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Conserved domains on  [gi|489115162|ref|WP_003025013|]
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MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Citrobacter]

Protein Classification

ATP-dependent zinc metalloprotease FtsH( domain architecture ID 11484915)

ATP-dependent zinc metalloprotease FtsH acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
1-644 0e+00

ATP-dependent zinc metalloprotease FtsH;


:

Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 1321.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   1 MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREAKINGREINVTKKDSNRYTTYIPVNDPKLLDN 80
Cdd:PRK10733   1 MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPVNDPKLLDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  81 LLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEA 160
Cdd:PRK10733  81 LLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
Cdd:PRK10733 161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 241 KKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
Cdd:PRK10733 241 KKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 321 LPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
Cdd:PRK10733 321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
Cdd:PRK10733 401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 481 GAEHVSTGASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRA 560
Cdd:PRK10733 481 GPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 561 RRLLNENMDILHSMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPgSSNNNSGSTGKPSAPRPVDEPRAPDSG-TMSE 639
Cdd:PRK10733 561 RQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEP-GASNNSDDNGTPKAPRPVDEPRTPNPGnTMSE 639

                 ....*
gi 489115162 640 QLGDK 644
Cdd:PRK10733 640 QLGDK 644
 
Name Accession Description Interval E-value
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
1-644 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 1321.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   1 MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREAKINGREINVTKKDSNRYTTYIPVNDPKLLDN 80
Cdd:PRK10733   1 MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPVNDPKLLDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  81 LLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEA 160
Cdd:PRK10733  81 LLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
Cdd:PRK10733 161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 241 KKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
Cdd:PRK10733 241 KKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 321 LPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
Cdd:PRK10733 321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
Cdd:PRK10733 401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 481 GAEHVSTGASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRA 560
Cdd:PRK10733 481 GPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 561 RRLLNENMDILHSMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPgSSNNNSGSTGKPSAPRPVDEPRAPDSG-TMSE 639
Cdd:PRK10733 561 RQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEP-GASNNSDDNGTPKAPRPVDEPRTPNPGnTMSE 639

                 ....*
gi 489115162 640 QLGDK 644
Cdd:PRK10733 640 QLGDK 644
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
11-595 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1122.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  11 IAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREAKINGREINVTKKD--SNRYTTYIPvNDPKLLDNLLTKNVKV 88
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDgtKTRFTTYRV-NDPELVDLLEEKGVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  89 VGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELV 168
Cdd:COG0465   80 TAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGG-GAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 169 EYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCII 248
Cdd:COG0465  159 DFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCII 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 249 FIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGRE 328
Cdd:COG0465  239 FIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGRE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 329 QILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQK 408
Cdd:COG0465  319 AILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 409 ESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGaeHVSTG 488
Cdd:COG0465  399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTG 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 489 ASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRARRLLNENM 568
Cdd:COG0465  477 ASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENR 556
                        570       580
                 ....*....|....*....|....*..
gi 489115162 569 DILHSMKDALMKYETIDAPQIDDLMAR 595
Cdd:COG0465  557 DKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
99-594 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 932.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   99 LASIFISWFP-MLLLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRF 177
Cdd:TIGR01241   2 LLGFLFSLLPpILLLVGVWFFFRRQMQGGGG-RAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  178 QKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVG 257
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  258 RQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRR 337
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  338 VPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAG 417
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  418 HAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGaeHVSTGASNDIKVAT 497
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  498 NLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRARRLLNENMDILHSMKDA 577
Cdd:TIGR01241 399 NIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*..
gi 489115162  578 LMKYETIDAPQIDDLMA 594
Cdd:TIGR01241 479 LLEKETITREEIKELLA 495
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
149-319 8.31e-128

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: 373.88  E-value: 8.31e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 149 TTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489115162 309 RPGRFDRQVVV 319
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
401-592 7.02e-97

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 295.28  E-value: 7.02e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  481 GaeHVSTGASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRA 560
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 489115162  561 RRLLNENMDILHSMKDALMKYETIDAPQIDDL 592
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
185-323 1.56e-21

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: 91.28  E-value: 1.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   185 PKGVLMVGPPGTGKTLLAKAIAGEAKVP---FFTISGSDFVE--------------MFVGVGASRVRDMFEQAKKAAPCI 247
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115162   248 IFIDEIDAvgrqrgagLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPgRFDRQVVVGLPD 323
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
188-223 1.42e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.53  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEA-----KVPFFTIsgSDFVE 223
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
 
Name Accession Description Interval E-value
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
1-644 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 1321.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   1 MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREAKINGREINVTKKDSNRYTTYIPVNDPKLLDN 80
Cdd:PRK10733   1 MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPVNDPKLLDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  81 LLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEA 160
Cdd:PRK10733  81 LLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
Cdd:PRK10733 161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 241 KKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
Cdd:PRK10733 241 KKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 321 LPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
Cdd:PRK10733 321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
Cdd:PRK10733 401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 481 GAEHVSTGASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRA 560
Cdd:PRK10733 481 GPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 561 RRLLNENMDILHSMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPgSSNNNSGSTGKPSAPRPVDEPRAPDSG-TMSE 639
Cdd:PRK10733 561 RQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEP-GASNNSDDNGTPKAPRPVDEPRTPNPGnTMSE 639

                 ....*
gi 489115162 640 QLGDK 644
Cdd:PRK10733 640 QLGDK 644
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
11-595 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1122.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  11 IAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREAKINGREINVTKKD--SNRYTTYIPvNDPKLLDNLLTKNVKV 88
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDgtKTRFTTYRV-NDPELVDLLEEKGVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  89 VGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELV 168
Cdd:COG0465   80 TAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGG-GAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 169 EYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCII 248
Cdd:COG0465  159 DFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCII 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 249 FIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGRE 328
Cdd:COG0465  239 FIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGRE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 329 QILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQK 408
Cdd:COG0465  319 AILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 409 ESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGaeHVSTG 488
Cdd:COG0465  399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTG 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 489 ASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRARRLLNENM 568
Cdd:COG0465  477 ASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENR 556
                        570       580
                 ....*....|....*....|....*..
gi 489115162 569 DILHSMKDALMKYETIDAPQIDDLMAR 595
Cdd:COG0465  557 DKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
99-594 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 932.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   99 LASIFISWFP-MLLLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRF 177
Cdd:TIGR01241   2 LLGFLFSLLPpILLLVGVWFFFRRQMQGGGG-RAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  178 QKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVG 257
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  258 RQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRR 337
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  338 VPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAG 417
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  418 HAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGaeHVSTGASNDIKVAT 497
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  498 NLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRARRLLNENMDILHSMKDA 577
Cdd:TIGR01241 399 NIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*..
gi 489115162  578 LMKYETIDAPQIDDLMA 594
Cdd:TIGR01241 479 LLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
3-601 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 652.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   3 KNLILW-LVIAVVLMSVFQSF----------GPSESNGRK------VDYSTFLQEVNQDQVREAKI--NGREI---NVTK 60
Cdd:CHL00176   6 KYAILIsLPLIVEKFTVWDVFyyssvedglkSPNNPDVVQnkassrMTYGRFLEYLDMGWIKKVDLydNGRTAiveASSP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  61 KDSNRYTTY---IPVNDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISW-FPMLLLIGVWIFFMR--QMQGGGGKGAMSF 134
Cdd:CHL00176  86 ELGNRPQRIrveLPVGASELIQKLKEANIDFDAHPPVLKSNIVTILSNLlLPLILIGVLWFFFQRssNFKGGPGQNLMNF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 135 GKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
Cdd:CHL00176 166 GKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVI 294
Cdd:CHL00176 246 SISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVI 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 295 AATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
Cdd:CHL00176 326 AATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTAR 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 375 GNKRVVSMVEFEKAKDKIMMGAERRSMVMTEaQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDA 454
Cdd:CHL00176 406 RKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQ 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 455 ISASRQKLESQISTLYGGRLAEEIIYGAEHVSTGASNDIKVATNLARNMVTQWGFSdKLGPL-LYAEEEGEVFLGRSVAK 533
Cdd:CHL00176 485 SLVSRSQILARIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPIsLESNNSTDPFLGRFMQR 563
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115162 534 AKHMSDETARIIDQEVKLLIERNYDRARRLLNENMDILHSMKDALMKYETIDAPQIDDLMARRDVRPP 601
Cdd:CHL00176 564 NSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILPP 631
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
149-319 8.31e-128

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: 373.88  E-value: 8.31e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 149 TTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489115162 309 RPGRFDRQVVV 319
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
149-398 1.36e-114

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 345.84  E-value: 1.36e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 149 TTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPAL 307
Cdd:COG1222  155 EGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD--GTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPAL 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 308 LRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEK 387
Cdd:COG1222  233 LRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEK 312
                        250
                 ....*....|.
gi 489115162 388 AKDKIMMGAER 398
Cdd:COG1222  313 AIEKVKKKTET 323
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
150-406 8.24e-101

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 312.54  E-value: 8.24e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
Cdd:PRK03992 129 TYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGE 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
Cdd:PRK03992 209 GARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAIL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388
Cdd:PRK03992 289 RPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKA 368
                        250
                 ....*....|....*...
gi 489115162 389 KDKIMMGAERRSMVMTEA 406
Cdd:PRK03992 369 IEKVMGKEEKDSMEEPGV 386
Peptidase_M41 pfam01434
Peptidase family M41;
401-592 7.02e-97

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 295.28  E-value: 7.02e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  401 MVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIY 480
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  481 GaeHVSTGASNDIKVATNLARNMVTQWGFSDKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKLLIERNYDRA 560
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 489115162  561 RRLLNENMDILHSMKDALMKYETIDAPQIDDL 592
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
141-393 7.54e-88

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 278.22  E-value: 7.54e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
Cdd:TIGR01242 111 MEVEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
Cdd:TIGR01242 191 ELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNR 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
Cdd:TIGR01242 271 PDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY 350
                         250
                  ....*....|....
gi 489115162  380 VSMVEFEKAKDKIM 393
Cdd:TIGR01242 351 VTMDDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
151-398 1.46e-81

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: 262.92  E-value: 1.46e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 151 FADVAGCDEAKEEVAELVEYLRE-PSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaGLGGGHDEREqtLNQMLVEMDGFEGNegIIVIAATNRPDVLDPALLR 309
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELRSD--VVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 310 pgRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAK 389
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ....*....
gi 489115162 390 DKIMMGAER 398
Cdd:COG0464  389 EREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
153-392 4.39e-71

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: 244.05  E-value: 4.39e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231
Cdd:TIGR01243 454 DIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEK 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEReqTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPG 311
Cdd:TIGR01243 534 AIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPG 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  312 RFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARG---------------- 375
Cdd:TIGR01243 612 RFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigspakeklevgeee 691
                         250
                  ....*....|....*....
gi 489115162  376 --NKRVVSMVEFEKAKDKI 392
Cdd:TIGR01243 692 flKDLKVEMRHFLEALKKV 710
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
160-317 8.47e-68

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: 218.31  E-value: 8.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 160 AKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQ 239
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115162 240 AKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQV 317
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
150-317 2.24e-67

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: 217.59  E-value: 2.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*....
gi 489115162 309 RPGRFDRQV 317
Cdd:cd19502  161 RPGRFDRKI 169
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
148-374 3.81e-66

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: 230.56  E-value: 3.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  148 KTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFV 226
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  227 GVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGgghDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPA 306
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115162  307 LLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
151-392 7.05e-65

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 213.98  E-value: 7.05e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 151 FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 231 SRVRDMFEQAKKaAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFegNEGIIVIAATNRPDVLDPALLRp 310
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 311 gRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKD 390
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 ..
gi 489115162 391 KI 392
Cdd:COG1223  234 QR 235
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
137-388 1.63e-63

26S protease regulatory subunit 6B-like protein; Provisional


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 215.40  E-value: 1.63e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 137 SKARMLT-EDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
Cdd:PTZ00454 129 SSIQLLQmSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFI 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVI 294
Cdd:PTZ00454 209 RVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVI 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 295 AATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
Cdd:PTZ00454 289 MATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVR 368
                        250
                 ....*....|....
gi 489115162 375 GNKRVVSMVEFEKA 388
Cdd:PTZ00454 369 KNRYVILPKDFEKG 382
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
160-319 2.07e-61

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: 201.36  E-value: 2.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 160 AKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFE 238
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 239 QAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEReqTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVV 318
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 489115162 319 V 319
Cdd:cd19511  159 V 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
150-393 1.47e-60

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 208.47  E-value: 1.47e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLSPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                 ....*
gi 489115162 389 KDKIM 393
Cdd:PTZ00361 421 KEKVL 425
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
153-319 2.25e-58

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: 193.66  E-value: 2.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglggGHDEREQTL-NQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRP 310
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 489115162 311 GRFDRQVVV 319
Cdd:cd19503  157 GRFDREVEI 165
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
161-319 1.45e-56

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in 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 second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 188.49  E-value: 1.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 161 KEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQ 239
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 240 AKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVV 319
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
188-321 4.17e-56

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: 186.26  E-value: 4.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglGGG 267
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489115162  268 HDEREQTLNQMLVEMDGFEGNEG-IIVIAATNRPDVLDPALLrpGRFDRQVVVGL 321
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
160-319 1.38e-55

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: 186.16  E-value: 1.38e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 160 AKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFE 238
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 239 QAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEReqTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVV 318
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 489115162 319 V 319
Cdd:cd19529  159 I 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
153-320 2.76e-53

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 179.94  E-value: 2.76e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglggGHDEREQTL-NQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRP 310
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156
                        170
                 ....*....|
gi 489115162 311 GRFDRQVVVG 320
Cdd:cd19519  157 GRFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
167-319 6.56e-49

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: 168.05  E-value: 6.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 167 LVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPC 246
Cdd:cd19530   12 ILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115162 247 IIFIDEIDAVGRQRGAGLGGGhdeREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVV 319
Cdd:cd19530   92 VIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
153-317 1.56e-47

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: 164.50  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELVEYLREPSR-FQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglGGGHDEREQTLNQMLVEMDGFEGNE----GIIVIAATNRPDVLDPAL 307
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 489115162 308 LRPGRFDRQV 317
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
160-317 1.98e-45

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: 158.75  E-value: 1.98e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 160 AKEEVAELVEYLRE-PSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFE 238
Cdd:cd19526    1 VKKALEETIEWPSKyPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 239 QAKKAAPCIIFIDEIDAVGRQRgaglggGHDER---EQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDR 315
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKR------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154

                 ..
gi 489115162 316 QV 317
Cdd:cd19526  155 LV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
161-319 4.84e-43

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 152.28  E-value: 4.84e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 161 KEEVAELVEY-LREPSRFQKlGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQ 239
Cdd:cd19527    2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 240 AKKAAPCIIFIDEIDAVGRQRGA-GLGGGHDEReqTLNQMLVEMDGFE-GNEGIIVIAATNRPDVLDPALLRPGRFDRQV 317
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 489115162 318 VV 319
Cdd:cd19527  159 YL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
154-319 1.24e-41

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: 148.27  E-value: 1.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 154 VAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRV 233
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 234 RDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFEG--NEGIIVIAATNRPDVLDPALLRpg 311
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVLNkpEDRVLVLGATNRPWELDEAFLR-- 155

                 ....*...
gi 489115162 312 RFDRQVVV 319
Cdd:cd19509  156 RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
153-316 1.72e-36

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 134.56  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIA-----GEAKVPFFTISGSDFVEMFV 226
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 227 GVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLnqmLVEMDGFEGNEGIIVIAATNRPDVLDPA 306
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTL---LALMDGLDNRGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|
gi 489115162 307 LLRPGRFDRQ 316
Cdd:cd19517  158 LRRPGRFDRE 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
151-319 1.34e-34

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 129.21  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 151 FADVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227
Cdd:cd19521    6 WEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGF-EGNEGIIVIAATNRPDVLDPA 306
Cdd:cd19521   83 ESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 489115162 307 LLRpgRFDRQVVV 319
Cdd:cd19521  160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
153-313 2.12e-34

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: 128.31  E-value: 2.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLG-GKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGF--EGNEGIIVIAATNRPDVLDPALL 308
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAIL 157

                 ....*..
gi 489115162 309 R--PGRF 313
Cdd:cd19520  158 RrmPKRF 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
153-319 1.33e-33

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 126.25  E-value: 1.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELVEY-LREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEG---NEG----IIVIAATNRPDVL 303
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGaseNDDpskmVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 489115162 304 DPALLRpgRFDRQVVV 319
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
151-319 1.11e-32

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 124.33  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 151 FADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229
Cdd:cd19525   21 WADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGF--EGNEGIIVIAATNRPDVLDPAL 307
Cdd:cd19525  100 EKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAA 176
                        170
                 ....*....|..
gi 489115162 308 LRpgRFDRQVVV 319
Cdd:cd19525  177 RR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
153-319 9.00e-32

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: 121.11  E-value: 9.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAELV--EYLRePSRFQKLGGKiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230
Cdd:cd19524    1 DIAGQDLAKQALQEMVilPSLR-PELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFEGN--EGIIVIAATNRPDVLDPALL 308
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 489115162 309 RpgRFDRQVVV 319
Cdd:cd19524  156 R--RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
155-321 2.69e-31

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: 119.17  E-value: 2.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 155 AGCDEAKEEVAELVEYlrepsrfqklggKIPKGVLMVGPPGTGKTLLAKAIAGEA---KVPFFTISGSDFVEMFVG---V 228
Cdd:cd00009    1 VGQEEAIEALREALEL------------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRqrgaglggghDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|...
gi 489115162 309 RPGRFDRQVVVGL 321
Cdd:cd00009  139 LYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
174-317 2.19e-30

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, 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: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 117.59  E-value: 2.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 174 PSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAI-----AGEAKVpfftISGSDFVEMFVGVGASRVRDMF-----EQAKKA 243
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeEQRRLG 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115162 244 APC---IIFIDEIDAVGRQRGAGlGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQV 317
Cdd:cd19504  100 ANSglhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
136-378 1.15e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 120.12  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 136 KSKARMLTEDQI------KTTFADVAGCDEAKEevaelveYLREPSR-FQK----LGGKIPKGVLMVGPPGTGKTLLAKA 204
Cdd:CHL00195 206 EEKKQIISQTEIlefysvNEKISDIGGLDNLKD-------WLKKRSTsFSKqasnYGLPTPRGLLLVGIQGTGKSLTAKA 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 205 IAGEAKVPFFTIsgsDFVEMF---VGVGASRVRDMFEQAKKAAPCIIFIDEID-AVGRQRGAGLGGghdereqTLNQMLV 280
Cdd:CHL00195 279 IANDWQLPLLRL---DVGKLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLA 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 281 EMDGF--EGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRV-PLS-PDIDAAIIARGTPGF 356
Cdd:CHL00195 349 TFITWlsEKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKF 428
                        250       260
                 ....*....|....*....|..
gi 489115162 357 SGADLANLVNEaALFAARGNKR 378
Cdd:CHL00195 429 SGAEIEQSIIE-AMYIAFYEKR 449
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
153-315 5.01e-23

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 95.90  E-value: 5.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVAElveylREPS---RFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229
Cdd:cd19507    1 DVGGLDNLKDWLKK-----RKAAfskQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 230 ASRVRDMFEQAKKAAPCIIFIDEID-AVGrqrGAGLGGGHDEREQTLNQMLVEMDgfEGNEGIIVIAATNRPDVLDPALL 308
Cdd:cd19507   76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFS---NADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELL 150

                 ....*..
gi 489115162 309 RPGRFDR 315
Cdd:cd19507  151 RKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
185-323 1.56e-21

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: 91.28  E-value: 1.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   185 PKGVLMVGPPGTGKTLLAKAIAGEAKVP---FFTISGSDFVE--------------MFVGVGASRVRDMFEQAKKAAPCI 247
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115162   248 IFIDEIDAvgrqrgagLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPgRFDRQVVVGLPD 323
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
153-319 1.36e-18

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: 83.40  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 153 DVAGCDEAKEEVA-ELVEYLREPSRFQKLGgKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 232 RVRDMFEQAKKAAPCIIFIDEIDAV--GRQRGAGLGGghdeREQTlnQMLVEMDGF--EGNEGIIVIAATNRPDVLDPAL 307
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESL 153
                        170
                 ....*....|..
gi 489115162 308 LRpgRFDRQVVV 319
Cdd:cd19523  154 RR--YFSKRLLV 163
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
164-319 8.23e-17

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. 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: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 77.78  E-value: 8.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 164 VAELVEYLREPSRFQKLGgkIP--KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDfvemfVGVGASRVRDMFEQAK 241
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRG--IPyrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 242 KAApcIIFIDEIDAV---GRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVV 318
Cdd:cd19510   75 KQS--IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIY 152

                 .
gi 489115162 319 V 319
Cdd:cd19510  153 M 153
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
5-93 1.38e-16

FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes. It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress, and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear.


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 75.72  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162    5 LILWLVIAVVLMSVFQSF-GPSESNGRKVDYSTFLQEVNQDQVREAKINGREIN------VTKKDSNRYTTYIPVN---- 73
Cdd:pfam06480   1 LLLWLLILLVLLLLFLLFlLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILptgvveGTLKDGSKFTTYFIPSlpnv 80
                          90       100
                  ....*....|....*....|...
gi 489115162   74 ---DPKLLDNLLTKNVKVVGEPP 93
Cdd:pfam06480  81 dslLEKLEDALEEKGVKVSVKPP 103
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
179-315 3.73e-15

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. 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: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 73.18  E-value: 3.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 179 KLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFV--------------EMFVGVGASRVRDMFEQAKKAA 244
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489115162 245 PCIIFIDEIDAVGRQRgaglgGGHDEREQT---LNQMLVEM-DGFEGNE--GIIVIAATNRPDVLDPALLRPGRFDR 315
Cdd:cd19505   86 PCIIWIPNIHELNVNR-----STQNLEEDPkllLGLLLNYLsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
186-317 6.38e-12

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. 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: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 63.70  E-value: 6.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 186 KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGL 264
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTSRRgLLLFVDEADAFLRKR-STE 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489115162 265 GGGHDEReQTLNQMLVEMDgfEGNEGIIVIAATNRPDVLDPALlrPGRFDRQV 317
Cdd:cd19512  101 KISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
PRK04195 PRK04195
replication factor C large subunit; Provisional
149-254 8.23e-12

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 68.02  E-value: 8.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 149 TTFADVAGCDEAKEEVAELVEylrepsRFQKlgGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDF-----VE 223
Cdd:PRK04195  11 KTLSDVVGNEKAKEQLREWIE------SWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489115162 224 MFVGvGASRVRDMFEQAKKaapcIIFIDEID 254
Cdd:PRK04195  83 RVAG-EAATSGSLFGARRK----LILLDEVD 108
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
154-269 9.70e-12

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 63.94  E-value: 9.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 154 VAGCDEAKEEVAELveyLREPSRFQKLGGKI-----PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVG 227
Cdd:cd19498   13 IIGQDEAKRAVAIA---LRNRWRRMQLPEELrdevtPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489115162 228 VGA-SRVRDMFEQakkaapcIIFIDEIDAVGRQRGaglGGGHD 269
Cdd:cd19498   90 RDVeSIIRDLVEG-------IVFIDEIDKIAKRGG---SSGPD 122
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
343-387 1.20e-10

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 56.78  E-value: 1.20e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 489115162  343 DIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEK 387
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
192-253 2.07e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.18  E-value: 2.07e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115162 192 GPPGTGKTLLAKAIAGEAKVPFFTISGSDFvemfvgvGASRVRDMFEQAKKAA----PCIIFIDEI 253
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
192-253 3.18e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 62.77  E-value: 3.18e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115162 192 GPPGTGKTLLAKAIAGEAKVPFFTISGsdfvemfVGVGASRVRDMFEQAKKAA----PCIIFIDEI 253
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
187-313 2.22e-09

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 56.15  E-value: 2.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  187 GVLMVGPPGTGKTLLAKAIAgEA--KVPFFTISGSDFVE-------MFVGVGASRVRDmfEQAKKAA--PCIIFIDEIDA 255
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVD--GPLVRAAreGEIAVLDEINR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489115162  256 VGRQRGAGLGGGHDEREqtlnqmLVEMDGFE----GNEGIIVIAATNRPD----VLDPALLRpgRF 313
Cdd:pfam07728  78 ANPDVLNSLLSLLDERR------LLLPDGGElvkaAPDGFRLIATMNPLDrglnELSPALRS--RF 135
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
159-221 6.38e-09

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 58.44  E-value: 6.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489115162 159 EAKEEVAELVEYLREpsrfQKLGGKipkGVLMVGPPGTGKTLLAKAIAGE--AKVPFFTISGSDF 221
Cdd:COG1224   45 EAREAAGIVVKMIKE----GKMAGK---GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
152-258 1.07e-08

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: 55.26  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 152 ADVAGCDEAKEEVaelVEYLREPSRFQKLGGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS-G--SDFVEM---- 224
Cdd:cd19500   10 ADHYGLEDVKERI---LEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghr 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489115162 225 --FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGR 258
Cdd:cd19500   84 rtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
156-221 1.08e-07

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 54.24  E-value: 1.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115162  156 GCDEAKEEVAELVEYLREpsrfQKLGGKipkGVLMVGPPGTGKTLLAKAIAGE--AKVPFFTISGSDF 221
Cdd:pfam06068  28 GQEKAREAAGVIVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
188-304 2.11e-07

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 49.81  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVgvgaSRVRDMFEQAKkaaPCIIFIDEIDAVGRQRGAglggg 267
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARASQG----- 68
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489115162 268 hDEREQTLNQMLVEMDGFeGNEGIIVIAATNRPDVLD 304
Cdd:cd01120   69 -DRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI 103
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
138-317 1.48e-06

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 51.38  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  138 KARMLTEDQikTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIP---KGVLMVGPPGTGKTLLAKAIA------GE 208
Cdd:TIGR03922 264 KAKLLAEAE--AELAEQIGLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiycglGV 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  209 AKVP-FFTISGSDFVEMFVGVGASRVRDMFEqakKAAPCIIFIDEIDAVGRQRGaglGGGHDEREQTLNQMLVEM--DGF 285
Cdd:TIGR03922 342 LRKPlVREVSRADLIGQYIGESEAKTNEIID---SALGGVLFLDEAYTLVETGY---GQKDPFGLEAIDTLLARMenDRD 415
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489115162  286 EgnegIIVIAATNRPDvLDPAL-----LRpGRFDRQV 317
Cdd:TIGR03922 416 R----LVVIGAGYRKD-LDKFLevnegLR-SRFTRVI 446
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
154-258 2.48e-06

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 49.14  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 154 VAGCDEAKEEVAELV--EYLR--EPSRFQKLGGKIPKG-VLMVGPPGTGKTLLAKAIAGEAKVPF-------FTISGsdf 221
Cdd:cd19497   14 VIGQERAKKVLSVAVynHYKRirNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFaiadattLTEAG--- 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489115162 222 vemFVGVGASRVRDMFEQA-----KKAAPCIIFIDEIDAVGR 258
Cdd:cd19497   91 ---YVGEDVENILLKLLQAadydvERAQRGIVYIDEIDKIAR 129
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
188-258 7.04e-06

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 48.62  E-value: 7.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPF-------FTISGsdfvemFVGvgasrvrdmfE----------QA-----KKAAP 245
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPFaiadattLTEAG------YVG----------EdvenillkllQAadydvEKAQR 174
                         90
                 ....*....|...
gi 489115162 246 CIIFIDEIDAVGR 258
Cdd:PRK05342 175 GIVYIDEIDKIAR 187
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
188-258 8.92e-06

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 48.51  E-value: 8.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPfFTIS--------GsdfvemFVGvgasrvrdmfE----------QA-----KKAA 244
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteaG------YVG----------EdvenillkllQAadydvEKAE 174
                         90
                 ....*....|....
gi 489115162 245 PCIIFIDEIDAVGR 258
Cdd:COG1219  175 RGIIYIDEIDKIAR 188
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
188-253 1.67e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.43  E-value: 1.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDFVEMFVGVGAsrvRDmfeqakkaapcIIFIDEI 253
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI 111
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
188-351 2.67e-05

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: 46.31  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDFVEMFVGVGASRVRDM-----FEQakkaapcIIFIDEIDav 256
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpSDILGTYIYDQQTGEFEFrpgplFAN-------VLLADEIN-- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 257 grqRGaglggghdeREQTLNQML-------VEMDG--FEGNEGIIVIAATNRPDV-----LDPALLRpgRFDRQVVVGLP 322
Cdd:COG0714  105 ---RA---------PPKTQSALLeameerqVTIPGgtYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYP 170
                        170       180       190
                 ....*....|....*....|....*....|.
gi 489115162 323 DVRGREQILKVHMRR--VPLSPDIDAAIIAR 351
Cdd:COG0714  171 DAEEEREILRRHTGRhlAEVEPVLSPEELLA 201
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
188-307 2.87e-05

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: 45.52  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPF-FTISGSDFVEM--------FVGVGASRVRDMFEQAKKAAP---CIIF--IDEI 253
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQELIDdkdALVFvlIDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489115162 254 DAVGRQRGAGLGGGH-DEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPAL 307
Cdd:cd19508  135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
186-253 3.23e-05

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.93  E-value: 3.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489115162 186 KGVLMVGPPGTGKTLLAKAIAGEA-----KVPFFTIsgSDFV-EMFVGVGASRVRDMFEQAKKaAPCIIfIDEI 253
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLVnELKEARADGRLERLLKRLAK-VDLLI-LDEL 169
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
185-254 3.65e-05

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: 44.49  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  185 PKGV-LMVGPPGTGKTLLAKAIAGE---AKVPFFTISGSDFVE-----MFVG-----VGASRVRDMFEQAKKAAPCIIFI 250
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 489115162  251 DEID 254
Cdd:pfam07724  82 DEIE 85
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
183-253 5.21e-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: 5.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 183 KIPKGVLMVGPPGTGKT----LLAKAIAGEAKVPFFTI------SGSDFVEMFVGVGAS---RVRD-MFEQA-KKAA--- 244
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVqfhpswSYEDFLLGYRPSLDEgkyEPTPgIFLRFcLKAEknp 298
                         90
                 ....*....|.
gi 489115162 245 --PCIIFIDEI 253
Cdd:COG1401  299 dkPYVLIIDEI 309
44 PHA02544
clamp loader, small subunit; Provisional
182-390 8.47e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 44.98  E-value: 8.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 182 GKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS----DFVEMFVGVGASRVrdmfeqAKKAAPCIIFIDEIDavg 257
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV------SLTGGGKVIIIDEFD--- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 258 rqrGAGLGGGHDEreqtlnqMLVEMDGFEGNEGIIVIAatNRPDVLDPALLrpGRFdRQVVVGLPDVRGREQILKVHMRR 337
Cdd:PHA02544 111 ---RLGLADAQRH-------LRSFMEAYSKNCSFIITA--NNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMMKQMIVR 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115162 338 ---------VPLSPDIDAAIIARGTPgfsgaDLANLVNEAALFAARG-----------NKRVVSMVEFEKAKD 390
Cdd:PHA02544 176 ckgileaegVEVDMKVLAALVKKNFP-----DFRRTINELQRYASTGkidagilsevtNSDIDDVVEALKAKD 243
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
188-207 1.42e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 44.65  E-value: 1.42e-04
                         10        20
                 ....*....|....*....|
gi 489115162 188 VLMVGPPGTGKTLLAKAIAG 207
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
162-304 1.62e-04

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 44.45  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 162 EEVAELVEYLREPsrfqkLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAK-------VPFFTI------------------ 216
Cdd:COG1474   33 EEIEELASALRPA-----LRGERPSNVLIYGPTGTGKTAVAKYVLEELEeeaeergVDVRVVyvncrqastryrvlsril 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 217 ----SGSDFVEmfVGVGASRVRDMFEQA--KKAAPCIIFIDEIDAVgrqrgaglggGHDEREQTLNQMLVEMDGFEGNE- 289
Cdd:COG1474  108 eelgSGEDIPS--TGLSTDELFDRLYEAldERDGVLVVVLDEIDYL----------VDDEGDDLLYQLLRANEELEGARv 175
                        170
                 ....*....|....*
gi 489115162 290 GIIVIaaTNRPDVLD 304
Cdd:COG1474  176 GVIGI--SNDLEFLE 188
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
183-319 2.38e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 41.85  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 183 KIPKG--VLMVGPPGTGKTLLAKAIAGEAKVP--FFTISGSDFVEMFVGVGASRVRDMFE----QAKKAA--------PC 246
Cdd:cd00267   21 TLKAGeiVALVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIGYVPQlsggQRQRVAlaralllnPD 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489115162 247 IIFIDEIDavgrqrgAGLgggHDEREQTLNQMLVEMdgfeGNEGIIVIAATNRPDVLDPAllrpgrFDRQVVV 319
Cdd:cd00267  101 LLLLDEPT-------SGL---DPASRERLLELLREL----AEEGRTVIIVTHDPELAELA------ADRVIVL 153
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
154-254 3.59e-04

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: 41.78  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 154 VAGCDEAKEEVAELVEY----LREPSRfqklggkiPKGVLM-VGPPGTGKTLLAKAIAGE---AKVPFFTISGSDFVEMF 225
Cdd:cd19499   13 VVGQDEAVKAVSDAIRRaragLSDPNR--------PIGSFLfLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKH 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115162 226 VG----------VGASRVRDMFEQAKKAAPCIIFIDEID 254
Cdd:cd19499   85 SVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
151-207 4.53e-04

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 41.75  E-value: 4.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489115162  151 FADVAGCDEAKE--EVAelveylrepsrfqKLGGKipkGVLMVGPPGTGKTLLAKAIAG 207
Cdd:pfam01078   2 LADVKGQEQAKRalEIA-------------AAGGH---NLLMIGPPGSGKTMLAKRLPG 44
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
150-218 7.96e-04

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.56  E-value: 7.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489115162  150 TFADVAGCDEAKEEVAELVEYLRepSRfqklgGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISG 218
Cdd:pfam05496   5 TLDEYIGQEKVKENLKIFIEAAK--QR-----GEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
188-259 1.29e-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: 41.13  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489115162  188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDFVEMFVGVGAsrvRDmfeqakkaapcIIFIDEIDAVGRQ 259
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEIHRLSPA 96
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
188-262 1.34e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 40.38  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 188 VLMVGPPGTGKT-LLAKAIAGEAK----------VPFFTISGSDFVEMFVGV-GASRVRDMFEQA-KKAAPCIIFIdeID 254
Cdd:cd04105    3 VLLLGPSDSGKTaLFTKLTTGKVRstvtsiepnvASFYSNSSKGKKLTLVDVpGHEKLRDKLLEYlKASLKAIVFV--VD 80

                 ....*...
gi 489115162 255 AVGRQRGA 262
Cdd:cd04105   81 SATFQKNI 88
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
188-223 1.42e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.53  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEA-----KVPFFTIsgSDFVE 223
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
166-309 2.05e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 41.33  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 166 ELVEYLREPSRFQKLGGKIPKgVLMVGPPGTGKTLLAKAIA---------GEAKVPFF----TISGS----DFVEMFVGV 228
Cdd:COG5635  162 NLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrDLAEEasleDLLAEALEK 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQrgaglggghDEREQTLNQMLVEMDGFEGNEGIIviaaTNRPDVLDPALL 308
Cdd:COG5635  241 RGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII----TSRPEGYDSSEL 307

                 .
gi 489115162 309 R 309
Cdd:COG5635  308 E 308
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
161-255 2.24e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 40.34  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 161 KEEVAELVEYLREpsrfqklgGKIPKGVLMVGPPGTGKTLLAKAIA----GEAKVP-----------FFTISGSDFVEMF 225
Cdd:COG0470    2 EEAWEQLLAAAES--------GRLPHALLLHGPPGIGKTTLALALArdllCENPEGgkacgqchsrlMAAGNHPDLLELN 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489115162 226 VGV-----GASRVRDMFEQAKKAAPC----IIFIDEIDA 255
Cdd:COG0470   74 PEEksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADA 112
rfc PRK00440
replication factor C small subunit; Reviewed
150-255 2.76e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 40.24  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 150 TFADVAGCDEAKEEVAELVEylrepsrfqklGGKIPKgVLMVGPPGTGKTLLAKAIAGEakvpfftISGSDFVEMFVGVG 229
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTTAALALARE-------LYGEDWRENFLELN 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489115162 230 AS--R----VRDMFEQAKKAAPC------IIFIDEIDA 255
Cdd:PRK00440  76 ASdeRgidvIRNKIKEFARTAPVggapfkIIFLDEADN 113
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
180-209 2.93e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 39.51  E-value: 2.93e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489115162 180 LGGKIPKG--VLMVGPPGTGKTLLAKAIAGEA 209
Cdd:COG0467   13 LGGGLPRGssTLLSGPPGTGKTTLALQFLAEG 44
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
152-238 3.08e-03

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 40.69  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 152 ADVAGCDEAKEEVaelVEYLREPSRFQKLGGKIpkgVLMVGPPGTGKTLLAKAIAgeakvpffTISGSDFVEMFVGvgas 231
Cdd:PRK10787 322 TDHYGLERVKDRI---LEYLAVQSRVNKIKGPI---LCLVGPPGVGKTSLGQSIA--------KATGRKYVRMALG---- 383

                 ....*..
gi 489115162 232 RVRDMFE 238
Cdd:PRK10787 384 GVRDEAE 390
IcmF COG3523
Type VI protein secretion system component VasK [Intracellular trafficking, secretion, and ...
86-199 4.52e-03

Type VI protein secretion system component VasK [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442745 [Multi-domain]  Cd Length: 1192  Bit Score: 40.32  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162   86 VKVVGEPPEEPSLLASIFIswFPMLLLIGVWIFFMRQmqggggkgamsFGKSKARMLtEDQIKTTFADVAGCDEAKEEVA 165
Cdd:COG3523    31 LAIGDYRPLESVLVRLLAI--AVILLLWLLVWLVRRW-----------RARRANRAL-EDALAEQAEEKAAADPSREEIE 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489115162  166 ELVEYLREP------SRFQKLGGKipKGV------LMVGPPGTGKT 199
Cdd:COG3523    97 ALRERFQEAlatlkkSRLGQGGGR--RALyelpwyLIIGPPGAGKT 140
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
145-372 4.65e-03

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 39.95  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 145 DQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPK------GVLMVGPPGTGKTLLAKAI---AGEAKVPFFT 215
Cdd:COG2204  108 EELLAAVERALERRRLRRENAEDSGLIGRSPAMQEVRRLIEKvapsdaTVLITGESGTGKELVARAIhrlSPRADGPFVA 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 216 ISGSDFV------EMFVGV-----GASRVRD-MFEQAKKaapCIIFIDEIDAVGRQRGAGLGGGHDEREqtlnqmlVEMD 283
Cdd:COG2204  188 VNCAAIPeellesELFGHEkgaftGAVARRIgKFELADG---GTLFLDEIGEMPLALQAKLLRVLQERE-------FERV 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 284 GfeGNEGIIV----IAATNRPdvLDpALLRPGRFDR-------QVVVGLPDVRGR------------EQILKVHMRRVPL 340
Cdd:COG2204  258 G--GNKPIPVdvrvIAATNRD--LE-ELVEEGRFREdlyyrlnVFPIELPPLRERredipllarhflARFAAELGKPVKL 332
                        250       260       270
                 ....*....|....*....|....*....|..
gi 489115162 341 SPDIDAAIIARGTPGfSGADLANLVNEAALFA 372
Cdd:COG2204  333 SPEALEALLAYDWPG-NVRELENVIERAVILA 363
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
180-243 5.22e-03

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 38.78  E-value: 5.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489115162 180 LGGKIPKG--VLMVGPPGTGKTL-----LAKAIAGEAKVPFFTisgsdFVEmfvgvgasRVRDMFEQAKKA 243
Cdd:cd01124   12 LGGGIPKGsvTLLTGGPGTGKTLfglqfLYAGAKNGEPGLFFT-----FEE--------SPERLLRNAKSF 69
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
188-218 5.34e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 5.34e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 489115162 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG 218
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
192-344 7.35e-03

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.02  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 192 GPPGTGKTLLAKAIAGEAKVPFFT-----ISGSDFVEMFvgVGASRVRDMFEQAKKAAPC-IIFIDEIdavgrQRGAGlg 265
Cdd:COG0593   41 GGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDF--INAIRNNTIEEFKEKYRSVdVLLIDDI-----QFLAG-- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162 266 gghDEREQ-----TLNqMLVEMDGFegnegiIVIAATNRP---DVLDPALLRpgRFDRQVVVGL--PDVRGREQIL--KV 333
Cdd:COG0593  112 ---KEATQeeffhTFN-ALREAGKQ------IVLTSDRPPkelPGLEERLRS--RLEWGLVVDIqpPDLETRIAILrkKA 179
                        170
                 ....*....|.
gi 489115162 334 HMRRVPLSPDI 344
Cdd:COG0593  180 ADRGLELPDEV 190
Sigma54_activat pfam00158
Sigma-54 interaction domain;
188-253 8.41e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.77  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  188 VLMVGPPGTGKTLLAKAI---AGEAKVPFFTISGSDFV------EMFvGV------GASRVRD-MFEQAKKAapcIIFID 251
Cdd:pfam00158  25 VLITGESGTGKELFARAIhqlSPRADGPFVAVNCAAIPeellesELF-GHekgaftGADSDRKgLFELADGG---TLFLD 100

                  ..
gi 489115162  252 EI 253
Cdd:pfam00158 101 EI 102
AAA_22 pfam13401
AAA domain;
186-256 9.71e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489115162  186 KGVLMV-GPPGTGKTLLAKAIA---GEAKVPFFTI------SGSDFVEMFV---------GVGASRVRDMFEQA--KKAA 244
Cdd:pfam13401   5 AGILVLtGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglplsgRLSKEELLAALQQLllALAV 84
                          90
                  ....*....|..
gi 489115162  245 PCIIFIDEIDAV 256
Cdd:pfam13401  85 AVVLIIDEAQHL 96
 
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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