NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1011865138|ref|WP_062682931|]
View 

MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Achromobacter]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-595 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1070.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  14 IALVLFTVFKQFDGRAQTQDGVTYTQFMDDAKAGRIRKVDVQGDVLYVTPDAGR--AYTLTSPGDLWMVSDLLKYGVQVS 91
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRVNDPELVDLLEEKGVEVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  92 GKPREEQSLLMSIFVSWFPMLLLIGVWVFFMRQMQGGGRGgAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQELVD 171
Cdd:COG0465    81 AKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG-AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 172 FLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIF 251
Cdd:COG0465   160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 252 IDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQ 331
Cdd:COG0465   240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 332 ILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEEERK 411
Cdd:COG0465   320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 412 NTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMDQMTTGASN 491
Cdd:COG0465   400 ITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASN 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 492 DFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILEDNRDKV 571
Cdd:COG0465   480 DLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKL 559
                         570       580
                  ....*....|....*....|....
gi 1011865138 572 EVMTAALLEWETIDADQINDIIEG 595
Cdd:COG0465   560 DALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-595 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1070.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  14 IALVLFTVFKQFDGRAQTQDGVTYTQFMDDAKAGRIRKVDVQGDVLYVTPDAGR--AYTLTSPGDLWMVSDLLKYGVQVS 91
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRVNDPELVDLLEEKGVEVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  92 GKPREEQSLLMSIFVSWFPMLLLIGVWVFFMRQMQGGGRGgAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQELVD 171
Cdd:COG0465    81 AKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG-AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 172 FLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIF 251
Cdd:COG0465   160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 252 IDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQ 331
Cdd:COG0465   240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 332 ILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEEERK 411
Cdd:COG0465   320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 412 NTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMDQMTTGASN 491
Cdd:COG0465   400 ITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASN 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 492 DFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILEDNRDKV 571
Cdd:COG0465   480 DLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKL 559
                         570       580
                  ....*....|....*....|....
gi 1011865138 572 EVMTAALLEWETIDADQINDIIEG 595
Cdd:COG0465   560 DALAEALLEKETLDGEELEEILAG 583
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
10-615 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 839.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  10 VWMVIALVLFTVFKQFDGRAQTQDGVTYTQFMDDAKAGRIRKVDVQGDVLYVTPDAGRAYTLTSP-GDLWMVSDLLKYGV 88
Cdd:PRK10733    7 LWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPvNDPKLLDNLLTKNV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  89 QVSGKPREEQSLLMSIFVSWFPMLLLIGVWVFFMRQMQGGGRGGAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQE 168
Cdd:PRK10733   87 KVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 169 LVDFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPC 248
Cdd:PRK10733  167 LVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPC 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 249 IIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRG 328
Cdd:PRK10733  247 IIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 329 REQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEE 408
Cdd:PRK10733  327 REQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEA 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 409 ERKNTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFM--DQMT 486
Cdd:PRK10733  407 QKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYgpEHVS 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 487 TGASNDFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILED 566
Cdd:PRK10733  487 TGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTD 566
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011865138 567 NRDKVEVMTAALLEWETIDADQINDIIEGRPPRPP---KTPSGPSDTSDTPP 615
Cdd:PRK10733  567 NMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPagwEEPGASNNSDDNGT 618
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
101-594 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: 837.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 101 LMSIFVSWFP-MLLLIGVWVFFMRQMQGGGRGgAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQELVDFLRDPSKF 179
Cdd:TIGR01241   2 LLGFLFSLLPpILLLVGVWFFFRRQMQGGGGR-AFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 180 QKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIFIDEIDAVG 259
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 260 RQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQILKVHMRK 339
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 340 VPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEEERKNTAYHESG 419
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 420 HAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMDQMTTGASNDFERATAI 499
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 500 ARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILEDNRDKVEVMTAALL 579
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1011865138 580 EWETIDADQINDIIE 594
Cdd:TIGR01241 481 EKETITREEIKELLA 495
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
151-321 5.64e-126

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: 368.48  E-value: 5.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 151 ITFADVAGCDEAKEDVQELVDFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 231 GAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALL 310
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1011865138 311 RPGRFDRQVVV 321
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
404-592 2.72e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 267.16  E-value: 2.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 404 VMPEEERKNTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMD 483
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 484 QMTTGASNDFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKI 563
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKEI 161
                         170       180
                  ....*....|....*....|....*....
gi 1011865138 564 LEDNRDKVEVMTAALLEWETIDADQINDI 592
Cdd:pfam01434 162 LTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
187-325 5.80e-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: 89.74  E-value: 5.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  187 PRGVLMVGSPGTGKTLLAKAIAGEAKVP---FFSISGSDFVE--------------MFVGVGAARVRDMFENAKKHAPCI 249
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138  250 IFIDEIDAVGRQRGaglgggndEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPgRFDRQVVVPLPD 325
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-595 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1070.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  14 IALVLFTVFKQFDGRAQTQDGVTYTQFMDDAKAGRIRKVDVQGDVLYVTPDAGR--AYTLTSPGDLWMVSDLLKYGVQVS 91
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRVNDPELVDLLEEKGVEVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  92 GKPREEQSLLMSIFVSWFPMLLLIGVWVFFMRQMQGGGRGgAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQELVD 171
Cdd:COG0465    81 AKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG-AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 172 FLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIF 251
Cdd:COG0465   160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 252 IDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQ 331
Cdd:COG0465   240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 332 ILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEEERK 411
Cdd:COG0465   320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 412 NTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMDQMTTGASN 491
Cdd:COG0465   400 ITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASN 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 492 DFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILEDNRDKV 571
Cdd:COG0465   480 DLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKL 559
                         570       580
                  ....*....|....*....|....
gi 1011865138 572 EVMTAALLEWETIDADQINDIIEG 595
Cdd:COG0465   560 DALAEALLEKETLDGEELEEILAG 583
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
10-615 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 839.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  10 VWMVIALVLFTVFKQFDGRAQTQDGVTYTQFMDDAKAGRIRKVDVQGDVLYVTPDAGRAYTLTSP-GDLWMVSDLLKYGV 88
Cdd:PRK10733    7 LWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPvNDPKLLDNLLTKNV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  89 QVSGKPREEQSLLMSIFVSWFPMLLLIGVWVFFMRQMQGGGRGGAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQE 168
Cdd:PRK10733   87 KVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 169 LVDFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPC 248
Cdd:PRK10733  167 LVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPC 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 249 IIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRG 328
Cdd:PRK10733  247 IIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 329 REQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEE 408
Cdd:PRK10733  327 REQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEA 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 409 ERKNTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFM--DQMT 486
Cdd:PRK10733  407 QKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYgpEHVS 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 487 TGASNDFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILED 566
Cdd:PRK10733  487 TGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTD 566
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011865138 567 NRDKVEVMTAALLEWETIDADQINDIIEGRPPRPP---KTPSGPSDTSDTPP 615
Cdd:PRK10733  567 NMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPagwEEPGASNNSDDNGT 618
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
101-594 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: 837.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 101 LMSIFVSWFP-MLLLIGVWVFFMRQMQGGGRGgAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQELVDFLRDPSKF 179
Cdd:TIGR01241   2 LLGFLFSLLPpILLLVGVWFFFRRQMQGGGGR-AFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 180 QKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIFIDEIDAVG 259
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 260 RQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQILKVHMRK 339
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 340 VPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIVMPEEERKNTAYHESG 419
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 420 HAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMDQMTTGASNDFERATAI 499
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 500 ARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILEDNRDKVEVMTAALL 579
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1011865138 580 EWETIDADQINDIIE 594
Cdd:TIGR01241 481 EKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
35-602 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 610.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  35 VTYTQFMDDAKAGRIRKVDvqgdvLYvtpDAGRAYTL--TSP--GDLW-------------MVSDLLKYGVQVSGKPREE 97
Cdd:CHL00176   52 MTYGRFLEYLDMGWIKKVD-----LY---DNGRTAIVeaSSPelGNRPqrirvelpvgaseLIQKLKEANIDFDAHPPVL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  98 QSLLMSIFVSW-FPMLLLIGVWVFFMRQ--MQGGGRGGAFSFGKSRARMLDENTNQITFADVAGCDEAKEDVQELVDFLR 174
Cdd:CHL00176  124 KSNIVTILSNLlLPLILIGVLWFFFQRSsnFKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 175 DPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIFIDE 254
Cdd:CHL00176  204 KPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDE 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 255 IDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQILK 334
Cdd:CHL00176  284 IDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILK 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 335 VHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIvMPEEERKNTA 414
Cdd:CHL00176  364 VHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPL-EDSKNKRLIA 442
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 415 YHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEE-LFMD-QMTTGASND 492
Cdd:CHL00176  443 YHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEvVFGStEVTTGASND 522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 493 FERATAIARDIVTRYGMtDELGPM-VYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKILEDNRDKV 571
Cdd:CHL00176  523 LQQVTNLARQMVTRFGM-SSIGPIsLESNNSTDPFLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLI 601
                         570       580       590
                  ....*....|....*....|....*....|.
gi 1011865138 572 EVMTAALLEWETIDADQINDIIEGRPPRPPK 602
Cdd:CHL00176  602 DLLVELLLQKETIDGDEFREIVNSYTILPPK 632
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
151-321 5.64e-126

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: 368.48  E-value: 5.64e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 151 ITFADVAGCDEAKEDVQELVDFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 231 GAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALL 310
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1011865138 311 RPGRFDRQVVV 321
Cdd:cd19501   161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
150-400 1.11e-112

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 340.45  E-value: 1.11e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 150 QITFADVAGCDEAKEDVQELV-DFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:COG1222    74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 229 GVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGndEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPA 308
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 309 LLRPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFE 388
Cdd:COG1222   232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLE 311
                         250
                  ....*....|..
gi 1011865138 389 KAKDKIIMGAER 400
Cdd:COG1222   312 KAIEKVKKKTET 323
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
150-408 1.34e-100

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 311.77  E-value: 1.34e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 150 QITFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 229 GVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPA 308
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 309 LLRPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFE 388
Cdd:PRK03992  287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFL 366
                         250       260
                  ....*....|....*....|
gi 1011865138 389 KAKDKIIMGAERRSIVMPEE 408
Cdd:PRK03992  367 KAIEKVMGKEEKDSMEEPGV 386
Peptidase_M41 pfam01434
Peptidase family M41;
404-592 2.72e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 267.16  E-value: 2.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 404 VMPEEERKNTAYHESGHAIVARMLPKTDPVHKVTIIPRGRALGVTMQLPETDRYSMDKGRLLSTIAVLFGGRIAEELFMD 483
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 484 QMTTGASNDFERATAIARDIVTRYGMTDELGPMVYAENEGEVFLGRSVTKTTHMSEATMQKVDTEIRRIIDEQYGVARKI 563
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKEI 161
                         170       180
                  ....*....|....*....|....*....
gi 1011865138 564 LEDNRDKVEVMTAALLEWETIDADQINDI 592
Cdd:pfam01434 162 LTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
150-395 4.52e-85

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: 270.52  E-value: 4.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 150 QITFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 229 GVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPA 308
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 309 LLRPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFE 388
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFI 357

                  ....*..
gi 1011865138 389 KAKDKII 395
Cdd:TIGR01242 358 KAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
153-400 8.63e-80

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: 257.92  E-value: 8.63e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 153 FADVAGCDEAKEDVQELVD-FLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVG 231
Cdd:COG0464   156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 232 AARVRDMFENAKKHAPCIIFIDEIDAVGRQRGaGLGGGNDEREqtLNQMLVEMDGFESgqGVIVIAATNRPDVLDPALLR 311
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELRS--DVVVIAATNRPDLLDPALLR 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 312 pgRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAK 391
Cdd:COG0464   311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                  ....*....
gi 1011865138 392 DKIIMGAER 400
Cdd:COG0464   389 EREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
150-394 3.67e-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: 3.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 150 QITFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 229 GVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEReqTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPA 308
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 309 LLRPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARR----------- 377
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigspakekle 686
                         250       260
                  ....*....|....*....|....
gi 1011865138 378 -------NGRTVDMSDFEKAKDKI 394
Cdd:TIGR01243 687 vgeeeflKDLKVEMRHFLEALKKV 710
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
152-319 2.23e-65

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: 212.20  E-value: 2.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 152 TFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 231 GAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALL 310
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                  ....*....
gi 1011865138 311 RPGRFDRQV 319
Cdd:cd19502   161 RPGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
151-401 3.66e-64

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 216.55  E-value: 3.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 151 ITFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVG 229
Cdd:PTZ00454  142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 230 VGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPAL 309
Cdd:PTZ00454  222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 310 LRPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEK 389
Cdd:PTZ00454  302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEK 381
                         250
                  ....*....|..
gi 1011865138 390 AKDKIIMGAERR 401
Cdd:PTZ00454  382 GYKTVVRKTDRD 393
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
150-377 7.50e-64

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: 224.02  E-value: 7.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 150 QITFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 229 GVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGggnDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPA 308
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011865138 309 LLRPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARR 377
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
162-319 1.06e-63

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: 207.14  E-value: 1.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 162 AKEDVQELVDFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011865138 242 AKKHAPCIIFIDEIDAVGRQRGAglGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
153-394 1.95e-63

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 209.74  E-value: 1.95e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 153 FADVAGCDEAKEDVQELVDFLRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGA 232
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 233 ARVRDMFENAKKhAPCIIFIDEIDAVGRQRGAGLGGGndEREQTLNQMLVEMDGFESgqGVIVIAATNRPDVLDPALLRp 312
Cdd:COG1223    81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 313 gRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKAKD 392
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                  ..
gi 1011865138 393 KI 394
Cdd:COG1223   234 QR 235
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
152-395 4.16e-62

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 212.32  E-value: 4.16e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 152 TFADVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:PTZ00361  181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 231 GAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALL 310
Cdd:PTZ00361  261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 311 RPGRFDRQVVVPLPDIRGREQILKVHMRKVPLSPNVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEKA 390
Cdd:PTZ00361  341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                  ....*
gi 1011865138 391 KDKII 395
Cdd:PTZ00361  421 KEKVL 425
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
162-321 5.01e-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: 200.20  E-value: 5.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 162 AKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFE 240
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 241 NAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEReqTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVV 320
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                  .
gi 1011865138 321 V 321
Cdd:cd19511   159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
155-321 3.82e-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: 192.51  E-value: 3.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 234 RVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGlGGGNDEReqTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPG 313
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                  ....*...
gi 1011865138 314 RFDRQVVV 321
Cdd:cd19503   158 RFDREVEI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
190-323 2.34e-55

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: 183.95  E-value: 2.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGaglGGG 269
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011865138 270 NDEREQTLNQMLVEMDGFESGQG-VIVIAATNRPDVLDPALLrpGRFDRQVVVPL 323
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
163-321 3.80e-55

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: 184.64  E-value: 3.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 163 KEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 242 AKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVV 321
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
162-321 7.48e-54

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: 181.15  E-value: 7.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 162 AKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFE 240
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 241 NAKKHAPCIIFIDEIDAVGRQRGAGLGGGNDEReqTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVV 320
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                  .
gi 1011865138 321 V 321
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 ...
155-322 3.12e-50

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: 171.47  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 234 RVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglGGGNDEReQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPG 313
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK--THGEVER-RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                  ....*....
gi 1011865138 314 RFDRQVVVP 322
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
173-321 1.41e-48

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: 166.89  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 173 LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKHAPCIIFI 252
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011865138 253 DEIDAVGRQRGaglGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVVV 321
Cdd:cd19530    96 DEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
155-319 2.26e-48

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: 166.81  E-value: 2.26e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDFL-RDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 234 RVRDMFENAKKHAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQMLVEMDGF----ESGQGVIVIAATNRPDVLDPAL 309
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                         170
                  ....*....|
gi 1011865138 310 LRPGRFDRQV 319
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 ...
169-319 1.81e-44

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: 155.66  E-value: 1.81e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 169 LVDFLRDPSK----FQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKK 244
Cdd:cd19526     5 LEETIEWPSKypkiFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011865138 245 HAPCIIFIDEIDAVGRQRGAGLGGGNDereQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
163-321 2.23e-42

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: 149.97  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 163 KEDVQELVDF-LRDPSKFQKlGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19527     2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 242 AKKHAPCIIFIDEIDAVGRQRGA-GLGGGNDEReqTLNQMLVEMDGFE-SGQGVIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                  ..
gi 1011865138 320 VV 321
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 ...
156-321 1.53e-40

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: 145.19  E-value: 1.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 156 VAGCDEAKEDVQELVDFlrdPSKFQKL--GGR-IPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGA 232
Cdd:cd19509     1 IAGLDDAKEALKEAVIL---PSLRPDLfpGLRgPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 233 ARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglggGNDEREQTL-NQMLVEMDGFE--SGQGVIVIAATNRPDVLDPAL 309
Cdd:cd19509    78 KIVRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAF 153
                         170
                  ....*....|..
gi 1011865138 310 LRpgRFDRQVVV 321
Cdd:cd19509   154 LR--RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
151-321 2.46e-37

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: 136.53  E-value: 2.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 151 ITFADVAGCDEAKEDVQELVDFlrdPSKFQKL--GGRIP-RGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMF 227
Cdd:cd19521     4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 228 VGVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglgGGNDEREQTLNQMLVEMDGF-ESGQGVIVIAATNRPDVLD 306
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                         170
                  ....*....|....*
gi 1011865138 307 PALLRpgRFDRQVVV 321
Cdd:cd19521   158 SAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
155-318 5.38e-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: 133.02  E-value: 5.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDF-LRDPSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAIA-----GEAKVPFFSISGSDFVEMFV 228
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 229 GVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglgggndEREQT----LNQMLVEMDGFESGQGVIVIAATNRPDV 304
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                         170
                  ....*....|....
gi 1011865138 305 LDPALLRPGRFDRQ 318
Cdd:cd19517   154 LDPALRRPGRFDRE 167
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
155-321 6.06e-32

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: 121.63  E-value: 6.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDF-LRDPSKFQklGGRIP-RGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGA 232
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 233 ARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglGGGNDEREQTLNQMLVEMDGF-------ESGQGVIVIAATNRPDVL 305
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156
                         170
                  ....*....|....*.
gi 1011865138 306 DPALLRpgRFDRQVVV 321
Cdd:cd19522   157 DEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
155-315 2.00e-31

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: 119.84  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDF-LRDPSKFQKlgGRI---PRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDN--SRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 231 GAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGlgggndEREQTL---NQMLVEMDGFESGQG--VIVIAATNRPDVL 305
Cdd:cd19520    79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDL 152
                         170
                  ....*....|..
gi 1011865138 306 DPALLR--PGRF 315
Cdd:cd19520   153 DEAILRrmPKRF 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
155-321 2.74e-31

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: 119.57  E-value: 2.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELVDFlrdPSKFQKL--GGRIP-RGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVG 231
Cdd:cd19524     1 DIAGQDLAKQALQEMVIL---PSLRPELftGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 232 AARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglgGGNDEREQTLNQMLVEMDGFESGQG--VIVIAATNRPDVLDPAL 309
Cdd:cd19524    78 EKLVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAV 154
                         170
                  ....*....|..
gi 1011865138 310 LRpgRFDRQVVV 321
Cdd:cd19524   155 LR--RFTKRVYV 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
149-321 4.06e-31

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: 119.71  E-value: 4.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 149 NQITFADVAGCDEAKEDVQELV--DFLRdPSKFQKLGGRiPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEM 226
Cdd:cd19525    17 PPINWADIAGLEFAKKTIKEIVvwPMLR-PDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 227 FVGVGAARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAglgGGNDEREQTLNQMLVEMDGFESG--QGVIVIAATNRPDV 304
Cdd:cd19525    95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQE 171
                         170
                  ....*....|....*..
gi 1011865138 305 LDPALLRpgRFDRQVVV 321
Cdd:cd19525   172 IDEAARR--RLVKRLYI 186
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
157-323 7.13e-30

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: 114.94  E-value: 7.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 157 AGCDEAKEDVQELVDflrdpskfqklgGRIPRGVLMVGSPGTGKTLLAKAIAGEA---KVPFFSISGSDFVEMFVG---V 230
Cdd:cd00009     1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 231 GAARVRDMFENAKKHAPCIIFIDEIDAVGRqrgaglgggnDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALL 310
Cdd:cd00009    69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                         170
                  ....*....|...
gi 1011865138 311 RPGRFDRQVVVPL 323
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; ...
176-319 4.71e-29

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: 113.74  E-value: 4.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 176 PSKFQKLGGRIPRGVLMVGSPGTGKTLLAKAI-----AGEAKVpffsISGSDFVEMFVGVGAARVRDMFENAKKHAPC-- 248
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011865138 249 ------IIFIDEIDAVGRQRGAGlGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19504   100 ansglhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
186-395 7.12e-29

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 120.51  E-value: 7.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 186 IPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSIsgsDFVEMF---VGVGAARVRDMFENAKKHAPCIIFIDEID-AVGRQ 261
Cdd:CHL00195  258 TPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 262 RGAGLGGGNDEREQTLNQMLVEMDGFesgqgVIVIAATNRPDVLDPALLRPGRFDRQVVVPLPDIRGREQILKVHMRKV- 340
Cdd:CHL00195  335 ESKGDSGTTNRVLATFITWLSEKKSP-----VFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFr 409
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138 341 PLS-PNVDATILARGCPGFSGADLANLVNEaALFAARRNGRTVDMSDFEKAKDKII 395
Cdd:CHL00195  410 PKSwKKYDIKKLSKLSNKFSGAEIEQSIIE-AMYIAFYEKREFTTDDILLALKQFI 464
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
155-317 5.60e-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: 5.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQElvdflRDPS---KFQKLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVG 231
Cdd:cd19507     1 DVGGLDNLKDWLKK-----RKAAfskQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 232 AARVRDMFENAKKHAPCIIFIDEID-AVGRQRGAGLGGGNderEQTLNQMLVEMDgfESGQGVIVIAATNRPDVLDPALL 310
Cdd:cd19507    76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTS---SRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELL 150

                  ....*..
gi 1011865138 311 RPGRFDR 317
Cdd:cd19507   151 RKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
187-325 5.80e-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: 89.74  E-value: 5.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  187 PRGVLMVGSPGTGKTLLAKAIAGEAKVP---FFSISGSDFVE--------------MFVGVGAARVRDMFENAKKHAPCI 249
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138  250 IFIDEIDAVGRQRGaglgggndEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPgRFDRQVVVPLPD 325
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
166-321 5.85e-20

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: 87.02  E-value: 5.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 166 VQELVDFLRDPSKFQKLGgrIP--RGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDfvemfVGVGAARVRDMFENAK 243
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRG--IPyrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 244 KHApcIIFIDEIDAV---GRQRGAGLGGGNDEREQTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPALLRPGRFDRQVV 320
Cdd:cd19510    75 KQS--IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIY 152

                  .
gi 1011865138 321 V 321
Cdd:cd19510   153 M 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
155-321 5.08e-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: 81.47  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 155 DVAGCDEAKEDVQELV--DFLRdPSKFQKLGgRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGVGA 232
Cdd:cd19523     1 DIAGLGALKAAIKEEVlwPLLR-PDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 233 ARVRDMFENAKKHAPCIIFIDEIDAVGRQRGAGLGGGNdeREQTlnQMLVEMDGFESG--QGVIVIAATNRPDVLDPALL 310
Cdd:cd19523    79 KILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154
                         170
                  ....*....|.
gi 1011865138 311 RpgRFDRQVVV 321
Cdd:cd19523   155 R--YFSKRLLV 163
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
181-317 3.31e-13

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: 67.79  E-value: 3.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 181 KLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFV--------------EMFVGVGAARVRDMFENAKKHA 246
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011865138 247 PCIIFIDEIDAVGRQRGAGLGGGNdeREQTLNQMLVEM-DGFE--SGQGVIVIAATNRPDVLDPALLRPGRFDR 317
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEED--PKLLLGLLLNYLsRDFEksSTRNILVIASTHIPQKVDPALIAPNRLDT 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
345-389 2.38e-12

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: 61.79  E-value: 2.38e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1011865138 345 NVDATILARGCPGFSGADLANLVNEAALFAARRNGRTVDMSDFEK 389
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK04195 PRK04195
replication factor C large subunit; Provisional
152-271 2.31e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 63.02  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 152 TFADVAGCDEAKEDVQELVDflrdpsKFQKlgGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDF-----VEM 226
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIE------SWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1011865138 227 FVGvGAARVRDMFENAKKhapcIIFIDEIDavgrqrgaGLGGGND 271
Cdd:PRK04195   84 VAG-EAATSGSLFGARRK----LILLDEVD--------GIHGNED 115
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
188-319 1.21e-09

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: 57.15  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 188 RGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVGvGAARVRDMFENAKK-HAPCIIFIDEIDAVGRQRgAGL 266
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-STE 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1011865138 267 GGGNDEReQTLNQMLVEMdGFESGQGVIVIaATNRPDVLDPALlrPGRFDRQV 319
Cdd:cd19512   101 KISEDLR-AALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
194-255 5.56e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.56  E-value: 5.56e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138 194 GSPGTGKTLLAKAIAGEAKVPFFSISGSDFvemfvgvGAARVRDMFENAKKHA----PCIIFIDEI 255
Cdd:PRK13342   43 GPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
194-255 1.87e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 56.99  E-value: 1.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138 194 GSPGTGKTLLAKAIAGEAKVPFFSISGsdfvemfVGVGAARVRDMFENAKKHA----PCIIFIDEI 255
Cdd:COG2256    56 GPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
186-274 2.41e-08

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: 54.31  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 186 IPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEM-FVGVGA-ARVRDMFENakkhapcIIFIDEIDAVGRQRG 263
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIAKRGG 117
                          90
                  ....*....|.
gi 1011865138 264 AglGGGNDERE 274
Cdd:cd19498   118 S--SGPDVSRE 126
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
10-94 1.66e-07

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: 49.91  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138  10 VWMVIALVLFTVFKQF--DGRAQTQDgVTYTQFMDDAKAGRIRKVDVQGD------VLYVTPDAGRAYTLTSPGDLWMVS 81
Cdd:pfam06480   3 LWLLILLVLLLLFLLFllSSSSSTKE-ISYSEFLEYLEAGKVKKVVVQDDeilptgVVEGTLKDGSKFTTYFIPSLPNVD 81
                          90       100
                  ....*....|....*....|.
gi 1011865138  82 DLL--------KYGVQVSGKP 94
Cdd:pfam06480  82 SLLekledaleEKGVKVSVKP 102
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
144-223 2.31e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 53.44  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 144 LDENTNQITFAD-VAGCDEAKEDVQELVDFLRDpskfQKLGGRiprGVLMVGSPGTGKTLLAKAIAGE--AKVPFFSISG 220
Cdd:COG1224    27 LDENGKAKFVADgLVGQVEAREAAGIVVKMIKE----GKMAGK---GILIVGPPGTGKTALAVAIARElgEDTPFVAISG 99

                  ...
gi 1011865138 221 SDF 223
Cdd:COG1224   100 SEI 102
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
144-223 5.63e-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: 51.93  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 144 LDENTNQITFAD-VAGCDEAKEDVQELVDFLRDpskfQKLGGRiprGVLMVGSPGTGKTLLAKAIAGE--AKVPFFSISG 220
Cdd:pfam06068  13 LDEDGEARYVSGgLVGQEKAREAAGVIVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKElgEDTPFTSISG 85

                  ...
gi 1011865138 221 SDF 223
Cdd:pfam06068  86 SEV 88
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
189-315 1.07e-06

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: 48.44  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 189 GVLMVGSPGTGKTLLAKAIAgEA--KVPFFSISGSDFVE-------MFVGVGAARVRD--MFENAKKhaPCIIFIDEIDA 257
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEINR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138 258 VGRQRGAGLGGGNDEREqtlnqmLVEMDGFE----SGQGVIVIAATNRPD----VLDPALLRpgRF 315
Cdd:pfam07728  78 ANPDVLNSLLSLLDERR------LLLPDGGElvkaAPDGFRLIATMNPLDrglnELSPALRS--RF 135
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
166-410 5.53e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 166 VQELVDFLRDPskfqkLGGRIPRGVLMVGSPGTGKTLLAKAIAGEAK-------VPF-------------FSI------- 218
Cdd:COG1474    35 IEELASALRPA-----LRGERPSNVLIYGPTGTGKTAVAKYVLEELEeeaeergVDVrvvyvncrqastrYRVlsrilee 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 219 --SGSDFVEmfVGVGAARVRDMFENA--KKHAPCIIFIDEIDAVGRqrgaglgggnDEREQTLNQmLVEMDGFESGQGVI 294
Cdd:COG1474   110 lgSGEDIPS--TGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVD----------DEGDDLLYQ-LLRANEELEGARVG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 295 VIAATNRPDV---LDPALLRpgRF-DRQVVVP---LPDIRgreQILKvHMRKVPLSPNV-DATILARgCpgfsgADLA-- 364
Cdd:COG1474   177 VIGISNDLEFlenLDPRVKS--SLgEEEIVFPpydADELR---DILE-DRAELAFYDGVlSDEVIPL-I-----AALAaq 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011865138 365 ---------NLVNEAALFAARRNGRTVDMSDFEKAKDKIIMGAERRSIV-MPEEER 410
Cdd:COG1474   245 ehgdarkaiDLLRVAGEIAEREGSDRVTEEHVREAREKIERDRLLEVLRgLPTHEK 300
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
190-306 5.79e-06

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: 45.96  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSDFVEMFVgvgaARVRDMFENAKkhaPCIIFIDEIDAVGRQRgaglggG 269
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARAS------Q 67
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1011865138 270 NDEREQTLNQMLVEMDGFESGqGVIVIAATNRPDVLD 306
Cdd:cd01120    68 GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDI 103
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
188-309 1.65e-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: 46.29  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 188 RGVLMVGSPGTGKTLLAKAIAGEAKV---------------------PFFSISGSDFVEMFvgvgaARVRDMFENAKkha 246
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDDKD--- 124
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011865138 247 pCIIF--IDEIDAVGRQRGAgLGGGNDERE--QTLNQMLVEMDGFESGQGVIVIAATNRPDVLDPAL 309
Cdd:cd19508   125 -ALVFvlIDEVESLAAARSA-SSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
44 PHA02544
clamp loader, small subunit; Provisional
174-222 3.90e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 46.14  E-value: 3.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011865138 174 RDPSKFQKL--GGRIPRGVLMVGSPGTGKTLLAKAIAGEAKVPFFSISGSD 222
Cdd:PHA02544   28 ADKETFKSIvkKGRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD 78
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
154-260 8.45e-05

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: 43.70  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 154 ADVAGCDEAKEDVQEL--VDFLRdpskfQKLGGRIprgVLMVGSPGTGKTLLAKAIAGEAKVPFFSIS-G--SDFVEM-- 226
Cdd:cd19500    10 ADHYGLEDVKERILEYlaVRKLK-----GSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrg 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1011865138 227 ----FVGVGAARVRDMFENAKKHAPcIIFIDEIDAVGR 260
Cdd:cd19500    82 hrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
190-256 2.88e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 41.80  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGE---AKVPFFSISGSDFVE-----MFVGVGAARVR-----DMFENAKKHAPCIIFIDEID 256
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
140-319 3.49e-04

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: 43.68  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 140 RARMLDENTNQItfADVAGCDEAKEDVQELVDFLRDPSKFQKLGGRIP---RGVLMVGSPGTGKTLLAKAIA------GE 210
Cdd:TIGR03922 264 KAKLLAEAEAEL--AEQIGLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiycglGV 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 211 AKVP-FFSISGSDFVEMFVGVGAARVRDMFENAKKHapcIIFIDEIDAVGRQRGaglGGGNDEREQTLNQMLVEM--DGF 287
Cdd:TIGR03922 342 LRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY---GQKDPFGLEAIDTLLARMenDRD 415
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1011865138 288 EsgqgVIVIAATNRPDvLDPAL-----LRpGRFDRQV 319
Cdd:TIGR03922 416 R----LVVIGAGYRKD-LDKFLevnegLR-SRFTRVI 446
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
194-395 4.14e-04

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 42.87  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 194 GSPGTGKTLLAKAIAGEAKVPFFS-----ISGSDFVEMFvgVGAARVRDMFENAKKHAPC-IIFIDEIdavgrQRGAGlg 267
Cdd:COG0593    41 GGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDF--INAIRNNTIEEFKEKYRSVdVLLIDDI-----QFLAG-- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 268 ggnDEREQ-----TLNQMLvemdgfESG-QgvIVIAATNRP---DVLDPALLRpgRFDRQVVVPL--PDIRGREQIL--K 334
Cdd:COG0593   112 ---KEATQeeffhTFNALR------EAGkQ--IVLTSDRPPkelPGLEERLRS--RLEWGLVVDIqpPDLETRIAILrkK 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011865138 335 VHMRKVPLSPNVdATILARGCPGfSGADLanlvnEAAL----FAARRNGRTVDM-------SDFEKAKDKII 395
Cdd:COG0593   179 AADRGLELPDEV-LEYLARRIER-NVREL-----EGALnrldAYALLTGRPITLelarevlKDLLRAQKKEI 243
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
190-260 6.05e-04

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: 41.82  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGEAKVPfFSIS-----------GSDfVEMFVG--VGAArvrdMF--ENAKKHapcIIFIDE 254
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VENILLklLQAA----DYdvERAQRG---IVYIDE 123

                  ....*.
gi 1011865138 255 IDAVGR 260
Cdd:cd19497   124 IDKIAR 129
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
190-255 7.08e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.04  E-value: 7.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGEAKVPFFSISG------SDFVEMFVGVGAarvRDmfenakkhapcIIFIDEI 255
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI 111
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
190-209 7.21e-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: 42.33  E-value: 7.21e-04
                          10        20
                  ....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAG 209
Cdd:COG0606   214 LLMIGPPGSGKTMLARRLPG 233
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
185-255 8.08e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.45  E-value: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 185 RIPRGVLMVGSPGTGKT----LLAKAIAGEAK-----VPFF-SISGSDFVEMFV---GVGAARVRD-MF----ENAKKH- 245
Cdd:COG1401   219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpSWSYEDFLLGYRpslDEGKYEPTPgIFlrfcLKAEKNp 298
                          90
                  ....*....|.
gi 1011865138 246 -APCIIFIDEI 255
Cdd:COG1401   299 dKPYVLIIDEI 309
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
163-257 1.12e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.50  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 163 KEDVQELVDFLRdpskfqklGGRIPRGVLMVGSPGTGKTLLAKAIA----GEAKVP-----------FFSISGSDFVEMF 227
Cdd:COG0470     2 EEAWEQLLAAAE--------SGRLPHALLLHGPPGIGKTTLALALArdllCENPEGgkacgqchsrlMAAGNHPDLLELN 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1011865138 228 VGV-----GAARVRDMFENAKKHAPC----IIFIDEIDA 257
Cdd:COG0470    74 PEEksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADA 112
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
190-209 2.43e-03

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: 39.83  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAG 209
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
190-260 2.90e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 40.53  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGEAKVPfFSIS-----------GSDfVEMFVG--VGAArvrDM-FENAKKHapcIIFIDEI 255
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENILLklLQAA---DYdVEKAQRG---IVYIDEI 182

                  ....*
gi 1011865138 256 DAVGR 260
Cdd:PRK05342  183 DKIAR 187
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
190-260 4.12e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.03  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865138 190 VLMVGSPGTGKTLLAKAIAGEAKVPfFSIS-----------GSDfVEMFVgvgaarVR-------DMfENAKKHapcIIF 251
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKllqaadyDV-EKAERG---IIY 179

                  ....*....
gi 1011865138 252 IDEIDAVGR 260
Cdd:COG1219   180 IDEIDKIAR 188
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
188-255 4.84e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 4.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011865138 188 RGVLMVGSPGTGKTLLAKAIAGEA-----KVPFFSIsgSDFV-EMFVGVGAARVRDMFENAKKhAPCIIfIDEI 255
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLVnELKEARADGRLERLLKRLAK-VDLLI-LDEL 169
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
182-211 5.67e-03

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.74  E-value: 5.67e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1011865138 182 LGGRIPRG--VLMVGSPGTGKTLLAKAIAGEA 211
Cdd:COG0467    13 LGGGLPRGssTLLSGPPGTGKTTLALQFLAEG 44
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH