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Conserved domains on  [gi|818302953|gb|KKP87263|]
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ATP-dependent zinc metalloprotease FtsH [candidate division CPR3 bacterium GW2011_GWE2_35_7]

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];
35-619 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 947.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  35 LAVIGLYVFYTFFTPSNLfEKEVPLTEIAQDIKDNKVEKVFVTSEKLTVNYKDGQQK--ISRISGQDGVIEAFKNlgvdp 112
Cdd:COG0465    1 IALLLVLLFNLFSSSSSS-VKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTrfTTYRVNDPELVDLLEE----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 113 SKIEIKFENTSTSSFWVNLIAQFFPVLLMIVFFFIIMRQAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAKKEL 192
Cdd:COG0465   75 KGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 193 QEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNA 272
Cdd:COG0465  155 QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 273 PAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINYPDM 352
Cdd:COG0465  235 PCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 353 EGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKK-RLQT 431
Cdd:COG0465  315 KGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKsRVIS 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 432 EEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFNEQT 511
Cdd:COG0465  395 EKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 512 VGASSDIETATGIAREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKEILIK 590
Cdd:COG0465  475 TGASNDLERATKIARAMVTEYGMSeKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTE 554
                        570       580
                 ....*....|....*....|....*....
gi 818302953 591 NRNKLDLLAQKLMKQETVESEEFEKLMQQ 619
Cdd:COG0465  555 NRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
35-619 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 947.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  35 LAVIGLYVFYTFFTPSNLfEKEVPLTEIAQDIKDNKVEKVFVTSEKLTVNYKDGQQK--ISRISGQDGVIEAFKNlgvdp 112
Cdd:COG0465    1 IALLLVLLFNLFSSSSSS-VKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTrfTTYRVNDPELVDLLEE----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 113 SKIEIKFENTSTSSFWVNLIAQFFPVLLMIVFFFIIMRQAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAKKEL 192
Cdd:COG0465   75 KGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 193 QEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNA 272
Cdd:COG0465  155 QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 273 PAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINYPDM 352
Cdd:COG0465  235 PCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 353 EGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKK-RLQT 431
Cdd:COG0465  315 KGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKsRVIS 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 432 EEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFNEQT 511
Cdd:COG0465  395 EKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 512 VGASSDIETATGIAREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKEILIK 590
Cdd:COG0465  475 TGASNDLERATKIARAMVTEYGMSeKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTE 554
                        570       580
                 ....*....|....*....|....*....
gi 818302953 591 NRNKLDLLAQKLMKQETVESEEFEKLMQQ 619
Cdd:COG0465  555 NRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
127-617 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: 756.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  127 FWVNLIAQFFPVLLMIVF-FFIIMRQAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAKKELQEVVEFLKYPKKF 205
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGvWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  206 TSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNAPAILFIDELDAIG 285
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  286 RQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKK 365
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  366 KPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKK-RLQTEEDREIIAYHESG 444
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKsRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  445 HAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFNEQTVGASSDIETATGI 524
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  525 AREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKEILIKNRNKLDLLAQKLM 603
Cdd:TIGR01241 401 ARAMVTEWGMSdKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....
gi 818302953  604 KQETVESEEFEKLM 617
Cdd:TIGR01241 481 EKETITREEIKELL 494
ftsH CHL00176
cell division protein; Validated
114-619 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 608.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 114 KIEIKFENTSTSSFWVNLIAQ-FFPVLLMIVFFFIIMR---QAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAK 189
Cdd:CHL00176 113 NIDFDAHPPVLKSNIVTILSNlLLPLILIGVLWFFFQRssnFKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAK 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 190 KELQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAK 269
Cdd:CHL00176 193 EEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAK 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 270 KNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINY 349
Cdd:CHL00176 273 ENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSL 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 350 PDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKKRL 429
Cdd:CHL00176 353 PDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPL 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 430 QTEEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFN- 508
Cdd:CHL00176 433 EDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGs 512
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 509 -EQTVGASSDIETATGIAREMVCRYGMSTLGPIML-GEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKE 586
Cdd:CHL00176 513 tEVTTGASNDLQQVTNLARQMVTRFGMSSIGPISLeSNNSTDPFLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQ 592
                        490       500       510
                 ....*....|....*....|....*....|...
gi 818302953 587 ILIKNRNKLDLLAQKLMKQETVESEEFEKLMQQ 619
Cdd:CHL00176 593 ILKDNRVLIDLLVELLLQKETIDGDEFREIVNS 625
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
177-347 1.81e-120

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: 354.62  E-value: 1.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 177 VTFNDAAGVEEAKKELQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGV 256
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 257 GASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALM 336
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 818302953 337 RPGRFDRRVVI 347
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
428-616 2.30e-74

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 236.34  E-value: 2.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  428 RLQTEEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVF 507
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  508 NEQTVGASSDIETATGIAREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKE 586
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSdKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 818302953  587 ILIKNRNKLDLLAQKLMKQETVESEEFEKL 616
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
213-351 1.83e-18

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: 82.42  E-value: 1.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953   213 PRGVLLVGAPGTGKTLLARAVAGEA---GVPFFSIAGSEFME--------------MLVGVGASRVRDLFGEAKKNAPAI 275
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302953   276 LFIDELDAIGRQRGagiggghdEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPgRFDRRVVINYPD 351
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
35-619 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 947.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  35 LAVIGLYVFYTFFTPSNLfEKEVPLTEIAQDIKDNKVEKVFVTSEKLTVNYKDGQQK--ISRISGQDGVIEAFKNlgvdp 112
Cdd:COG0465    1 IALLLVLLFNLFSSSSSS-VKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTrfTTYRVNDPELVDLLEE----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 113 SKIEIKFENTSTSSFWVNLIAQFFPVLLMIVFFFIIMRQAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAKKEL 192
Cdd:COG0465   75 KGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 193 QEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNA 272
Cdd:COG0465  155 QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 273 PAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINYPDM 352
Cdd:COG0465  235 PCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 353 EGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKK-RLQT 431
Cdd:COG0465  315 KGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKsRVIS 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 432 EEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFNEQT 511
Cdd:COG0465  395 EKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 512 VGASSDIETATGIAREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKEILIK 590
Cdd:COG0465  475 TGASNDLERATKIARAMVTEYGMSeKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTE 554
                        570       580
                 ....*....|....*....|....*....
gi 818302953 591 NRNKLDLLAQKLMKQETVESEEFEKLMQQ 619
Cdd:COG0465  555 NRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
127-617 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: 756.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  127 FWVNLIAQFFPVLLMIVF-FFIIMRQAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAKKELQEVVEFLKYPKKF 205
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGvWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  206 TSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNAPAILFIDELDAIG 285
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  286 RQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKK 365
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  366 KPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKK-RLQTEEDREIIAYHESG 444
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKsRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  445 HAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFNEQTVGASSDIETATGI 524
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  525 AREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKEILIKNRNKLDLLAQKLM 603
Cdd:TIGR01241 401 ARAMVTEWGMSdKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....
gi 818302953  604 KQETVESEEFEKLM 617
Cdd:TIGR01241 481 EKETITREEIKELL 494
ftsH CHL00176
cell division protein; Validated
114-619 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 608.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 114 KIEIKFENTSTSSFWVNLIAQ-FFPVLLMIVFFFIIMR---QAQSSGSNILSFGKSKAKLFTKDKTRVTFNDAAGVEEAK 189
Cdd:CHL00176 113 NIDFDAHPPVLKSNIVTILSNlLLPLILIGVLWFFFQRssnFKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAK 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 190 KELQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAK 269
Cdd:CHL00176 193 EEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAK 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 270 KNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINY 349
Cdd:CHL00176 273 ENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSL 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 350 PDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKKRL 429
Cdd:CHL00176 353 PDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPL 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 430 QTEEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFN- 508
Cdd:CHL00176 433 EDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGs 512
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 509 -EQTVGASSDIETATGIAREMVCRYGMSTLGPIML-GEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKE 586
Cdd:CHL00176 513 tEVTTGASNDLQQVTNLARQMVTRFGMSSIGPISLeSNNSTDPFLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQ 592
                        490       500       510
                 ....*....|....*....|....*....|...
gi 818302953 587 ILIKNRNKLDLLAQKLMKQETVESEEFEKLMQQ 619
Cdd:CHL00176 593 ILKDNRVLIDLLVELLLQKETIDGDEFREIVNS 625
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
35-619 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 576.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  35 LAVIGLYVFYTFfTPSNLFEKEVPLTEIAQDIKDNKVEKVFVTSEKLTVNYKDGQQKISRISGQD-GVIEAFKNlgvdpS 113
Cdd:PRK10733  11 IAVVLMSVFQSF-GPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPVNDpKLLDNLLT-----K 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 114 KIEIKFENTSTSSFWVNLIAQFFPVLLMIVFFFIIMRQAQSSGSN-ILSFGKSKAKLFTKDKTRVTFNDAAGVEEAKKEL 192
Cdd:PRK10733  85 NVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKgAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 193 QEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNA 272
Cdd:PRK10733 165 AELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 273 PAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVINYPDM 352
Cdd:PRK10733 245 PCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 353 EGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAATKVKLGPEKKRL-QT 431
Cdd:PRK10733 325 RGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMvMT 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 432 EEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVFNEQT 511
Cdd:PRK10733 405 EAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEH 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 512 V--GASSDIETATGIAREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKEIL 588
Cdd:PRK10733 485 VstGASNDIKVATNLARNMVTQWGFSeKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLL 564
                        570       580       590
                 ....*....|....*....|....*....|.
gi 818302953 589 IKNRNKLDLLAQKLMKQETVESEEFEKLMQQ 619
Cdd:PRK10733 565 TDNMDILHAMKDALMKYETIDAPQIDDLMAR 595
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
177-347 1.81e-120

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: 354.62  E-value: 1.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 177 VTFNDAAGVEEAKKELQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGV 256
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 257 GASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALM 336
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 818302953 337 RPGRFDRRVVI 347
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
173-428 4.88e-109

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 331.59  E-value: 4.88e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 173 DKTRVTFNDAAGVEEAKKELQEVVE-FLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFME 251
Cdd:COG1222   71 ESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 252 MLVGVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGhdEREQTLNQILVEMDGFDQTVNVIVIAATNRPDIL 331
Cdd:COG1222  151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 332 DPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAA 411
Cdd:COG1222  229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTME 308
                        250
                 ....*....|....*..
gi 818302953 412 DIEEAATKVKLGPEKKR 428
Cdd:COG1222  309 DLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
173-433 4.51e-88

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 279.41  E-value: 4.51e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 173 DKTRVTFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFME 251
Cdd:PRK03992 124 ESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQ 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 252 MLVGVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDIL 331
Cdd:PRK03992 204 KFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 332 DPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAA 411
Cdd:PRK03992 284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTME 363
                        250       260
                 ....*....|....*....|..
gi 818302953 412 DIEEAATKVKLGPEKKRLQTEE 433
Cdd:PRK03992 364 DFLKAIEKVMGKEEKDSMEEPG 385
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
179-422 1.62e-82

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: 265.24  E-value: 1.62e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 179 FNDAAGVEEAKKELQEVVE-FLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVG 257
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 258 ASRVRDLFGEAKKNAPAILFIDELDAIGRQRGaGIGGGHDEREqtLNQILVEMDGFDQtvNVIVIAATNRPDILDPALMR 337
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELRS--DVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 338 pgRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAA 417
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ....*
gi 818302953 418 TKVKL 422
Cdd:COG0464  389 EREDI 393
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
173-421 1.00e-79

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: 257.03  E-value: 1.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  173 DKTRVTFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFME 251
Cdd:TIGR01242 115 ERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  252 MLVGVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDIL 331
Cdd:TIGR01242 195 KYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDIL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  332 DPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAA 411
Cdd:TIGR01242 275 DPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMD 354
                         250
                  ....*....|
gi 818302953  412 DIEEAATKVK 421
Cdd:TIGR01242 355 DFIKAVEKVL 364
Peptidase_M41 pfam01434
Peptidase family M41;
428-616 2.30e-74

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 236.34  E-value: 2.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  428 RLQTEEDREIIAYHESGHAVTTYFLPQTDPVHRISIVSRGLALGYTMTPPQTDRYNENKTRLLNQIATLLGGRAAEEIVF 507
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  508 NEQTVGASSDIETATGIAREMVCRYGMS-TLGPIMLGEKEELIFLSRDLHEKRNYSEEFASKIDVEIEKIINQSYNKAKE 586
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSdKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 818302953  587 ILIKNRNKLDLLAQKLMKQETVESEEFEKL 616
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
177-442 2.05e-73

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: 250.21  E-value: 2.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  177 VTFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVG 255
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  256 VGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEReqTLNQILVEMDGFDQTVNVIVIAATNRPDILDPAL 335
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPAL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  336 MRPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILA-----ASQGKNKINA 410
Cdd:TIGR01243 608 LRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAAlresiGSPAKEKLEV 687
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 818302953  411 ADiEEAATKVKLGPEK-----KRLQTEEDREIIAYHE 442
Cdd:TIGR01243 688 GE-EEFLKDLKVEMRHflealKKVKPSVSKEDMLRYE 723
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
176-400 1.24e-67

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: 234.80  E-value: 1.24e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  176 RVTFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLV 254
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  255 GVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGgghDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPA 334
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302953  335 LMRPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILA 400
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAA 396
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
178-345 2.19e-65

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 212.20  E-value: 2.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 178 TFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGV 256
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 257 GASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALM 336
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*....
gi 818302953 337 RPGRFDRRV 345
Cdd:cd19502  161 RPGRFDRKI 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
188-347 1.65e-62

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: 204.05  E-value: 1.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 188 AKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFG 266
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 267 EAKKNAPAILFIDELDAIGRQRGAGIGGGHDEReqTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVV 346
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 818302953 347 I 347
Cdd:cd19511  159 V 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
173-416 3.33e-62

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 211.55  E-value: 3.33e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 173 DKTRVTFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFME 251
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 252 MLVGVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDIL 331
Cdd:PTZ00454 218 KYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 332 DPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAA 411
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPK 377

                 ....*
gi 818302953 412 DIEEA 416
Cdd:PTZ00454 378 DFEKG 382
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
179-421 4.41e-62

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 206.27  E-value: 4.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 179 FNDAAGVEEAKKELQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGA 258
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 259 SRVRDLFGEAkKNAPAILFIDELDAIGRQRGAgiGGGHDEREQTLNQILVEMDGFDQtvNVIVIAATNRPDILDPALMRp 338
Cdd:COG1223   81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 339 gRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEAAT 418
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 ...
gi 818302953 419 KVK 421
Cdd:COG1223  234 QRK 236
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
181-347 1.15e-61

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: 202.14  E-value: 1.15e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGAS 259
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 260 RVRDLFGEAKKNAPAILFIDELDAIGRQRGAgiggGHDEREQTL-NQILVEMDGFDQTVNVIVIAATNRPDILDPALMRP 338
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 818302953 339 GRFDRRVVI 347
Cdd:cd19503  157 GRFDREVEI 165
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
178-420 9.89e-61

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 208.86  E-value: 9.89e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 178 TFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGV 256
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 257 GASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALM 336
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 337 RPGRFDRRVVINYPDMEGRKGIIKIHMKKKPITEDVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEEA 416
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                 ....
gi 818302953 417 ATKV 420
Cdd:PTZ00361 421 KEKV 424
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
188-345 3.33e-60

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: 197.89  E-value: 3.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 188 AKKELQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGE 267
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818302953 268 AKKNAPAILFIDELDAIGRQRGAgiGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRV 345
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
189-347 4.88e-57

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: 189.64  E-value: 4.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 189 KKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGE 267
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 268 AKKNAPAILFIDELDAIGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVI 347
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
188-347 1.48e-55

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 185.78  E-value: 1.48e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 188 AKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFG 266
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 267 EAKKNAPAILFIDELDAIGRQRGAGIGGGHDEReqTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVV 346
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 818302953 347 I 347
Cdd:cd19529  159 I 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
181-347 1.00e-53

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 181.10  E-value: 1.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGAS 259
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 260 RVRDLFGEAKKNAPAILFIDELDAIGRQRGAgiggGHDEREQTL-NQILVEMDGFDQTVNVIVIAATNRPDILDPALMRP 338
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                 ....*....
gi 818302953 339 GRFDRRVVI 347
Cdd:cd19519  157 GRFDREIDI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
216-349 2.44e-51

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: 173.55  E-value: 2.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  216 VLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGagiGGG 295
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 818302953  296 HDEREQTLNQILVEMDGFDQTV-NVIVIAATNRPDILDPALMrpGRFDRRVVINY 349
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
185-347 1.51e-47

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: 164.20  E-value: 1.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 185 VEEAKKELQ-EVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRD 263
Cdd:cd19530    1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 264 LFGEAKKNAPAILFIDELDAIGRQRGagiGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDR 343
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                 ....
gi 818302953 344 RVVI 347
Cdd:cd19530  158 TLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
181-347 2.39e-47

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 164.11  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQEVVEFLKYPKK-FTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGAS 259
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 260 RVRDLFGEAKKNAPAILFIDELDAIGRQRGagiGGGHDEREQTLNQILVEMDGF----DQTVNVIVIAATNRPDILDPAL 335
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|..
gi 818302953 336 MRPGRFDRRVVI 347
Cdd:cd19518  158 RRAGRFDREICL 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
188-345 4.28e-45

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 157.59  E-value: 4.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 188 AKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFG 266
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 267 EAKKNAPAILFIDELDAIGRQRgagiggGHDER---EQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDR 343
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKR------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154

                 ..
gi 818302953 344 RV 345
Cdd:cd19526  155 LV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
189-343 1.15e-40

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: 145.73  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 189 KKELQEVVEF-LKYPKKFtSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRVRDLFGE 267
Cdd:cd19527    2 KKEILDTIQLpLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818302953 268 AKKNAPAILFIDELDAIGRQRGA-GIGGGHDEReqTLNQILVEMDGFDQTV-NVIVIAATNRPDILDPALMRPGRFDR 343
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
183-347 7.83e-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: 143.26  E-value: 7.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 183 AGVEEAKKELQEVVEF-LKYPKKFtSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGASRV 261
Cdd:cd19509    2 AGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 262 RDLFGEAKKNAPAILFIDELDAIGRQRGAgigGGHDEREQTLNQILVEMDGFDQTVN--VIVIAATNRPDILDPALMRpg 339
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR-- 155

                 ....*...
gi 818302953 340 RFDRRVVI 347
Cdd:cd19509  156 RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
181-343 3.40e-37

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: 136.49  E-value: 3.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAG-----VPFFSIAGSEFMEMLV 254
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 255 GVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAgiggghdEREQTLNQI----LVEMDGFDQTVNVIVIAATNRPDI 330
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIHASIvstlLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|...
gi 818302953 331 LDPALMRPGRFDR 343
Cdd:cd19517  154 LDPALRRPGRFDR 166
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
177-347 9.26e-35

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: 130.11  E-value: 9.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 177 VTFNDAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKiPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVG 255
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 256 VGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAgigGGHDEREQTLNQILVEMDGFDQTVN--VIVIAATNRPDILDP 333
Cdd:cd19525   98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 174
                        170
                 ....*....|....
gi 818302953 334 ALMRpgRFDRRVVI 347
Cdd:cd19525  175 AARR--RLVKRLYI 186
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
174-347 1.42e-34

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 129.21  E-value: 1.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 174 KTRVTFNDAAGVEEAKKELQEVVEF-LKYPKKFTslGAKIP-RGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFME 251
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 252 MLVGVGASRVRDLFGEAKKNAPAILFIDELDAIGRQRGAgigGGHDEREQTLNQILVEMDGF-DQTVNVIVIAATNRPDI 330
Cdd:cd19521   79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQ 155
                        170
                 ....*....|....*..
gi 818302953 331 LDPALMRpgRFDRRVVI 347
Cdd:cd19521  156 LDSAIRR--RFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
181-347 2.50e-32

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 122.79  E-value: 2.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQE-VVEFLKYPKKFTslGAKIP-RGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGA 258
Cdd:cd19522    1 DIADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 259 SRVRDLFGEAKKNAPAILFIDELDAIGRQRGAgiGGGHDEREQTLNQILVEMDGF-------DQTVNVIVIAATNRPDIL 331
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 818302953 332 DPALMRpgRFDRRVVI 347
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
181-341 1.29e-30

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: 117.91  E-value: 1.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQEVVEF-LKYPKKFTSLG-AKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGA 258
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 259 SRVRDLFGEAKKNAPAILFIDELDAIGRQRGAgigGGHDEREQTLNQILVEMDGF--DQTVNVIVIAATNRPDILDPALM 336
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAIL 157

                 ....*..
gi 818302953 337 R--PGRF 341
Cdd:cd19520  158 RrmPKRF 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
181-347 1.46e-30

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: 117.64  E-value: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQEVVEF-LKYPKKFTSLGAKiPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGAS 259
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 260 RVRDLFGEAKKNAPAILFIDELDAIGRQRGAgigGGHDEREQTLNQILVEMDGFDQTVN--VIVIAATNRPDILDPALMR 337
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 818302953 338 pgRFDRRVVI 347
Cdd:cd19524  157 --RFTKRVYV 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
202-347 9.35e-29

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 112.97  E-value: 9.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 202 PKKFTSLGAKIPRGVLLVGAPGTGKTLLARAV-----AGEAGVpffsIAGSEFMEMLVGVGASRVRDLFGEAKKNAPA-- 274
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818302953 275 ------ILFIDELDAIGRQRGAGiGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRVVI 347
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
183-349 1.13e-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: 108.77  E-value: 1.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 183 AGVEEAKKELQEVVEflkypkkftslgAKIPRGVLLVGAPGTGKTLLARAVAGEA---GVPFFSIAGSEFMEMLVG---V 256
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 257 GASRVRDLFGEAKKNAPAILFIDELDAIGRqrgagiggghDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALM 336
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|...
gi 818302953 337 RPGRFDRRVVINY 349
Cdd:cd00009  139 LYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
175-403 1.05e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 110.88  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 175 TRVTFNDAAGVEEAKKELQEVVEflKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLV 254
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLKKRST--SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIV 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 255 GVGASRVRDLFGEAKKNAPAILFIDELD-AIGRQRGAGIGGghdereqTLNQILVEMDGF--DQTVNVIVIAATNRPDIL 331
Cdd:CHL00195 301 GESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLATFITWlsEKKSPVFVVATANNIDLL 373
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818302953 332 DPALMRPGRFDRRVVINYPDMEGRKGIIKIHMKK-KPIT-EDVNIDKLARRTVGFSGADLENMLNEAAILAASQ 403
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKfRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYE 447
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
181-343 1.41e-20

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: 88.96  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQevveflKYPKKFTS----LGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGV 256
Cdd:cd19507    1 DVGGLDNLKDWLK------KRKAAFSKqasaYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 257 GASRVRDLFGEAKKNAPAILFIDELD-AIGrqrGAGIGGGHDEREQTLNQILVEMDgfDQTVNVIVIAATNRPDILDPAL 335
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFS---NADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPEL 149

                 ....*...
gi 818302953 336 MRPGRFDR 343
Cdd:cd19507  150 LRKGRFDE 157
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
181-347 1.77e-19

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: 85.71  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 181 DAAGVEEAKKELQ-EVVEFLKYPKKFTSLgAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVGAS 259
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 260 RVRDLFGEAKKNAPAILFIDELDAI--GRQRGAGIGGghdeREQTlnQILVEMDGF-----DQtvnVIVIAATNRPDILD 332
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVlgsgeDG---VLVVCTTSKPEEID 150
                        170
                 ....*....|....*
gi 818302953 333 PALMRpgRFDRRVVI 347
Cdd:cd19523  151 ESLRR--YFSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
213-351 1.83e-18

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: 82.42  E-value: 1.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953   213 PRGVLLVGAPGTGKTLLARAVAGEA---GVPFFSIAGSEFME--------------MLVGVGASRVRDLFGEAKKNAPAI 275
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818302953   276 LFIDELDAIGRQRGagiggghdEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPgRFDRRVVINYPD 351
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
192-345 1.34e-15

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: 74.31  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 192 LQEVVEFLKYPKKFTSLGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEfmemlVGVGASRVRDLFGEAKKN 271
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818302953 272 ApaILFIDELDA---IGRQRGAGIGGGHDEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDRRV 345
Cdd:cd19510   77 S--IILLEDIDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
371-415 1.68e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 62.17  E-value: 1.68e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 818302953  371 DVNIDKLARRTVGFSGADLENMLNEAAILAASQGKNKINAADIEE 415
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
214-345 4.59e-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: 61.39  E-value: 4.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 214 RGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMlvGV-GASRVRDLFGEAKK-NAPAILFIDELDAIGRQRgAG 291
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-ST 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 818302953 292 IGGGHDEReQTLNQILVEMDgfDQTVNVIVIAATNRPDILDPALMrpGRFDRRV 345
Cdd:cd19512  100 EKISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAIN--DRIDEMV 148
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
215-341 3.74e-10

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 58.07  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  215 GVLLVGAPGTGKTLLARAVAgEA--GVPFFSIAGSEFME-------MLVGVGASRVRDlfGEAKKNA--PAILFIDELDA 283
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVD--GPLVRAAreGEIAVLDEINR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818302953  284 IgrqrgagigggHDEREQTLNQILVE-----MDGFDQTV----NVIVIAATNRPDI----LDPALMRpgRF 341
Cdd:pfam07728  78 A-----------NPDVLNSLLSLLDErrlllPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS--RF 135
PRK04195 PRK04195
replication factor C large subunit; Provisional
178-419 6.02e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 61.86  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 178 TFNDAAGVEEAKKELQEVVEflKYPKKftslgaKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEF-----MEM 252
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE--SWLKG------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 253 LVGvGASRVRDLFGEAKKnapaILFIDELDaigrqrgaGIGGGHDE---REqtLNQILvemdgfDQTVNVIVIAAtNrpD 329
Cdd:PRK04195  84 VAG-EAATSGSLFGARRK----LILLDEVD--------GIHGNEDRggaRA--ILELI------KKAKQPIILTA-N--D 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 330 ILDPALmRPGRfDRRVVINYPDMEGR---KGIIKIHMKKKPITEDVNIDKLARRtvgfSGADLE---NMLNeaailAASQ 403
Cdd:PRK04195 140 PYDPSL-RELR-NACLMIEFKRLSTRsivPVLKRICRKEGIECDDEALKEIAER----SGGDLRsaiNDLQ-----AIAE 208
                        250
                 ....*....|....*.
gi 818302953 404 GKNKINAADIEEAATK 419
Cdd:PRK04195 209 GYGKLTLEDVKTLGRR 224
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
208-343 6.84e-10

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: 58.16  E-value: 6.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 208 LGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFM--------------EMLVGVGASRVRDLFGEAKKNAP 273
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818302953 274 AILFID---ELDaIGRQrgagiggGHDEREQT------LNQILVEMDGFDQTVNVIVIAATNRPDILDPALMRPGRFDR 343
Cdd:cd19505   87 CIIWIPnihELN-VNRS-------TQNLEEDPklllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
212-345 1.65e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 54.69  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 212 IPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEmlVG-VG---ASRVRDLfgeakknAPAILFIDELDAIGRQ 287
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE--VGyVGrdvESIIRDL-------VEGIVFIDEIDKIAKR 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818302953 288 RGagiGGGHD-EREQTLNQILVEMDGfdQTVN----------VIVIAA----TNRPDILDPALMrpGRFDRRV 345
Cdd:cd19498  116 GG---SSGPDvSREGVQRDLLPIVEG--STVStkygpvktdhILFIAAgafhVAKPSDLIPELQ--GRFPIRV 181
ycf2 CHL00206
Ycf2; Provisional
208-463 2.12e-08

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 57.61  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  208 LGAKIPRGVLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEF-------------------------------------- 249
Cdd:CHL00206 1625 LALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFldnkpkgfliddididdsddiddsddidrdldtelltm 1704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  250 -----MEMLVGVGASRVRDLFGEAKKNAPAILFID---ELDAigrqrgagigggHDEREQTLNQiLVEMDGFD----QTV 317
Cdd:CHL00206 1705 mnaltMDMMPKIDRFYITLQFELAKAMSPCIIWIPnihDLNV------------NESNYLSLGL-LVNSLSRDcercSTR 1771
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  318 NVIVIAATNRPDILDPALMRPGRFD-----RRVVI-----NYPDMEGRKGiikIHMKKKPItedvNIDKLARRTVGFSGA 387
Cdd:CHL00206 1772 NILVIASTHIPQKVDPALIAPNKLNtcikiRRLLIpqqrkHFFTLSYTRG---FHLEKKMF----HTNGFGSITMGSNAR 1844
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818302953  388 DLENMLNEAAILAASQGKNKINAADIEEAATKV--KLGPEKKRLQteeDREIIAYhESGHAVTTYFLPQTDPVHRISI 463
Cdd:CHL00206 1845 DLVALTNEALSISITQKKSIIDTNTIRSALHRQtwDLRSQVRSVQ---DHGILFY-QIGRAVAQNVLLSNCPIDPISI 1918
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
214-250 1.43e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.12  E-value: 1.43e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 818302953 214 RGVLLVGAPGTGKTLLARAVAGEAG--VPFFSIAGSEFM 250
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEIY 103
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
216-280 1.51e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.82  E-value: 1.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 216 VLLVGAPGTGKTLLARAVAGEAGVPFFSI-AgsefmemlVGVGASRVRDLFGEAKKNA----PAILFIDE 280
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALsA--------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
180-286 4.13e-06

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: 47.55  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 180 NDAAGVEEAKkelQEVVEFLKYPKKFTSLGAKIprgVLLVGAPGTGKTLLARAVAGEAGVPF--FSIAGSEFMEMLVG-- 255
Cdd:cd19500   10 ADHYGLEDVK---ERILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGVRDEAEIRGhr 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 818302953 256 ---VGA--SRVRDLFGEAKKNAPAILfIDELDAIGR 286
Cdd:cd19500   84 rtyVGAmpGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
216-280 4.15e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 4.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818302953 216 VLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFmemlvgvGASRVRDLFGEAKKNAPA----ILFIDE 280
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRSAgrrtILFIDE 100
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
214-249 4.54e-06

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: 49.23  E-value: 4.54e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 818302953  214 RGVLLVGAPGTGKTLLARAVAGEAG--VPFFSIAGSEF 249
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
216-362 3.00e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.31  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 216 VLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEfmEMLVGvgasrvrDLFGE----AKKNAP---------AILFIDELD 282
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFTP--DLLPS-------DILGTyiydQQTGEFefrpgplfaNVLLADEIN 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 283 -AigrqrgagiggghdeREQTLNQILVEMDgfDQTVNV-----------IVIAATNRPDI-----LDPALMRpgRFDRRV 345
Cdd:COG0714  105 rA---------------PPKTQSALLEAME--ERQVTIpggtyklpepfLVIATQNPIEQegtypLPEAQLD--RFLLKL 165
                        170
                 ....*....|....*..
gi 818302953 346 VINYPDMEGRKGIIKIH 362
Cdd:COG0714  166 YIGYPDAEEEREILRRH 182
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
193-334 3.27e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 47.11  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 193 QEVVEFLKYPKKFTSLGAKIPRgVLLVGAPGTGKTLLARAVA---------GEAGVPFF----SIAGS----EFMEMLVG 255
Cdd:COG5635  161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrDLAEEasleDLLAEALE 239
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818302953 256 VGASRVRDLFGEAKKNAPAILFIDELDAIGRQrgagiggghDEREQTLNQILVEMDGFDQtVNVIViaaTNRPDILDPA 334
Cdd:COG5635  240 KRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPK-ARVII---TSRPEGYDSS 305
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
213-322 2.64e-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: 42.11  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  213 PRGVLLVGAPGTGKTLLARAV---AGEAGVPFFSIAGSEFMEMLVGVGA----SRVRDLFGEAkKNAPAILFIDELDAIG 285
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEAltreGLLRQLLDEL-ESSLLEAWRAALLEAL 102
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 818302953  286 RQRGAGIGGGHDEREQTLNQILVEMDGFDQTVnVIVI 322
Cdd:pfam13191 103 APVPELPGDLAERLLDLLLRLLDLLARGERPL-VLVL 138
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
216-326 3.34e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 41.80  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  216 VLLVGAPGTGKTLLARAVAGEAGV---PFFSIAGSEFME-----MLVG-----VGASRVRDLFGEAKKNAPAILFIDELD 282
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 818302953  283 AIgrqrgagigggHDEREQTLNQIL---VEMDGFDQTV---NVIVIAATN 326
Cdd:pfam07724  86 KA-----------HPGVQNDLLQILeggTLTDKQGRTVdfkNTLFIMTGN 124
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
214-335 4.92e-04

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 41.66  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 214 RGVLLVGAPGTGKTLLARAVAGEAGVPF-FSIAGSEFMEMlvgVGASRVRDLFGEAKKNApAILF--------------- 277
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEI---NSHSLFSKWFSESGKLV-TKMFqkiqeliddkdalvf 128
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818302953 278 --IDELDAIGRQRGAGIGGGH-DEREQTLNQILVEMDGFDQTVNVIVIAATNRPDILDPAL 335
Cdd:cd19508  129 vlIDEVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
216-332 5.48e-04

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: 40.18  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 216 VLLVGAPGTGKTLLARAVAGEA---GVPFFSIAgseFMEMLVgvgaSRVRDLfgeAKKNAPAILFIDELDAIGRQRGAgi 292
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDL---IEEKKLDIIIIDSLSSLARASQG-- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 818302953 293 ggghDEREQTLNQILVEMDGFDQTvNVIVIAATNRPDILD 332
Cdd:cd01120   69 ----DRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDI 103
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
178-280 2.53e-03

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: 39.02  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953  178 TFNDAAGVEEAKKELQEVVEflkypkkftslGAKIpRG-----VLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFmem 252
Cdd:pfam05496   5 TLDEYIGQEKVKENLKIFIE-----------AAKQ-RGealdhVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI--- 69
                          90       100
                  ....*....|....*....|....*....
gi 818302953  253 lvgvgaSRVRDLFGEAKKNAPA-ILFIDE 280
Cdd:pfam05496  70 ------ERPGDLAAILTNLEPGdVLFIDE 92
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
211-348 2.57e-03

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: 38.77  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 211 KIPRG--VLLVGAPGTGKTLLARAVAGEAGVPFFSIA--GSEFMEMLVGVGASRVRDLF----GEAKK--------NAPA 274
Cdd:cd00267   21 TLKAGeiVALVGPNGSGKSTLLRAIAGLLKPTSGEILidGKDIAKLPLEELRRRIGYVPqlsgGQRQRvalarallLNPD 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818302953 275 ILFIDE----LDAIGRQRgagiggghdeREQTLNQILVEmdgfdqtvNVIVIAATNRPDILDPAlmrpgrFDRRVVIN 348
Cdd:cd00267  101 LLLLDEptsgLDPASRER----------LLELLRELAEE--------GRTVIIVTHDPELAELA------ADRVIVLK 154
AAA_28 pfam13521
AAA domain;
216-257 3.87e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 38.40  E-value: 3.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 818302953  216 VLLVGAPGTGKTLLARAVAGEAGVPFFSIAGSEFMEMLVGVG 257
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALAARFGYPVVPEAAREILEELGADG 43
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
213-342 3.98e-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: 38.70  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 213 PRGVLL-VGAPGTGKTLLARAVAGE---AGVPFFSIAGSEFMEM-----LVG-----VGASRVRDLFGEAKKNAPAILFI 278
Cdd:cd19499   40 PIGSFLfLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKhsvsrLIGappgyVGYTEGGQLTEAVRRKPYSVVLL 119
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818302953 279 DELDAigrqrgagiggGHDEREQTLNQILVE---MDGFDQTV---NVIVIAATN--RPDILdpalmrpGRFD 342
Cdd:cd19499  120 DEIEK-----------AHPDVQNLLLQVLDDgrlTDSHGRTVdfkNTIIIMTSNhfRPEFL-------NRID 173
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
203-367 4.61e-03

MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350658 [Multi-domain]  Cd Length: 311  Bit Score: 39.63  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 203 KKFTSLGAKIpRG---VLLVGAPGTGKTLLARAVAGEA-GVPFFSIAGSEfmemLVGVGASRVRDLFG-----EAKKNAP 273
Cdd:cd17706   29 QKILEDGTRI-RGdihILLVGDPGTAKSQILKYVLKIApRGVYTSGKGSS----GAGLTAAVVRDSETgewylEAGALVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 274 A---ILFIDELDAIGRQRGAGIgggHDEREQtlNQILVEMDGFDQTVN--VIVIAATN----RPDI---------LDPAL 335
Cdd:cd17706  104 AdggVCCIDEFDKMKELDRTAL---HEAMEQ--QTISIAKAGIVTTLNarCSILAAANpkggRYNPklspieninLPSPL 178
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 818302953 336 MRpgRFDR----RVVINYP-DMEGRKGIIKIHMKKKP 367
Cdd:cd17706  179 LS--RFDLifviRDDPDEErDEELAEHIIDLHRGSDP 213
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
184-286 5.76e-03

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 39.12  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818302953 184 GVEEAKKELQEVV----EFLKYPKKFTSLGAKIPRG-VLLVGAPGTGKTLLARAVAGEAGVPfFSIAGSEFMEMLVGVG- 257
Cdd:cd19497   16 GQERAKKVLSVAVynhyKRIRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVP-FAIADATTLTEAGYVGe 94
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 818302953 258 --ASRVRDLFGEAKKNAPA----ILFIDELDAIGR 286
Cdd:cd19497   95 dvENILLKLLQAADYDVERaqrgIVYIDEIDKIAR 129
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
216-292 5.98e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 37.67  E-value: 5.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818302953  216 VLLVGAPGTGKTLLARAVAGEAGVPFfsIAGSEFMEMLVGVGASRVRDLFgEAKKNAPAILFidELDAIGRQRGAGI 292
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVR--LSSDDERKRLFGEGRPSISYYT-DATDRTYERLH--ELARIALRAGRPV 73
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
216-235 8.29e-03

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: 39.25  E-value: 8.29e-03
                         10        20
                 ....*....|....*....|
gi 818302953 216 VLLVGAPGTGKTLLARAVAG 235
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
216-244 9.63e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 9.63e-03
                         10        20
                 ....*....|....*....|....*....
gi 818302953 216 VLLVGAPGTGKTLLARAVAGEAGVPFFSI 244
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
 
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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