493 747 REIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALT 787
Cdd:pfam05362 164 KTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
22-77 2.29e-06

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 46.28  E-value: 2.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2551685493   22 GLPILALRNMVLFPGVAIPVNVGRTKSLQLIKDA-QNSHTPIGVVCQRDAAVEDPGK 77
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEAlRRSQPYVIVFLLQDDPTETPEP 57
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
23-796 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1298.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPIGVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDESTTV 102
Cdd:COG0466    14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDGTVKV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 103 ILQGKmKRFRIDEITETFPYMRANVSLENEILPDanDKEFEALVSALKDLTFELLKNIGEQAKELVFAIRNIDSAHYLVN 182
Cdd:COG0466    94 LVEGL-QRARIKEFVQEEPYLEAEVEPLEEEEED--DKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGRLAD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 183 FLGANIPLSATQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEELG-GNMQ 261
Cdd:COG0466   171 FIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGeKDDG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 262 DQDIQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLDKDHYGL 341
Cdd:COG0466   251 EDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGL 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 342 DKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGAMPGRII 421
Cdd:COG0466   331 EKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRII 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 422 QGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNTISQPLLDRME 501
Cdd:COG0466   411 QGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRME 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 502 LIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRKVARLKASGKEYN 581
Cdd:COG0466   491 IIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKK 570
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 582 PTLSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQYIK 661
Cdd:COG0466   571 VTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKG-KLTLTGQLGDVMKESAQAALSYVR 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 662 SHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKILAA 741
Cdd:COG0466   650 SRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAA 729
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2551685493 742 KRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALTDEKVKNAID 796
Cdd:COG0466   730 HRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPKK 784
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
24-786 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: 940.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  24 PILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPI-GVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDEST-- 100
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYlGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSSGTat 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 101 -TVILQGkMKRFRIDEITETFPYMRANVSLENEILPDANDKEFEALVSALKDLTFELLK--NIGEQAKELVFAIRNIDSA 177
Cdd:TIGR00763  81 yKVVVEG-LRRIRIKELSDKGGYLVVRVDNLKEEPFDKDDEEIKALTREIKETFRELISlsKLFREQPALLSALEDIDEP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 178 HYLVNFLGANIPLSA-TQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEEL 256
Cdd:TIGR00763 160 GRLADFVAASLQLKEkDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKEL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 257 GGNMQDQD-IQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLD 335
Cdd:TIGR00763 240 GIEKDDKDeLEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 336 KDHYGLDKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGA 415
Cdd:TIGR00763 320 EDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 416 MPGRIIQGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNTISQP 495
Cdd:TIGR00763 400 MPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 496 LLDRMELIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRKVARLKA 575
Cdd:TIGR00763 480 LLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 576 SGKEYNPT------LSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVM 649
Cdd:TIGR00763 560 EQGEKKKSeaesvvITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKG-SLELTGQLGDVM 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 650 KESAVIALQYIKSHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVL 729
Cdd:TIGR00763 639 KESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVL 718
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2551685493 730 PVGGIKEKILAAKRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIAL 786
Cdd:TIGR00763 719 PIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
23-788 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 700.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALRNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPIGVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDESTTV 102
Cdd:PRK10787   11 IPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 103 ILQGkMKRFRIDEITETFPYMRANVSLENEilPDANDKEFEALVSALKDLTFELLKNIGEQAKELVFAIRNIDSAHYLVN 182
Cdd:PRK10787   91 LVEG-LQRARISALSDNGEHFSAKAEYLES--PTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 183 FLGANIPLSATQKQELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEELGgNMQD 262
Cdd:PRK10787  168 TIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG-EMDD 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 263 --QDIQELRERAEKKKWDSKTAEIFEKEMRKLERLHPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLDKDHYG 340
Cdd:PRK10787  247 apDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 341 LDKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIRGHRRTYIGAMPGRI 420
Cdd:PRK10787  327 LERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 421 IQGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNtISQPLLDRM 500
Cdd:PRK10787  407 IQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPLLDRM 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 501 ELIDISGYIIEEKVEIGRRHLVPKQLENHGLKEGDVIIPKKVMAAIVDQYTRESGVRELDKKIARIMRK-VARLKASGKE 579
Cdd:PRK10787  486 EVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKaVKQLLLDKSL 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 580 YNPTLSIDDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQY 659
Cdd:PRK10787  566 KHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKG-KLTYTGSLGEVMQESIQAALTV 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 660 IKSHASLLGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKIL 739
Cdd:PRK10787  645 VRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLL 724
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*....
gi 2551685493 740 AAKRAGIREIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALTD 788
Cdd:PRK10787  725 AAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQN 773
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
327-508 2.13e-127

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: 378.05  E-value: 2.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 327 LNHVQKQLDKDHYGLDKVKERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAEIR 406
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 407 GHRRTYIGAMPGRIIQGLIKAKSSNPVFVLDEIDKIGNDFKGDPASALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATA 486
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
                         170       180
                  ....*....|....*....|..
gi 2551685493 487 NNLNTISQPLLDRMELIDISGY 508
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
587-787 1.04e-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: 307.24  E-value: 1.04e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 587 DDLHEYLGAQEYNRDKYENNDYAGVVTGLAWTAVGGEILFVESSLSKSKGeKLTLTGNLGDVMKESAVIALQYIKSHASL 666
Cdd:pfam05362   5 KNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKG-KLTLTGQLGDVMKESAQAALSYVRSRAEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 667 LGIDEDIFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLPVGGIKEKILAAKRAGI 746
Cdd:pfam05362  84 LGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGI 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2551685493 747 REIILSEENRKDIEEIKESYLKGLTFHYVKNITDVLKIALT 787
Cdd:pfam05362 164 KTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
23-217 1.40e-47

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: 167.51  E-value: 1.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALRNMVLFPGVAIPVNVGRTKSLQLIKDA--QNSHTPIGVVCQRDAAVEDPGKDDLYEIGVIGEIIKILEMPDEST 100
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAAlnKDKLYGVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGTY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 101 TVILQGkMKRFRIDEITE-TFPYMRANVslenEILPDANDKEFEALVSALKDLtFELLKNIGEQAK--ELVFAIRNIDSA 177
Cdd:pfam02190  82 KVLVEG-LERVRIVELVKkEEPYLRAEV----EDLPEDSDELSEALKALVKEL-IEKLRRLLKLLLplELLLKIKDIENP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2551685493 178 HYLVNFLGANIPLSATQKQELLTISNIKERLFKLYEMLTQ 217
Cdd:pfam02190 156 GRLADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
366-503 7.00e-29

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 111.92  E-value: 7.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLhdeaeirghRRTYIGAMPGRIIQGLIKAKSSNP-VFVLDEIDKI-- 442
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSEL---------VSKYVGESEKRLRELFEAAKKLAPcVIFIDEIDALag 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551685493 443 -----GNDFKGDPASALLEVLDPEQNNTfhdnyididydlSKILFIATANNLNTISQPLLDRMELI 503
Cdd:pfam00004  72 srgsgGDSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRI 125
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
23-218 3.90e-28

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 111.89  E-value: 3.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  23 LPILALrNMVLFPGVAIPVNVGRTKSLQLIKDAQNSHTPIGVVCQRDAAvEDPGKDDLYEIGVIGEIIKILEMPDESTTV 102
Cdd:COG2802     7 LPLFPL-GAVLFPGGRLPLHIFEPRYLDMVRDCLAGDRPFGVVLIREGR-EVGGPPPLYDVGTLARITDFEELEDGRLDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 103 ILQGkMKRFRIDEITETF-PYMRANVslenEILPDANDKEFEALVSALKDLTFELLKNIGEQAKelVFAIRNIDSAHYLV 181
Cdd:COG2802    85 TLRG-VQRFRILEELQEDdPYRVAEV----EWLPDEPDLPVPEELEALRERLLRLLRRYPELAG--LEADPDLDDPEWLS 157
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2551685493 182 NFLGANIPLSATQKQELLTISNIKERLFKLYEMLTQE 218
Cdd:COG2802   158 NRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
341-492 5.84e-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: 78.86  E-value: 5.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 341 LDKVKERIIEHLAVLKLR--GDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEAeirghrRTYIGAMPG 418
Cdd:cd19481     2 KASLREAVEAPRRGSRLRryGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 419 RIIQgliKAKSSNP-VFVLDEIDKIGNDFKGDPAS--------ALLEVLDPEQNntfhdnyididydLSKILFIATANNL 489
Cdd:cd19481    76 KIFE---RARRLAPcILFIDEIDAIGRKRDSSGESgelrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139

                  ...
gi 2551685493 490 NTI 492
Cdd:cd19481   140 DLL 142
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
652-785 2.72e-16

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 78.48  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 652 SAVIALQYikshASLL-GIDediFDKWAVHIHVPEGAIPKDGPSAGITMVTSLASTFTQRKVKDHLAMTGEITLRGKVLP 730
Cdd:COG1750    75 SARIAALV----ASLLaGVD---LSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGP 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551685493 731 VGGIKEKILAAKRAGIREIILSEENRKDIEEIKESYLK----------GLTFHYVKNITDVLKIA 785
Cdd:COG1750   148 VGGVYEKLEAAASAGAKYFLIPKGQAILTGYNTQVGETvdlveygkelGVKVIEVSTIADALQYF 212
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
345-503 1.58e-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: 68.71  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 345 KERIIEHLAVLKLRGDMKSPIICLYGPPGVGKTSLGKSVAEALNRK---YIRISLGGLHDEAEIRGHRRTYIgampgRII 421
Cdd:cd00009     1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgapFLYLNASDLLEGLVVAELFGHFL-----VRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 422 QGLIKAKSSNPVFVLDEIDKIGNDFKgdpaSALLEVLDpeqnnTFHDNYidIDYDLSKILFIATANNLNTISQPLLDRME 501
Cdd:cd00009    76 LFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVLE-----TLNDLR--IDRENVRVIGATNRPLLGDLDRALYDRLD 144

                  ..
gi 2551685493 502 LI 503
Cdd:cd00009   145 IR 146
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
340-527 3.45e-13

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: 72.25  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 340 GLDKVKERIIEHLAVL----KLRGDMKSPI---ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrrtY 412
Cdd:COG0464   161 GLEEVKEELRELVALPlkrpELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 413 IGAMPGRIIQGLIKAKSSNPVFVL-DEIDKIGNDFKGDPASALLEVLdpeqnntfhdNYI--DIDYDLSKILFIATANNL 489
Cdd:COG0464   232 VGETEKNLREVFDKARGLAPCVLFiDEADALAGKRGEVGDGVGRRVV----------NTLltEMEELRSDVVVIAATNRP 301
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2551685493 490 NTISQPLLDRM-ELIDISGYIIEEKVEIGRRHLVPKQLE 527
Cdd:COG0464   302 DLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD 340
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
366-500 6.02e-10

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 58.07  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEAL-NRKYIRISLGGLHDEAEIRGHRRtYIGAMPGRIIQGLIKAKSSNPVFVLDEIDKIGN 444
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRN-IDPGGASWVDGPLVRAAREGEIAVLDEINRANP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551685493 445 DFkgdpASALLEVLDpeqNNTFH--DNYIDIDYDLSKILFIATANNL----NTISQPLLDRM 500
Cdd:pfam07728  81 DV----LNSLLSLLD---ERRLLlpDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
345-595 1.60e-08

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: 56.71  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 345 KERIIEH-LAVLKLRGdmksPIIcLYGPPGVGKTSLGKSVAEALNRKYIRIslgglhdeaeirghrRTYIGAMPGRIIqG 423
Cdd:COG0714    17 QEELIELvLIALLAGG----HLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSDIL-G 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 424 ---LIKAKSSN-----PVF---VL-DEIDkigndfKGDPA--SALLEVLDpeqnntfhDNYIDID---YDLSKILF-IAT 485
Cdd:COG0714    76 tyiYDQQTGEFefrpgPLFanvLLaDEIN------RAPPKtqSALLEAME--------ERQVTIPggtYKLPEPFLvIAT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 486 AN---NLNT--ISQPLLDRMEL-IDIsGY-IIEEKVEIGRRHL------VPKQLENHGLKEGD-----VIIPKKVMAAIV 547
Cdd:COG0714   142 QNpieQEGTypLPEAQLDRFLLkLYI-GYpDAEEEREILRRHTgrhlaeVEPVLSPEELLALQelvrqVHVSEAVLDYIV 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2551685493 548 D--QYTRES-------GVRE-LDkkIARIMRKVARLkaSGKEYnptLSIDDLHEYLGA 595
Cdd:COG0714   221 DlvRATREHpdlrkgpSPRAsIA--LLRAARALALL--DGRDY---VTPDDVKAVAGP 271
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
336-443 2.34e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 53.47  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 336 KDHYGLDKVKERIIEHLAVLKLRGDM-----KSPI--ICLYGPPGVGKTSLGKSVAEALNRKYIRISLgglhdeAEIrgh 408
Cdd:COG1222    78 DDIGGLDEQIEEIREAVELPLKNPELfrkygIEPPkgVLLYGPPGTGKTLLAKAVAGELGAPFIRVRG------SEL--- 148
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2551685493 409 RRTYIGAmPGRIIQGLI-KAKSSNPVFV-LDEIDKIG 443
Cdd:COG1222   149 VSKYIGE-GARNVREVFeLAREKAPSIIfIDEIDAIA 184
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
342-521 5.06e-07

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 51.81  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 342 DKVKERIIEHLAVLKLR--GDMKSPIICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrrtYIGAMPGR 419
Cdd:COG1223    12 KKLKLIIKELRRRENLRkfGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGETARN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 420 IIQGLIKAKSSNPVFVLDEIDKIGNDfKGDPA---------SALLevldpeQNntfhdnyidIDYDLSKILFIATANNLN 490
Cdd:COG1223    83 LRKLFDFARRAPCVIFFDEFDAIAKD-RGDQNdvgevkrvvNALL------QE---------LDGLPSGSVVIAATNHPE 146
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2551685493 491 TISQPLLDRMEL-IDISGYIIEEKVEIGRRHL 521
Cdd:COG1223   147 LLDSALWRRFDEvIEFPLPDKEERKEILELNL 178
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
359-503 8.17e-07

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 49.87  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 359 GDMKSPII--CLYGPPGVGKTSLGKSVAEAL---NRKYIRISLGGLHDEAEIrghrRTYIGAMPGRIIQG----LIKAKS 429
Cdd:cd19499    35 SDPNRPIGsfLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYMEKHSV----SRLIGAPPGYVGYTeggqLTEAVR 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551685493 430 SNP--VFVLDEIDkigndfKGDPA--SALLEVLDpeqNNTFHDNYiDIDYDLSKILFIATANNlntISQPLLDRMELI 503
Cdd:cd19499   111 RKPysVVLLDEIE------KAHPDvqNLLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSNH---FRPEFLNRIDEI 175
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
22-77 2.29e-06

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 46.28  E-value: 2.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2551685493   22 GLPILALRNMVLFPGVAIPVNVGRTKSLQLIKDA-QNSHTPIGVVCQRDAAVEDPGK 77
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEAlRRSQPYVIVFLLQDDPTETPEP 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
362-513 2.63e-06

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 47.75  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  362 KSPIICLYGPPGVGKTSLGKSVAEALNRKYIRI-------SLGGLHDEAEIRGHRRTYIGAMPGRIIQGLI-KAKSSNP- 432
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALaLARKLKPd 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493  433 VFVLDEIDkigndfkgdpaSALLEVLDPEQNNTFHDNYIDIDYDLSKILFIATANNLNTisqplLDRMELIDISGYIIEE 512
Cdd:smart00382  81 VLILDEIT-----------SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKD-----LGPALLRRRFDRRIVL 144

                   .
gi 2551685493  513 K 513
Cdd:smart00382 145 L 145
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
692-745 3.07e-06

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 50.19  E-value: 3.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551685493 692 GPSAGitMVTSLA--STFTQ------RKVkdhlAMTGEITLRGKVLPVGGIKEKILAAKRAG 745
Cdd:COG3480   240 GPSAG--LMFALGiyDQLTPgdltggKKI----AGTGTIDADGTVGPIGGIDQKVVAARRAG 295
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
366-443 9.51e-06

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: 46.56  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLhdeaeirghRRTYIGAMPgRIIQGLIK-AKSSNPVFV-LDEIDKIG 443
Cdd:cd19502    40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSEL---------VQKYIGEGA-RLVRELFEmAREKAPSIIfIDEIDAIG 109
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
368-395 3.51e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 47.00  E-value: 3.51e-05
                          10        20
                  ....*....|....*....|....*...
gi 2551685493 368 LYGPPGVGKTSLGKSVAEALNRKYIRIS 395
Cdd:PRK13342   41 LWGPPGTGKTTLARIIAGATDAPFEALS 68
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
336-443 4.30e-05

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: 44.92  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 336 KDHYGLDKVKERIIEHLAVLK-----LRGDMKSPI-ICLYGPPGVGKTSLGKSVAEALNRKYIRISlGGLHDEaeirghr 409
Cdd:cd19501     4 KDVAGCEEAKEELKEVVEFLKnpekfTKLGAKIPKgVLLVGPPGTGKTLLAKAVAGEAGVPFFSIS-GSDFVE------- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2551685493 410 rTYIGAMPGRIIQGLIKAKSSNP--VFVlDEIDKIG 443
Cdd:cd19501    76 -MFVGVGASRVRDLFEQAKKNAPciVFI-DEIDAVG 109
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
346-443 5.35e-05

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 44.32  E-value: 5.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 346 ERIIEHLAVLKLRGdmkspiICLYGPPGVGKTSLGKSVAEALNRKYIRIS----LGGLHDEAEirghrrtyigampGRII 421
Cdd:cd19518    23 PEYFQHLGVEPPRG------VLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESE-------------EKIR 83
                          90       100
                  ....*....|....*....|...
gi 2551685493 422 QGLIKAKSSNPVFV-LDEIDKIG 443
Cdd:cd19518    84 ELFDQAISNAPCIVfIDEIDAIT 106
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
196-487 6.37e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 46.30  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 196 QELLTISNIKERLFKLYEMLTQEAQLLQIKADIQSKTREDLNQQQREHFLQQQIRTIQEELGGNMQDQDIQELRERAEKK 275
Cdd:COG1401    63 ATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 276 KWDSKTAEIFEKEMRKLERL-HPQSPDFSVQYTYLDTLLELPWNEYTQDNFNLNHVQKQLDKDHYgldkvKERIIEHLAV 354
Cdd:COG1401   143 DLEERAALETEVLEALEAELeELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKF-----EETLEAFLAA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 355 LKlrgdmKSPIICLYGPPGVGKTSLGKSVAEAL----NRKYIRISLG-GLHDEAEIRGHR-----RTYIgAMPGRIIQGL 424
Cdd:COG1401   218 LK-----TKKNVILAGPPGTGKTYLARRLAEALggedNGRIEFVQFHpSWSYEDFLLGYRpsldeGKYE-PTPGIFLRFC 291
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551685493 425 IKAK--SSNP-VFVLDEIdkigNdfKGDPASA------LLEVLDPEQNNTFHDNYIDIDYDLS---KILFIATAN 487
Cdd:COG1401   292 LKAEknPDKPyVLIIDEI----N--RANVEKYfgellsLLESDKRGEELSIELPYSGEGEEFSippNLYIIGTMN 360
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
366-442 7.53e-05

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 43.64  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIrislgglhdeaEIRGHR--RTYIGAMPGRIIQGLIKAKSSNP-VFVLDEIDKI 442
Cdd:cd19529    30 ILLYGPPGTGKTLLAKAVATESNANFI-----------SVKGPEllSKWVGESEKAIREIFRKARQVAPcVIFFDEIDSI 98
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
368-395 9.71e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 45.43  E-value: 9.71e-05
                          10        20
                  ....*....|....*....|....*...
gi 2551685493 368 LYGPPGVGKTSLGKSVAEALNRKYIRIS 395
Cdd:COG2256    54 LWGPPGTGKTTLARLIANATDAEFVALS 81
44 PHA02544
clamp loader, small subunit; Provisional
364-616 1.54e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 44.60  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 364 PIICLYGP-PGVGKTSLGKSVAEALNRKYIRI--SLGGLHDeaeIRGHRRTYIGAMpgriiqgliKAKSSNPVFVLDEID 440
Cdd:PHA02544   43 PNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVngSDCRIDF---VRNRLTRFASTV---------SLTGGGKVIIIDEFD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 441 KIGNDFKGDPASALLEvldpeqnnTFHDNyididydlskILFIATANNLNTISQPLLDRMELIDISGYIIEEKVEIGrrh 520
Cdd:PHA02544  111 RLGLADAQRHLRSFME--------AYSKN----------CSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM--- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 521 lvpKQLENHG---LKEGDVIIPKKVMAAIVDQY---TResgvreldkkiaRIMRKVARLKASGKEYNPTLS------IDD 588
Cdd:PHA02544  170 ---KQMIVRCkgiLEAEGVEVDMKVLAALVKKNfpdFR------------RTINELQRYASTGKIDAGILSevtnsdIDD 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2551685493 589 LHEYLGAQEYNR-----DKYeNNDYAGVVTGLA 616
Cdd:PHA02544  235 VVEALKAKDFKAvralaPNY-ANDYASFVGKLY 266
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
366-459 3.64e-04

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 41.89  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrrtYIGAMPGRIIQGLIKAKSSNP-VFVLDEIDKI-- 442
Cdd:cd19511    30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK---------YVGESERAVREIFQKARQAAPcIIFFDEIDSLap 100
                          90       100
                  ....*....|....*....|...
gi 2551685493 443 --GNDFKGDPA----SALLEVLD 459
Cdd:cd19511   101 rrGQSDSSGVTdrvvSQLLTELD 123
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
370-487 5.69e-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: 41.41  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 370 GPPGVGKTSLGKSVAEALN---RKYIRIslgglhdEAeirghrRTY---------IGAMPGRIIQG----LIKAKSSNPV 433
Cdd:pfam07724  10 GPTGVGKTELAKALAELLFgdeRALIRI-------DM------SEYmeehsvsrlIGAPPGYVGYEeggqLTEAVRRKPY 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2551685493 434 FV--LDEIDKIGndfkGDPASALLEVLDPEQNNTFHDNYIDIDYdlskILFIATAN 487
Cdd:pfam07724  77 SIvlIDEIEKAH----PGVQNDLLQILEGGTLTDKQGRTVDFKN----TLFIMTGN 124
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
366-442 6.10e-04

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: 41.12  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIRISlgglhdeaeirGHrrTYIGAMPGRIIQGL----IKAKSSNP-VFVLDEID 440
Cdd:cd19503    37 VLLHGPPGTGKTLLARAVANEAGANFLSIS-----------GP--SIVSKYLGESEKNLreifEEARSHAPsIIFIDEID 103

                  ..
gi 2551685493 441 KI 442
Cdd:cd19503   104 AL 105
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
340-501 6.43e-04

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 41.18  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 340 GLDKVKERIIEhlAVLK-------LRGDMKSPI-ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrrt 411
Cdd:cd19509     3 GLDDAKEALKE--AVILpslrpdlFPGLRGPPRgILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSK--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 412 YIGAmPGRIIQGLIK-AKSSNP-VFVLDEIDKIGNDFKGDPASA-------LLEVLDPEQNNtfhdnyididyDLSKILF 482
Cdd:cd19509    72 WVGE-SEKIVRALFAlARELQPsIIFIDEIDSLLSERGSGEHEAsrrvkteFLVQMDGVLNK-----------PEDRVLV 139
                         170
                  ....*....|....*....
gi 2551685493 483 IATANNLNTISQPLLDRME 501
Cdd:cd19509   140 LGATNRPWELDEAFLRRFE 158
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
340-401 7.01e-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: 41.26  E-value: 7.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551685493 340 GLDKVKERIIEhLAVLKLR-------GDMKSPI--ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHD 401
Cdd:cd19520     4 GLDEVITELKE-LVILPLQrpelfdnSRLLQPPkgVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
366-392 1.10e-03

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 40.50  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*..
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYI 392
Cdd:COG0703     1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
346-439 1.19e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 42.24  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 346 ERIIEHLAVLKLRgdmKSPIICLYGPPGVGKTSLGKSVAEALnRKYIRISLgglhDEAEIRGhrrtYIGAMPGRIIQGLI 425
Cdd:COG1373     6 KRKILDKLLKLLD---NRKAVVITGPRQVGKTTLLKQLAKEL-ENILYINL----DDPRLRA----LAEEDPDDLLEALK 73
                          90
                  ....*....|....
gi 2551685493 426 KAKSSNPVFVLDEI 439
Cdd:COG1373    74 ELYPGKTYLFLDEI 87
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
366-448 1.41e-03

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 40.10  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrrtYIGAMPGRIIQGLIKAKSSNP-VFVLDEIDKI-- 442
Cdd:cd19526    30 ILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNK---------YIGASEQNVRDLFSRAQSAKPcILFFDEFDSIap 100

                  ....*...
gi 2551685493 443 --GNDFKG 448
Cdd:cd19526   101 krGHDSTG 108
aroK PRK00131
shikimate kinase; Reviewed
361-392 1.69e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 40.17  E-value: 1.69e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2551685493 361 MKSPIICLYGPPGVGKTSLGKSVAEALNRKYI 392
Cdd:PRK00131    2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
346-458 1.75e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.79  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 346 ERIIEHLAVLKLRGDMKSP-IICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHD--------EAEIRGHRRTYIGAM 416
Cdd:pfam13191   6 EEELEQLLDALDRVRSGRPpSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEnlpyspllEALTREGLLRQLLDE 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2551685493 417 PGRIIQGLIKAKssnpvfvLDEIDKIGNDFKGDPASALLEVL 458
Cdd:pfam13191  86 LESSLLEAWRAA-------LLEALAPVPELPGDLAERLLDLL 120
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
337-443 2.16e-03

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 41.56  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 337 DHYGLDKVKERIIEHLAVL-------KLRGDMKSPIIcLYGPPGVGKTSLGKSVAEALNRKYIRISLGglhDEAEIrghr 409
Cdd:PRK10733  153 DVAGCDEAKEEVAELVEYLrepsrfqKLGGKIPKGVL-MVGPPGTGKTLLAKAIAGEAKVPFFTISGS---DFVEM---- 224
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2551685493 410 rtYIGAMPGRIIQGLIKAKSSNPVFV-LDEIDKIG 443
Cdd:PRK10733  225 --FVGVGASRVRDMFEQAKKAAPCIIfIDEIDAVG 257
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
368-443 2.40e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 40.97  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 368 LYGPPGVGKTSLGKSVAEALNRKYIRISLGGLhdeaeirghRRTYI--GAmpgRIIQGLIK-AKSSNP--VFVlDEIDKI 442
Cdd:PRK03992  170 LYGPPGTGKTLLAKAVAHETNATFIRVVGSEL---------VQKFIgeGA---RLVRELFElAREKAPsiIFI-DEIDAI 236

                  .
gi 2551685493 443 G 443
Cdd:PRK03992  237 A 237
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
337-399 3.05e-03

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent 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: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 39.10  E-value: 3.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2551685493 337 DHYGLDKVKERIIEHLAVLKLRGDMKSPI------ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGL 399
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLlrlprsILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTL 69
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
336-519 3.07e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 40.36  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 336 KDHYGLDKVKERIIEHLAVLKLRGDMKSPIIcLYGPPGVGKTSLGKSVAEALNRKyIRISLGGLHDEaeirghrrtyiga 415
Cdd:TIGR00635   4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 416 mPGRIIqGLIKAKSSNPVFVLDEIDKIgndfkgdpASALLEVLDPEQNNTFHDNYID-------IDYDLSKILFIATANN 488
Cdd:TIGR00635  69 -PGDLA-AILTNLEEGDVLFIDEIHRL--------SPAVEELLYPAMEDFRLDIVIGkgpsarsVRLDLPPFTLVGATTR 138
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2551685493 489 LNTISQPLLDRMELI-DISGYIIEEKVEIGRR 519
Cdd:TIGR00635 139 AGMLTSPLRDRFGIIlRLEFYTVEELAEIVSR 170
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
365-392 3.29e-03

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: 39.08  E-value: 3.29e-03
                          10        20
                  ....*....|....*....|....*...
gi 2551685493 365 IICLYGPPGVGKTSLGKSVAEALNRKYI 392
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
AAA_22 pfam13401
AAA domain;
365-446 3.85e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 365 IICLYGPPGVGKTSLGKSVAEAL---NRKYIRISLGGLHDEAEIR----------GHRRTYIGAMPGRIIQGLiKAKSSN 431
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLLrallralglpLSGRLSKEELLAALQQLL-LALAVA 85
                          90
                  ....*....|....*
gi 2551685493 432 PVFVLDEIDKIGNDF 446
Cdd:pfam13401  86 VVLIIDEAQHLSLEA 100
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
337-442 4.40e-03

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 38.68  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 337 DHYGLDKVKERIIEHLAVLKLRGD----MKSPI--ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrr 410
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPElftgLRAPArgLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK-------- 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2551685493 411 tYIGAMPgRIIQGLIK-AKSSNP-VFVLDEIDKI 442
Cdd:cd19524    73 -YVGEGE-KLVRALFAvARELQPsIIFIDEVDSL 104
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
366-440 4.78e-03

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 38.62  E-value: 4.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKYIRISLGGLHDEaeirghrrtYIGAMPGRIIQGLIKAKSSNP-VFVLDEID 440
Cdd:cd19530    33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNK---------YVGESERAVRQVFQRARASAPcVIFFDEVD 99
PRK04195 PRK04195
replication factor C large subunit; Provisional
342-391 4.88e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 40.29  E-value: 4.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2551685493 342 DKVKERIIEHLAVLkLRGDMKSPIIcLYGPPGVGKTSLgksvAEALNRKY 391
Cdd:PRK04195   20 EKAKEQLREWIESW-LKGKPKKALL-LYGPPGVGKTSL----AHALANDY 63
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
365-509 4.91e-03

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: 38.97  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 365 IICLYGPPGVGKTSLGKSVAEALNrkyIRISLGGLHDE-AEIRGHRR-----TYIGAMPGRI---IQGLIKAKsSNPVFV 435
Cdd:cd19508    54 LVLLHGPPGTGKTSLCKALAQKLS---IRLSSRYRYGQlIEINSHSLfskwfSESGKLVTKMfqkIQELIDDK-DALVFV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 436 L-DEIDKIGNDFKGDPAS-----------ALLEVLDpeQNNTFHDNYIdidydlskilfIATANNLNTISQPLLDRMeli 503
Cdd:cd19508   130 LiDEVESLAAARSASSSGtepsdairvvnAVLTQID--RIKRYHNNVI-----------LLTSNLLEKIDVAFVDRA--- 193

                  ....*.
gi 2551685493 504 DISGYI 509
Cdd:cd19508   194 DIKQYI 199
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
366-391 5.60e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.20  E-value: 5.60e-03
                          10        20
                  ....*....|....*....|....*.
gi 2551685493 366 ICLYGPPGVGKTSLGKSVAEALNRKY 391
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKL 26
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
361-436 5.99e-03

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


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 38.55  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 361 MKSP-IICLYGPPGVGKTSLGKSVAEALNRKYIRISlggLHDEAEIRGH-------RRTYIgAMPGRIIQGLIKAKSSNP 432
Cdd:COG4088     1 MDSPmLLILTGPPGSGKTTFAKALAQRLYAEGIAVA---LLHSDDFRRFlvnesfpKETYE-EVVEDVRTTTADNALDNG 76

                  ....
gi 2551685493 433 VFVL 436
Cdd:COG4088    77 YSVI 80
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
345-397 6.23e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 39.73  E-value: 6.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2551685493 345 KERIIEHLAVL----KLRGDmksPI--ICLYGPPGVGKTSLGKSVAEALNRKyIRISLG 397
Cdd:PRK00080   30 QEKVKENLKIFieaaKKRGE---ALdhVLLYGPPGLGKTTLANIIANEMGVN-IRITSG 84
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
348-442 8.38e-03

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: 39.51  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551685493 348 IIEHLAVLKLRGdmkspiICLYGPPGVGKTSLGKSVAEALNRKYIRIslgglhDEAEIRGhrrTYIGAMPGRIIQGLIKA 427
Cdd:TIGR01243 203 LFEHLGIEPPKG------VLLYGPPGTGKTLLAKAVANEAGAYFISI------NGPEIMS---KYYGESEERLREIFKEA 267
                          90
                  ....*....|....*.
gi 2551685493 428 KSSNP-VFVLDEIDKI 442
Cdd:TIGR01243 268 EENAPsIIFIDEIDAI 283
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
365-403 9.79e-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: 37.47  E-value: 9.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2551685493 365 IICLYGPPGVGKTSLGKSVAEALNrkYIRISLGGLHDEA 403
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKLG--LPYLDTGGIRTEE 37
 
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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