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Conserved domains on  [gi|1831511375|ref|NP_001366715|]
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ATP-dependent zinc metalloprotease YME1 homolog [Caenorhabditis elegans]

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

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
170-686 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 692.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 170 RTYTDGFVKGLLSNGVSGAGKDGKKSNT----LTRFYIFLVFCIFFGYLTGRIRVrvGDRQIGSLFFSNPQEVNPEDVQV 245
Cdd:COG0465    62 RVNDPELVDLLEEKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRRMQG--GGGGAMSFGKSKAKLYDEDKPKV 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 246 TFDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQG 325
Cdd:COG0465   140 TFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 326 ARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSI--HPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLR 403
Cdd:COG0465   220 ASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLR 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 404 PGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEAR 483
Cdd:COG0465   300 PGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAI 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 484 DRVLMGPARTGGRIPDEEaNRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDV 563
Cdd:COG0465   380 DRVIAGPERKSRVISEKE-KKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAV 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 564 MMGGRVAEELIFGDdkVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNESAL----VKVSDLAPQTAELIDAE 639
Cdd:COG0465   459 LLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLgrdiGQSRNYSEETAREIDEE 536
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511375 640 INRVLQESYKRAKVILETKKKEHQLLAEALLEYETLSADEVKRVISG 686
Cdd:COG0465   537 VRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
170-686 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 692.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 170 RTYTDGFVKGLLSNGVSGAGKDGKKSNT----LTRFYIFLVFCIFFGYLTGRIRVrvGDRQIGSLFFSNPQEVNPEDVQV 245
Cdd:COG0465    62 RVNDPELVDLLEEKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRRMQG--GGGGAMSFGKSKAKLYDEDKPKV 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 246 TFDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQG 325
Cdd:COG0465   140 TFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 326 ARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSI--HPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLR 403
Cdd:COG0465   220 ASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLR 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 404 PGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEAR 483
Cdd:COG0465   300 PGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAI 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 484 DRVLMGPARTGGRIPDEEaNRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDV 563
Cdd:COG0465   380 DRVIAGPERKSRVISEKE-KKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAV 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 564 MMGGRVAEELIFGDdkVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNESAL----VKVSDLAPQTAELIDAE 639
Cdd:COG0465   459 LLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLgrdiGQSRNYSEETAREIDEE 536
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511375 640 INRVLQESYKRAKVILETKKKEHQLLAEALLEYETLSADEVKRVISG 686
Cdd:COG0465   537 VRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
195-685 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: 615.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 195 SNTLTRFYIFLVFCIFFGYLTGRiRVRVGDRQIGSLFFSNPQEVNPEDVQVTFDDVRGMDEAKLEVEEIVDYLKDPEKYS 274
Cdd:TIGR01241   3 LGFLFSLLPPILLLVGVWFFFRR-QMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 275 RLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGS 354
Cdd:TIGR01241  82 KLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 355 KR--VSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKI 432
Cdd:TIGR01241 162 QRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 433 VHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEARDRVLMGPARTGGRIPDEEaNRNTAYHEAG 512
Cdd:TIGR01241 242 KLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKE-KKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 513 HTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDVMMGGRVAEELIFGDdkVTTGAADDLSKAT 592
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGE--VTTGASNDIKQAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 593 QLAVQMVKVFGMSDKVGLRDFTAQDNESALVKVSDLAP----QTAELIDAEINRVLQESYKRAKVILETKKKEHQLLAEA 668
Cdd:TIGR01241 399 NIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKeyseETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*..
gi 1831511375 669 LLEYETLSADEVKRVIS 685
Cdd:TIGR01241 479 LLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
180-706 6.21e-150

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 451.03  E-value: 6.21e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 180 LLSNGVSGAGKDGKKSNTLTRFYI-FLVFCIFFGYLTGRIRVRVGDRQIGSLFF--SNPQEVNPEDVQVTFDDVRGMDEA 256
Cdd:PRK10733   81 LLTKNVKVVGEPPEEPSLLASIFIsWFPMLLLIGVWIFFMRQMQGGGGKGAMSFgkSKARMLTEDQIKTTFADVAGCDEA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 257 KLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKA 336
Cdd:PRK10733  161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 337 KARAPCIIFIDEIDSVGSKRVS--NSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTVP 414
Cdd:PRK10733  241 KKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 415 KPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEARDRVLMGPARTg 494
Cdd:PRK10733  321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERR- 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 495 GRIPDEEANRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDVMMGGRVAEELI 574
Cdd:PRK10733  400 SMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEII 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 575 FGDDKVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNE----SALVKVSDLAPQTAELIDAEINRVLQESYKR 650
Cdd:PRK10733  480 YGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEvflgRSVAKAKHMSDETARIIDQEVKALIERNYNR 559
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831511375 651 AKVILETKKKEHQLLAEALLEYETLSADEVKRVISGQKIkRPtPAAVKKSNETKRN 706
Cdd:PRK10733  560 ARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDV-RP-PAGWEEPGASNNS 613
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
245-413 1.23e-100

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: 306.47  E-value: 1.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 245 VTFDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQ 324
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 325 GARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSI--HPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALL 402
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGggHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1831511375 403 RPGRFDVRVTV 413
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
496-683 3.46e-91

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 282.57  E-value: 3.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 496 RIPDEEANRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDVMMGGRVAEELIF 575
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 576 GddKVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNESALV----KVSDLAPQTAELIDAEINRVLQESYKRA 651
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGrgmgKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1831511375 652 KVILETKKKEHQLLAEALLEYETLSADEVKRV 683
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
281-417 4.69e-20

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: 87.43  E-value: 4.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375  281 PKGVLLVGPPGTGKTLLARAIAGEAQVP---FFHTAGSEFDEV--------------LVGQGARRVRDLFDKAKARAPCI 343
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831511375  344 IFIDEIDSVGSKRVSNSIhpyanqTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPgRFDVRVTVPKPD 417
Cdd:smart00382  82 LILDEITSLLDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
284-349 2.28e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEA-----QVPFFHTAGsefdevLVGQ--GARRVRDLFDKAK--ARAPCIIfIDEI 349
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTAAD------LVEQlaQARADGRLGRLLRrlARYDLLI-IDEL 160
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
260-308 4.85e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 38.24  E-value: 4.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831511375 260 VEEIVDYLKD-PEKYSRLggrlpkgVLLVGPPGTGKTLLARAIAGEAQVP 308
Cdd:NF033453    1 LEKLKRSVDEaESLYYKL-------ILLVGPPGSGKTALLRELAAKRGAP 43
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
170-686 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 692.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 170 RTYTDGFVKGLLSNGVSGAGKDGKKSNT----LTRFYIFLVFCIFFGYLTGRIRVrvGDRQIGSLFFSNPQEVNPEDVQV 245
Cdd:COG0465    62 RVNDPELVDLLEEKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRRMQG--GGGGAMSFGKSKAKLYDEDKPKV 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 246 TFDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQG 325
Cdd:COG0465   140 TFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 326 ARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSI--HPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLR 403
Cdd:COG0465   220 ASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLR 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 404 PGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEAR 483
Cdd:COG0465   300 PGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAI 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 484 DRVLMGPARTGGRIPDEEaNRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDV 563
Cdd:COG0465   380 DRVIAGPERKSRVISEKE-KKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAV 458
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 564 MMGGRVAEELIFGDdkVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNESAL----VKVSDLAPQTAELIDAE 639
Cdd:COG0465   459 LLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLgrdiGQSRNYSEETAREIDEE 536
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511375 640 INRVLQESYKRAKVILETKKKEHQLLAEALLEYETLSADEVKRVISG 686
Cdd:COG0465   537 VRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
195-685 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: 615.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 195 SNTLTRFYIFLVFCIFFGYLTGRiRVRVGDRQIGSLFFSNPQEVNPEDVQVTFDDVRGMDEAKLEVEEIVDYLKDPEKYS 274
Cdd:TIGR01241   3 LGFLFSLLPPILLLVGVWFFFRR-QMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 275 RLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGS 354
Cdd:TIGR01241  82 KLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 355 KR--VSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKI 432
Cdd:TIGR01241 162 QRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 433 VHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEARDRVLMGPARTGGRIPDEEaNRNTAYHEAG 512
Cdd:TIGR01241 242 KLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKE-KKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 513 HTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDVMMGGRVAEELIFGDdkVTTGAADDLSKAT 592
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGE--VTTGASNDIKQAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 593 QLAVQMVKVFGMSDKVGLRDFTAQDNESALVKVSDLAP----QTAELIDAEINRVLQESYKRAKVILETKKKEHQLLAEA 668
Cdd:TIGR01241 399 NIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKeyseETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*..
gi 1831511375 669 LLEYETLSADEVKRVIS 685
Cdd:TIGR01241 479 LLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
180-706 6.21e-150

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 451.03  E-value: 6.21e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 180 LLSNGVSGAGKDGKKSNTLTRFYI-FLVFCIFFGYLTGRIRVRVGDRQIGSLFF--SNPQEVNPEDVQVTFDDVRGMDEA 256
Cdd:PRK10733   81 LLTKNVKVVGEPPEEPSLLASIFIsWFPMLLLIGVWIFFMRQMQGGGGKGAMSFgkSKARMLTEDQIKTTFADVAGCDEA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 257 KLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKA 336
Cdd:PRK10733  161 KEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQA 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 337 KARAPCIIFIDEIDSVGSKRVS--NSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTVP 414
Cdd:PRK10733  241 KKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 415 KPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEARDRVLMGPARTg 494
Cdd:PRK10733  321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERR- 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 495 GRIPDEEANRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDVMMGGRVAEELI 574
Cdd:PRK10733  400 SMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEII 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 575 FGDDKVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNE----SALVKVSDLAPQTAELIDAEINRVLQESYKR 650
Cdd:PRK10733  480 YGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEvflgRSVAKAKHMSDETARIIDQEVKALIERNYNR 559
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831511375 651 AKVILETKKKEHQLLAEALLEYETLSADEVKRVISGQKIkRPtPAAVKKSNETKRN 706
Cdd:PRK10733  560 ARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDV-RP-PAGWEEPGASNNS 613
ftsH CHL00176
cell division protein; Validated
245-694 1.36e-149

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 449.89  E-value: 1.36e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 245 VTFDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQ 324
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 325 GARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVS--NSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALL 402
Cdd:CHL00176  260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 403 RPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEA 482
Cdd:CHL00176  340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 483 RDRVLMGPArtGGRIPDEEANRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLD 562
Cdd:CHL00176  420 IDRVIAGLE--GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIV 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 563 VMMGGRVAEELIFGDDKVTTGAADDLSKATQLAVQMVKVFGMSdKVGLRDFTAQDNESALV-----KVSDLAPQTAELID 637
Cdd:CHL00176  498 GALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLgrfmqRNSEYSEEIADKID 576
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511375 638 AEINRVLQESYKRAKVILETKKKEHQLLAEALLEYETLSADEVKRVISGQKIKRPTP 694
Cdd:CHL00176  577 MEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILPPKK 633
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
240-486 1.01e-103

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 320.41  E-value: 1.01e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 240 PEDVQVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFD 318
Cdd:COG1222    70 AESPDVTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 319 EVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLD 398
Cdd:COG1222   150 SKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLD 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 399 KALLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAY 478
Cdd:COG1222   230 PALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMED 309

                  ....*...
gi 1831511375 479 LDEARDRV 486
Cdd:COG1222   310 LEKAIEKV 317
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
245-413 1.23e-100

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: 306.47  E-value: 1.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 245 VTFDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQ 324
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 325 GARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSI--HPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALL 402
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGggHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1831511375 403 RPGRFDVRVTV 413
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
496-683 3.46e-91

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 282.57  E-value: 3.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 496 RIPDEEANRNTAYHEAGHTLVSLYTKDATPLHKVTIIPRGQSLGHTAMLPEKDSYQLTKAQMLATLDVMMGGRVAEELIF 575
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 576 GddKVTTGAADDLSKATQLAVQMVKVFGMSDKVGLRDFTAQDNESALV----KVSDLAPQTAELIDAEINRVLQESYKRA 651
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGrgmgKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1831511375 652 KVILETKKKEHQLLAEALLEYETLSADEVKRV 683
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
244-487 7.75e-81

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 262.85  E-value: 7.75e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 244 QVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLV 322
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 323 GQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRV--SNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKA 400
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTdsGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 401 LLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLD 480
Cdd:PRK03992  287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFL 366

                  ....*..
gi 1831511375 481 EARDRVL 487
Cdd:PRK03992  367 KAIEKVM 373
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
235-486 2.08e-77

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: 254.07  E-value: 2.08e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 235 PQEVNPEDVQVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTA 313
Cdd:COG0464   144 LEEELLELREAILDDLGGLEEVKEELRELVALpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 314 GSEFDEVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSiHPYANQTINQLLSEMDGFTrnEGIIVIAATNR 393
Cdd:COG0464   224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG-DGVGRRVVNTLLTEMEELR--SDVVVIAATNR 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 394 VDDLDKALLRpgRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVE 473
Cdd:COG0464   301 PDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREP 378
                         250
                  ....*....|...
gi 1831511375 474 VTMAYLDEARDRV 486
Cdd:COG0464   379 VTTEDLLEALERE 391
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
247-482 5.98e-68

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 223.61  E-value: 5.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 247 FDDVRGMDEAKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGA 326
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 327 RRVRDLFDKAKaRAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGFtrNEGIIVIAATNRVDDLDKALLRpgR 406
Cdd:COG1223    81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--R 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831511375 407 FDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEA 482
Cdd:COG1223   156 FDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
241-487 1.10e-67

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: 226.99  E-value: 1.10e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 241 EDVQVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDE 319
Cdd:TIGR01242 115 ERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 320 VLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRV--SNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDL 397
Cdd:TIGR01242 195 KYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTdsGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDIL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 398 DKALLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMA 477
Cdd:TIGR01242 275 DPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMD 354
                         250
                  ....*....|
gi 1831511375 478 YLDEARDRVL 487
Cdd:TIGR01242 355 DFIKAVEKVL 364
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
256-413 3.36e-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: 207.52  E-value: 3.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 256 AKLEVEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDK 335
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831511375 336 AKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTV 413
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
236-487 2.43e-61

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: 219.01  E-value: 2.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 236 QEVNPEDVQVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAG 314
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRG 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 315 SEFDEVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRV 394
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRP 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 395 DDLDKALLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEV 474
Cdd:TIGR01243 601 DILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP 680
                         250
                  ....*....|...
gi 1831511375 475 TMAYLDEARDRVL 487
Cdd:TIGR01243 681 AKEKLEVGEEEFL 693
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
246-413 3.34e-58

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: 194.86  E-value: 3.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 246 TFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQ 324
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 325 GARRVRDLFDKAKARAPCIIFIDEIDSVGSKRV--SNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALL 402
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFdsGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                         170
                  ....*....|.
gi 1831511375 403 RPGRFDVRVTV 413
Cdd:cd19502   161 RPGRFDRKIEF 171
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
256-413 7.61e-57

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: 190.57  E-value: 7.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 256 AKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFD 334
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831511375 335 KAKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTV 413
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 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 ...
249-408 3.63e-52

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: 178.25  E-value: 3.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGAR 327
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 328 RVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSiHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRF 407
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQ-REVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRF 159

                  .
gi 1831511375 408 D 408
Cdd:cd19503   160 D 160
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
284-414 9.63e-52

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: 175.47  E-value: 9.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSiHP 363
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG-DS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1831511375 364 YANQTINQLLSEMDGFTRNEG-IIVIAATNRVDDLDKALLrpGRFDVRVTVP 414
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
246-499 2.54e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 181.89  E-value: 2.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 246 TFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQ 324
Cdd:PTZ00361  181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 325 GARRVRDLFDKAKARAPCIIFIDEIDSVGSKR--VSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALL 402
Cdd:PTZ00361  261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 403 RPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDEA 482
Cdd:PTZ00361  341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420
                         250
                  ....*....|....*..
gi 1831511375 483 RDRVLMgpaRTGGRIPD 499
Cdd:PTZ00361  421 KEKVLY---RKKGNIPE 434
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
245-487 5.40e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 177.26  E-value: 5.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 245 VTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVG 323
Cdd:PTZ00454  142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 324 QGARRVRDLFDKAKARAPCIIFIDEIDSVGSKR--VSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKAL 401
Cdd:PTZ00454  222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 402 LRPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDE 481
Cdd:PTZ00454  302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEK 381

                  ....*.
gi 1831511375 482 ARDRVL 487
Cdd:PTZ00454  382 GYKTVV 387
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
257-408 1.70e-48

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: 168.07  E-value: 1.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 257 KLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDK 335
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 336 AKARAPCIIFIDEIDSVGSKRVSNSIHP--YANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFD 408
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLD 156
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
256-413 3.78e-48

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: 166.90  E-value: 3.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 256 AKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFD 334
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831511375 335 KAKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTV 413
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
244-466 6.64e-48

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: 180.87  E-value: 6.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 244 QVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLV 322
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 323 GQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRvSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALL 402
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKR-EEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALR 332
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831511375 403 RPGRFDVRVTVPKPDLAGRVDIFNFYLSKIVHSGGIDPKVLAKGSTGFTGADIENMVNQAALKA 466
Cdd:TIGR01243 333 RPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAA 396
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
249-408 1.13e-47

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 166.04  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIVDYLK-DPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGAR 327
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 328 RVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSiHPYANQTINQLLSEMDGFTRNE----GIIVIAATNRVDDLDKALLR 403
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQ-REMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPALRR 159

                  ....*
gi 1831511375 404 PGRFD 408
Cdd:cd19518   160 AGRFD 164
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
249-414 3.52e-45

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: 159.14  E-value: 3.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGAR 327
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 328 RVRDLFDKAKARAPCIIFIDEIDSVGSKRvSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRF 407
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRF 159

                  ....*..
gi 1831511375 408 DVRVTVP 414
Cdd:cd19519   160 DREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
253-408 3.36e-43

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: 153.41  E-value: 3.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 253 MDEAKLEVE-EIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRD 331
Cdd:cd19530     1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511375 332 LFDKAKARAPCIIFIDEIDSVGSKRvSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFD 408
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKR-GDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
250-413 2.17e-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: 145.57  E-value: 2.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 250 VRGMDEAKLEVEEIVDY-LKDPEKYSrLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARR 328
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 329 VRDLFDKAKARAPCIIFIDEIDSVGSKRVSnSIHPYANQTINQLLSEMDGFT--RNEGIIVIAATNRVDDLDKALLRpgR 406
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGS-GEHEASRRVKTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR--R 156

                  ....*..
gi 1831511375 407 FDVRVTV 413
Cdd:cd19509   157 FEKRIYI 163
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
256-408 1.53e-39

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: 142.95  E-value: 1.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 256 AKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFD 334
Cdd:cd19526     1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831511375 335 KAKARAPCIIFIDEIDSVGSKRVSNSIHpYANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFD 408
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTG-VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLD 153
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
262-408 2.35e-36

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: 134.18  E-value: 2.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 262 EIVDYLKDPEKYSRL---GGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKAKA 338
Cdd:cd19527     4 EILDTIQLPLEHPELfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831511375 339 RAPCIIFIDEIDSVGSKR-VSNSIHPYANQTINQLLSEMDGF-TRNEGIIVIAATNRVDDLDKALLRPGRFD 408
Cdd:cd19527    84 AKPCVIFFDELDSLAPSRgNSGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFD 155
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
249-408 2.66e-35

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: 131.48  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIA-----GEAQVPFFHTAGSEFDEVLV 322
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 323 GQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVS--NSIHpyaNQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKA 400
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSkqEQIH---ASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPA 157

                  ....*...
gi 1831511375 401 LLRPGRFD 408
Cdd:cd19517   158 LRRPGRFD 165
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
224-413 4.24e-34

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: 128.57  E-value: 4.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 224 DRQIGSLFFSNPQEVNPEdvqVTFDDVRGMDEAKLEVEEIVDY-LKDPEKYSRLGGRlPKGVLLVGPPGTGKTLLARAIA 302
Cdd:cd19525     1 EPKMIELIMSEIMDHGPP---INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 303 GEAQVPFFHTAGSEFDEVLVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRvSNSIHPYANQTINQLLSEMDGFTR- 381
Cdd:cd19525    77 SQSGATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR-GEGEHESSRRIKTEFLVQLDGATTs 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1831511375 382 -NEGIIVIAATNRVDDLDKALLRpgRFDVRVTV 413
Cdd:cd19525   156 sEDRILVVGATNRPQEIDEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
249-413 8.61e-33

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 124.33  E-value: 8.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIV-------DYLKdpekysrlGGRLP-KGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEV 320
Cdd:cd19522     1 DIADLEEAKKLLEEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 321 LVGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDGF---TRNEG----IIVIAATNR 393
Cdd:cd19522    73 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVggaSENDDpskmVMVLAATNF 152
                         170       180
                  ....*....|....*....|
gi 1831511375 394 VDDLDKALLRpgRFDVRVTV 413
Cdd:cd19522   153 PWDIDEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
249-409 5.98e-32

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: 121.76  E-value: 5.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIVDY-LKDPEKYSrlGGRL---PKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQ 324
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 325 GARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSiHPYANQTINQLLSEMDGFTR--NEGIIVIAATNRVDDLDKALL 402
Cdd:cd19520    79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTD-HEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDEAIL 157

                  ....*....
gi 1831511375 403 R--PGRFDV 409
Cdd:cd19520   158 RrmPKRFHI 166
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
249-413 3.30e-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: 3.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEVEEIVDYLKD-PEKYSRLGgRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGAR 327
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLrPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 328 RVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSiHPYANQTINQLLSEMDGFTRN--EGIIVIAATNRVDDLDKALLRpg 405
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGE-HEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                  ....*...
gi 1831511375 406 RFDVRVTV 413
Cdd:cd19524   157 RFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
245-413 4.18e-29

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: 113.80  E-value: 4.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 245 VTFDDVRGMDEAKLEVEEIVDYlkdPEKYSRL--GGRLP-KGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVL 321
Cdd:cd19521     4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 322 VGQGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSIHPyANQTINQLLSEMDGFTRN-EGIIVIAATNRVDDLDKA 400
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEA-SRRIKTELLVQMNGVGNDsQGVLVLGATNIPWQLDSA 159
                         170
                  ....*....|...
gi 1831511375 401 LLRpgRFDVRVTV 413
Cdd:cd19521   160 IRR--RFEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
270-413 4.78e-28

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: 111.04  E-value: 4.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 270 PEKYSRLGGRLPKGVLLVGPPGTGKTLLARAI-----AGEAQVpffhTAGSEFDEVLVGQGARRVRDLFDKA----KARA 340
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqRRLG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 341 PC----IIFIDEIDSV----GSKRVSNSIHpyaNQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVT 412
Cdd:cd19504   100 ANsglhIIIFDEIDAIckqrGSMAGSTGVH---DTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQME 176

                  .
gi 1831511375 413 V 413
Cdd:cd19504   177 I 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
252-415 7.18e-27

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: 106.85  E-value: 7.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 252 GMDEAKLEVEEIVDYLKdpekysrlggrlPKGVLLVGPPGTGKTLLARAIAGEA---QVPFFHTAGSEFDEVLVGQGARR 328
Cdd:cd00009     2 GQEEAIEALREALELPP------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 329 ---VRDLFDKAKARAPCIIFIDEIDSVGSKRVsnsihpyaNQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPG 405
Cdd:cd00009    70 hflVRLLFELAEKAKPGVLFIDEIDSLSRGAQ--------NALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYD 141
                         170
                  ....*....|
gi 1831511375 406 RFDVRVTVPK 415
Cdd:cd00009   142 RLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
243-494 1.03e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 111.26  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 243 VQVTFDDVRGMDEAKleveeivDYLKD-----PEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFH-TAGSE 316
Cdd:CHL00195  223 VNEKISDIGGLDNLK-------DWLKKrstsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRlDVGKL 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 317 FDEvLVGQGARRVRDLFDKAKARAPCIIFIDEIDsvgsKRVSNSIHPYANQTINQLLSEMDGF--TRNEGIIVIAATNRV 394
Cdd:CHL00195  296 FGG-IVGESESRMRQMIRIAEALSPCILWIDEID----KAFSNSESKGDSGTTNRVLATFITWlsEKKSPVFVVATANNI 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 395 DDLDKALLRPGRFDVRVTVPKPDLAGRVDIFNFYLSKI--VHSGGIDPKVLAKGSTGFTGADIENMVNQAALKAATDN-- 470
Cdd:CHL00195  371 DLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKre 450
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1831511375 471 --------AVE--VTMAYLDEARDRVLMGPARTG 494
Cdd:CHL00195  451 fttddillALKqfIPLAQTEKEQIEALQNWASSG 484
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
249-408 2.56e-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: 97.05  E-value: 2.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKleveeivDYLKDPEK-----YSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVG 323
Cdd:cd19507     1 DVGGLDNLK-------DWLKKRKAafskqASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 324 QGARRVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEMDgfTRNEGIIVIAATNRVDDLDKALLR 403
Cdd:cd19507    74 ESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLR 151

                  ....*
gi 1831511375 404 PGRFD 408
Cdd:cd19507   152 KGRFD 156
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
249-413 1.40e-22

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: 94.95  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 249 DVRGMDEAKLEV-EEIVDYLKDPEKYSRLGgRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGAR 327
Cdd:cd19523     1 DIAGLGALKAAIkEEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 328 RVRDLFDKAKARAPCIIFIDEIDSVGSKRVSNsiHPYANQTINQLLSEMDGF--TRNEGIIVIAATNRVDDLDKALLRpg 405
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDE--ASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR-- 155

                  ....*...
gi 1831511375 406 RFDVRVTV 413
Cdd:cd19523   156 YFSKRLLV 163
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
260-413 2.55e-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: 88.18  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 260 VEEIVDYLKDPEKYSRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEfdevlVGQGARRVRDLFDKAKAR 339
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831511375 340 ApcIIFIDEIDSVGSKRVSNSIHPYANQ-----TINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPGRFDVRVTV 413
Cdd:cd19510    77 S--IILLEDIDAAFESREHNKKNPSAYGglsrvTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
281-417 4.69e-20

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: 87.43  E-value: 4.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375  281 PKGVLLVGPPGTGKTLLARAIAGEAQVP---FFHTAGSEFDEV--------------LVGQGARRVRDLFDKAKARAPCI 343
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831511375  344 IFIDEIDSVGSKRVSNSIhpyanqTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKALLRPgRFDVRVTVPKPD 417
Cdd:smart00382  82 LILDEITSLLDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
275-408 2.14e-15

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 74.33  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 275 RLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEF--------------DEVLVGQGARRVRDLFDKAKARA 340
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLlynkpdfgnddwidGMLILKESLHRLNLQFELAKAMS 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831511375 341 PCIIFIDEIDSVGSKRVSNSIHPYANQTINQLLSEM-DGF----TRNegIIVIAATNRVDDLDKALLRPGRFD 408
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLsRDFekssTRN--ILVIASTHIPQKVDPALIAPNRLD 156
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
283-407 1.71e-13

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: 68.09  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 283 GVLLVGPPGTGKTLLARAIAgEA--QVPFFHTAGSEF---DEVLvgqGARRVRDLFDK-------AKARAPCIIFIDEID 350
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteEDLF---GRRNIDPGGASwvdgplvRAAREGEIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 351 SVGSKrVSNSIHPYANqtiNQLLSEMDGFTR----NEGIIVIAATNRVD----DLDKALLRpgRF 407
Cdd:pfam07728  77 RANPD-VLNSLLSLLD---ERRLLLPDGGELvkaaPDGFRLIATMNPLDrglnELSPALRS--RF 135
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
282-411 5.73e-11

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: 61.00  E-value: 5.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 282 KGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEvLVGQGARRVRDLFDKA-KARAPCIIFIDEIDSVGSKRVSNS 360
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP-MGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511375 361 IHPYANQTINQLLSEMDGFTRNegIIVIAATNRVDDLDKALlrPGRFDVRV 411
Cdd:cd19512   102 ISEDLRAALNAFLYRTGEQSNK--FMLVLASNQPEQFDWAI--NDRIDEMV 148
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
280-411 2.54e-10

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: 60.09  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 280 LPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEV-LVGQGARR-VRDLFDKakarapcIIFIDEIDSVGSKRV 357
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVESiIRDLVEG-------IVFIDEIDKIAKRGG 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831511375 358 SNSIHPYANQTINQLLSEMDGFT--------RNEGIIVIAA----TNRVDDLDKALlrPGRFDVRV 411
Cdd:cd19498   118 SSGPDVSREGVQRDLLPIVEGSTvstkygpvKTDHILFIAAgafhVAKPSDLIPEL--QGRFPIRV 181
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
278-349 5.53e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.91  E-value: 5.53e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831511375 278 GRLPKgVLLVGPPGTGKTLLARAIAGEAQVPFfhtagsefdEVL--VGQGARRVRDLFDKAKARA----PCIIFIDEI 349
Cdd:COG2256    47 GRLSS-MILWGPPGTGKTTLARLIANATDAEF---------VALsaVTSGVKDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
277-349 5.94e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.94  E-value: 5.94e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511375 277 GGRLPKgVLLVGPPGTGKTLLARAIAGEAQVPFFhtagsEFDEVLVGQgaRRVRDLFDKAKARA----PCIIFIDEI 349
Cdd:PRK13342   33 AGRLSS-MILWGPPGTGKTTLARIIAGATDAPFE-----ALSAVTSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
252-414 1.36e-08

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: 57.93  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 252 GMDEAKLEVEEIVDYLKDPEKYSRLGGRLP---KGVLLVGPPGTGKTLLARAIA------GEAQVP-FFHTAGSEFDEVL 321
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 322 VGQGARRVRDLFDKAKARapcIIFIDEIDSVGSKRVSNSiHPYANQTINQLLSEMDGfTRNEGIIVIAATNrvDDLDKAL 401
Cdd:TIGR03922 360 IGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQK-DPFGLEAIDTLLARMEN-DRDRLVVIGAGYR--KDLDKFL 432
                         170
                  ....*....|....*...
gi 1831511375 402 -----LRpGRFDVRVTVP 414
Cdd:TIGR03922 433 evnegLR-SRFTRVIEFP 449
PRK04195 PRK04195
replication factor C large subunit; Provisional
246-350 1.39e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 58.01  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 246 TFDDVRGMDEAKlevEEIVDYLKdpekySRLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFD-----EV 320
Cdd:PRK04195   12 TLSDVVGNEKAK---EQLREWIE-----SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQRtadviER 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 1831511375 321 LVGQGARRvRDLFDKAKArapcIIFIDEID 350
Cdd:PRK04195   84 VAGEAATS-GSLFGARRK----LILLDEVD 108
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
284-398 7.48e-08

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: 51.35  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVgqgaRRVRDLFDKAKaraPCIIFIDEIDSVGSKRVSNSIHP 363
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARASQGDRSSE 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831511375 364 YANQTInqllsEMDGFTRNEGIIVIAATNRVDDLD 398
Cdd:cd01120    74 LLEDLA-----KLLRAARNTGITVIATIHSDKFDI 103
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
272-317 1.47e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 54.59  E-value: 1.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1831511375 272 KYSRLGGRlpkGVLLVGPPGTGKTLLARAIAGE--AQVPFFHTAGSEF 317
Cdd:COG1224    58 KEGKMAGK---GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
284-401 2.37e-07

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: 51.68  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPF-FHTAGSEFDEV--------LVGQGARRVRDLFDKAKARAP---CIIF--IDEI 349
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQELIDdkdALVFvlIDEV 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 350 DSVGSKR--VSNSIHPY-ANQTINQLLSEMDGFTRNEGIIVIAATNRVDDLDKAL 401
Cdd:cd19508   135 ESLAAARsaSSSGTEPSdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
263-317 6.08e-07

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 52.31  E-value: 6.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511375 263 IVDYLKDpekySRLGGRlpkGVLLVGPPGTGKTLLARAIAGE--AQVPFFHTAGSEF 317
Cdd:pfam06068  39 IVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
281-410 8.34e-07

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: 49.50  E-value: 8.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 281 PKGV-LLVGPPGTGKTLLARAIAGE---AQVPFFHTAGSEFDE--------------VLVGQGARrvrdLFDKAKARAPC 342
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEehsvsrligappgyVGYEEGGQ----LTEAVRRKPYS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 343 IIFIDEIDsvgsKrvsnsIHPYANQTINQLLSE---MDGF-----TRNegIIVIAATN---------------------- 392
Cdd:pfam07724  78 IVLIDEIE----K-----AHPGVQNDLLQILEGgtlTDKQgrtvdFKN--TLFIMTGNfgsekisdasrlgdspdyellk 146
                         170       180
                  ....*....|....*....|..
gi 1831511375 393 -RVDDLDKALLRP---GRFDVR 410
Cdd:pfam07724 147 eEVMDLLKKGFIPeflGRLPII 168
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
250-361 2.77e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 49.52  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 250 VRGMDEAK--LEVEEIVDY--LKDPEKYSRLGGRLPKG-VLLVGPPGTGKTLLARAIAGEAQVPFFHT----------AG 314
Cdd:cd19497    14 VIGQERAKkvLSVAVYNHYkrIRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIAdattlteagyVG 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1831511375 315 SEFDEVLVG--QGARrvrdlFDKAKARAPcIIFIDEIDSVGSKRVSNSI 361
Cdd:cd19497    94 EDVENILLKllQAAD-----YDVERAQRG-IVYIDEIDKIARKSENPSI 136
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
280-403 3.08e-06

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 47.62  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 280 LPKG--VLLVGPPGTGKTLLARAIAGEAQVP----FFHtaGSEFDEVLVGQGARRVRDLFD------------KAKARAP 341
Cdd:cd00267    22 LKAGeiVALVGPNGSGKSTLLRAIAGLLKPTsgeiLID--GKDIAKLPLEELRRRIGYVPQlsggqrqrvalaRALLLNP 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831511375 342 CIIFIDEIDSvgskrvsnSIHPYANQTINQLLSEMdgftRNEGIIVIAATNRVDDLDKALLR 403
Cdd:cd00267   100 DLLLLDEPTS--------GLDPASRERLLELLREL----AEEGRTVIIVTHDPELAELAADR 149
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
247-349 3.95e-06

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 48.62  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 247 FDDVRGMDEAKLEVEEIVDYLKDPEkysrlggrlpkGVLLVGPPGTGKTLLARAIAGEA-----QVPFFHTAgSEFDEVL 321
Cdd:COG1484    76 FDAQPGLDRRQILELATLDFIERGE-----------NLILLGPPGTGKTHLAIALGHEAcragyRVRFTTAP-DLVNELK 143
                          90       100
                  ....*....|....*....|....*...
gi 1831511375 322 VGQGARRVRDLFDKAKaRAPCIIfIDEI 349
Cdd:COG1484   144 EARADGRLERLLKRLA-KVDLLI-LDEL 169
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
284-361 4.36e-06

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 49.66  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFfhT---------AGsefdevLVG-----------QGArrvrDlFDKAKA-RApc 342
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTLARILDVPF--AiadattlteAG------YVGedvenillkllQAA----D-YDVEKAeRG-- 176
                          90
                  ....*....|....*....
gi 1831511375 343 IIFIDEIDSVGSKRVSNSI 361
Cdd:COG1219   177 IIYIDEIDKIARKSENPSI 195
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
438-481 5.00e-06

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: 43.68  E-value: 5.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1831511375 438 IDPKVLAKGSTGFTGADIENMVNQAALKAATDNAVEVTMAYLDE 481
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
248-354 1.09e-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: 46.40  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 248 DDVRGMDEAKlevEEIVDYLKdpekYSRLGGRLpKG--VLLVGPPGTGKTLLARAIAGEAQVPFFHTA-GSEFDE----- 319
Cdd:cd19500    10 ADHYGLEDVK---ERILEYLA----VRKLKGSM-KGpiLCLVGPPGVGKTSLGKSIARALGRKFVRISlGGVRDEaeirg 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1831511375 320 ---VLVGQGARRVRDLFDKAKARAPcIIFIDEIDSVGS 354
Cdd:cd19500    82 hrrTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
284-424 2.11e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 47.08  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFH---TAG---SEF--DEVLVGQ-GARRVRD--LFDkakarapCIIFIDEIDsv 352
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRiqfTPDllpSDIlgTYIYDQQtGEFEFRPgpLFA-------NVLLADEIN-- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 353 gskRVSnsihPyanQTINQLLSEM-------DGFTR--NEGIIVIAATNRVD-----DLDKALLRpgRFDVRVTVPKPDL 418
Cdd:COG0714   105 ---RAP----P---KTQSALLEAMeerqvtiPGGTYklPEPFLVIATQNPIEqegtyPLPEAQLD--RFLLKLYIGYPDA 172

                  ....*.
gi 1831511375 419 AGRVDI 424
Cdd:COG0714   173 EEEREI 178
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
284-361 2.38e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 47.46  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPfFHTA-----------GSEFDEVLVG--QGArrvrDlFDKAKA-RApcIIFIDEI 349
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGEDVENILLKllQAA----D-YDVEKAqRG--IVYIDEI 182
                          90
                  ....*....|..
gi 1831511375 350 DSVGSKRVSNSI 361
Cdd:PRK05342  183 DKIARKSENPSI 194
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
278-350 6.56e-05

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 45.35  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 278 GRLPKGVLLVGPPGTGKTLLARAIA-------GEAQVPFFH------TAGSEFD----EVLVGQGARR---VRDLFDKAK 337
Cdd:COG0470    15 GRLPHALLLHGPPGIGKTTLALALArdllcenPEGGKACGQchsrlmAAGNHPDllelNPEEKSDQIGidqIRELGEFLS 94
                          90
                  ....*....|....*..
gi 1831511375 338 ARAPC----IIFIDEID 350
Cdd:COG0470    95 LTPLEggrkVVIIDEAD 111
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
259-306 6.93e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 45.61  E-value: 6.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1831511375 259 EVEEIVDYLKDPekysrLGGRLPKGVLLVGPPGTGKTLLARAIAGEAQ 306
Cdd:COG1474    34 EIEELASALRPA-----LRGERPSNVLIYGPTGTGKTAVAKYVLEELE 76
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
284-314 1.59e-04

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 42.87  E-value: 1.59e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFHTAG 314
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
247-303 1.66e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 44.65  E-value: 1.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831511375 247 FDDVRGMDEAK--LEVeeivdylkdpekySRLGGRlpkGVLLVGPPGTGKTLLARAIAG 303
Cdd:COG0606   191 LADVKGQEQAKraLEI-------------AAAGGH---NLLMIGPPGSGKTMLARRLPG 233
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
284-349 4.54e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 4.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDevlvgqgarRVRDLF---------DkakarapcIIFIDEI 349
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALE---------KPGDLAailtnleegD--------VLFIDEI 111
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
259-400 5.63e-04

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 41.34  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 259 EVEEIVDYLKDPEKYSrlggrlPKGVLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDEVLVGQGARR-------VRD 331
Cdd:pfam13191   8 ELEQLLDALDRVRSGR------PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEaltreglLRQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831511375 332 LFDKAKAR--APCIIFIDEIdsvgSKRVSNSIHPYANQTINQLLSEMDGFTRNEGIIVIAatnrVDDLDKA 400
Cdd:pfam13191  82 LLDELESSllEAWRAALLEA----LAPVPELPGDLAERLLDLLLRLLDLLARGERPLVLV----LDDLQWA 144
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
245-349 5.73e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 43.22  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 245 VTFDDVRGMDEAKLEVEEIVDYL--KDPEKYSRLGGRL--PKGVLLVGPPGTGKT----LLARAIAGEAQ-----VPfFH 311
Cdd:COG1401   181 LSAAEELYSEDLESEDDYLKDLLreKFEETLEAFLAALktKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQ-FH 259
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831511375 312 TAGSEFDEVL-----VGQGARRVRD-LFDKA--KARA----PCIIFIDEI 349
Cdd:COG1401   260 PSWSYEDFLLgyrpsLDEGKYEPTPgIFLRFclKAEKnpdkPYVLIIDEI 309
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
284-349 6.61e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.38  E-value: 6.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDevlvgqgarRVRDL---------FDkakarapcIIFIDEI 349
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAIE---------KPGDLaailtnleeGD--------VLFIDEI 114
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
276-305 8.83e-04

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 41.44  E-value: 8.83e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1831511375 276 LGGRLPKG--VLLVGPPGTGKTLLARAIAGEA 305
Cdd:COG0467    13 LGGGLPRGssTLLSGPPGTGKTTLALQFLAEG 44
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
247-303 1.08e-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: 40.98  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831511375 247 FDDVRGMDEAK--LEVEEIvdylkdpekysrlGGRlpkGVLLVGPPGTGKTLLARAIAG 303
Cdd:pfam01078   2 LADVKGQEQAKraLEIAAA-------------GGH---NLLMIGPPGSGKTMLAKRLPG 44
PRK13341 PRK13341
AAA family ATPase;
285-349 1.86e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.58  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 285 LLVGPPGTGKTLLARAIAGeaqvpffHTAG--SEFDEVLVGqgarrVRDL---FDKAKARAP-----CIIFIDEI 349
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIAN-------HTRAhfSSLNAVLAG-----VKDLraeVDRAKERLErhgkrTILFIDEV 118
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
284-349 2.28e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEA-----QVPFFHTAGsefdevLVGQ--GARRVRDLFDKAK--ARAPCIIfIDEI 349
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTAAD------LVEQlaQARADGRLGRLLRrlARYDLLI-IDEL 160
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
246-302 2.46e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 40.56  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511375 246 TFDDVRGMdeaklevEEIVDYLKdpekYSRLGGRLPKGVLLVGPPGTGKTLLARAIA 302
Cdd:COG2812     8 TFDDVVGQ-------EHVVRTLK----NALASGRLAHAYLFTGPRGVGKTTLARILA 53
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
284-486 2.56e-03

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 40.72  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAI------AGEAQVP---------------FFHTAGSeFdevlvgQGARRVRD-LFDKAKArap 341
Cdd:COG2204   157 VLITGESGTGKELVARAIhrlsprADGPFVAvncaaipeelleselFGHEKGA-F------TGAVARRIgKFELADG--- 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 342 CIIFIDEIDSVgskrvsnsihPYANQTinQLLS--EMDGFTR---NEGIIV----IAATNRvdDLdKALLRPGRFD---- 408
Cdd:COG2204   227 GTLFLDEIGEM----------PLALQA--KLLRvlQEREFERvggNKPIPVdvrvIAATNR--DL-EELVEEGRFRedly 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 409 -----VRVTVPkPDLAGRVDI---FNFYLSKIVHSGGIDPKVLAKGSTGFTGAD-------IENMVNQAALKAATDnavE 473
Cdd:COG2204   292 yrlnvFPIELP-PLRERREDIpllARHFLARFAAELGKPVKLSPEALEALLAYDwpgnvreLENVIERAVILADGE---V 367
                         250
                  ....*....|...
gi 1831511375 474 VTMAYLDEARDRV 486
Cdd:COG2204   368 ITAEDLPEALEEV 380
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
248-301 2.83e-03

PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.


Pssm-ID: 214810  Cd Length: 361  Bit Score: 40.74  E-value: 2.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1831511375  248 DDVRGMDEAkleVEEIVDYLKDPEKysRLGGRlpKGVL-LVGPPGTGKTLLARAI 301
Cdd:smart00763  51 HDFFGMEEA---IERFVNYFKSAAQ--GLEER--KQILyLLGPVGGGKSSLVECL 98
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
250-350 3.15e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 39.08  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 250 VRGMDEAKLEVEEIV----DYLKDPEKysrlggrlPKGVLL-VGPPGTGKTLLARAIAGeaqvpFFHTAG--------SE 316
Cdd:cd19499    13 VVGQDEAVKAVSDAIrrarAGLSDPNR--------PIGSFLfLGPTGVGKTELAKALAE-----LLFGDEdnliridmSE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831511375 317 FDE--------------VLVGQGARrvrdLFDKAKARAPCIIFIDEID 350
Cdd:cd19499    80 YMEkhsvsrligappgyVGYTEGGQ----LTEAVRRKPYSVVLLDEIE 123
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
284-349 3.16e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 40.36  E-value: 3.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGEAQVPFFHTAGSEFDevlvgqgarRVRDLFDKAKARAPC-IIFIDEI 349
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAILTNLEEGdVLFIDEI 90
44 PHA02544
clamp loader, small subunit; Provisional
278-445 3.39e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 40.36  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 278 GRLPKGVLLVGPPGTGKTLLARAIAGE--AQVPFFHTAGSEFDEV--LVGQGARRVrDLFDKAKarapcIIFIDEIDSVG 353
Cdd:PHA02544   40 GRIPNMLLHSPSPGTGKTTVAKALCNEvgAEVLFVNGSDCRIDFVrnRLTRFASTV-SLTGGGK-----VIIIDEFDRLG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 354 SKRVSNSihpyanqtinqLLSEMDGFTRNEGIIVIAatNRVDDLDKALLrpGRFDVrVTVPKPDLAGRVDIFnfyLSKIV 433
Cdd:PHA02544  114 LADAQRH-----------LRSFMEAYSKNCSFIITA--NNKNGIIEPLR--SRCRV-IDFGVPTKEEQIEMM---KQMIV 174
                         170       180
                  ....*....|....*....|
gi 1831511375 434 HSGGI--------DPKVLAK 445
Cdd:PHA02544  175 RCKGIleaegvevDMKVLAA 194
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
279-303 4.78e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 40.18  E-value: 4.78e-03
                          10        20
                  ....*....|....*....|....*..
gi 1831511375 279 RLPKG--VLLVGPPGTGKTLLARAIAG 303
Cdd:COG4178   385 SLKPGerLLITGPSGSGKSTLLRAIAG 411
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
260-308 4.85e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 38.24  E-value: 4.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831511375 260 VEEIVDYLKD-PEKYSRLggrlpkgVLLVGPPGTGKTLLARAIAGEAQVP 308
Cdd:NF033453    1 LEKLKRSVDEaESLYYKL-------ILLVGPPGSGKTALLRELAAKRGAP 43
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
250-302 5.55e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831511375 250 VRGMDEAkleVEEIVDY-------LKDPEKysrlggrlPKGV-LLVGPPGTGKTLLARAIA 302
Cdd:COG0542   551 VIGQDEA---VEAVADAirrsragLKDPNR--------PIGSfLFLGPTGVGKTELAKALA 600
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
284-348 6.69e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.00  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511375 284 VLLVGPPGTGKTLLARAIAGE-------AQVP--------FFHTAGSEFD-EVLVGQGARRVRD----LFDKAKARAPCI 343
Cdd:COG3267    46 VVLTGEVGTGKTTLLRRLLERlpddvkvAYIPnpqlspaeLLRAIADELGlEPKGASKADLLRQlqefLLELAAAGRRVV 125

                  ....*
gi 1831511375 344 IFIDE 348
Cdd:COG3267   126 LIIDE 130
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
285-302 7.71e-03

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 39.62  E-value: 7.71e-03
                          10
                  ....*....|....*...
gi 1831511375 285 LLVGPPGTGKTLLARAIA 302
Cdd:COG0466   356 CLVGPPGVGKTSLGKSIA 373
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
278-302 9.95e-03

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 38.73  E-value: 9.95e-03
                          10        20
                  ....*....|....*....|....*..
gi 1831511375 278 GRLPKG--VLLVGPPGTGKTLLARAIA 302
Cdd:COG3598     8 GLLPEGgvTLLAGPPGTGKSFLALQLA 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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