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Conserved domains on  [gi|1080851426|gb|OFQ15109|]
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cell division protein FtsH [Streptococcus sp. HMSC076H07]

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];
17-624 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 905.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  17 ILLIIAVITTFQyylkGTSSQNQQISYTKLVKQLKAGEIKSISYQPSggvvEVSGTYKKAKTiksaNSFTflggsvatkv 96
Cdd:COG0465     2 ALLLVLLFNLFS----SSSSSVKEISYSEFLQLVEAGKVKSVTIQGD----RITGTLKDGTK----TRFT---------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  97 tgfnsVILPNDSSiksLVSAAEENNTNIQVKHESSSGTWISYIASFLPLVIMIGFFMMMMNQ-GGGARGAMSFGKNKARS 175
Cdd:COG0465    60 -----TYRVNDPE---LVDLLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRmQGGGGGAMSFGKSKAKL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 176 SSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 255
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 256 VEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSD 335
Cdd:COG0465   212 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPD 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 336 VLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVID 415
Cdd:COG0465   292 VLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVT 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 416 ASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDD 495
Cdd:COG0465   372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEE 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 496 MKEQLAGLMGGRVAEEIIFNAQTTGASNDFEQATAMARAMVTEYGMSEKLGPVQYE--GNHAMMAGQMSPEKSYSAQTAQ 573
Cdd:COG0465   452 LLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGesEGEVFLGRDIGQSRNYSEETAR 531
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080851426 574 LIDDEVRHLLNEARNKAADIINENRDTHKLIAEALLKYETLDAAQIKSIFE 624
Cdd:COG0465   532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
17-624 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 905.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  17 ILLIIAVITTFQyylkGTSSQNQQISYTKLVKQLKAGEIKSISYQPSggvvEVSGTYKKAKTiksaNSFTflggsvatkv 96
Cdd:COG0465     2 ALLLVLLFNLFS----SSSSSVKEISYSEFLQLVEAGKVKSVTIQGD----RITGTLKDGTK----TRFT---------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  97 tgfnsVILPNDSSiksLVSAAEENNTNIQVKHESSSGTWISYIASFLPLVIMIGFFMMMMNQ-GGGARGAMSFGKNKARS 175
Cdd:COG0465    60 -----TYRVNDPE---LVDLLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRmQGGGGGAMSFGKSKAKL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 176 SSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 255
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 256 VEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSD 335
Cdd:COG0465   212 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPD 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 336 VLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVID 415
Cdd:COG0465   292 VLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVT 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 416 ASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDD 495
Cdd:COG0465   372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEE 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 496 MKEQLAGLMGGRVAEEIIFNAQTTGASNDFEQATAMARAMVTEYGMSEKLGPVQYE--GNHAMMAGQMSPEKSYSAQTAQ 573
Cdd:COG0465   452 LLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGesEGEVFLGRDIGQSRNYSEETAR 531
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080851426 574 LIDDEVRHLLNEARNKAADIINENRDTHKLIAEALLKYETLDAAQIKSIFE 624
Cdd:COG0465   532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
134-624 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: 737.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 134 TWISYIASFLP--LVIMIGFFMMMMNQGGGARGAMSFGKNKARSSSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRY 211
Cdd:TIGR01241   1 SLLGFLFSLLPpiLLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 212 KSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVG 291
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 292 RRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKN 371
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 372 KPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAG 451
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 452 HTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIFNAQTTGASNDFEQATAM 531
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 532 ARAMVTEYGMSEKLGPVQY--EGNHAMMAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAADIINENRDTHKLIAEALL 609
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYgsDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1080851426 610 KYETLDAAQIKSIFE 624
Cdd:TIGR01241 481 EKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
158-622 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 554.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 158 QGGGARGAMSFGKNKARSSSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAK 237
Cdd:PRK10733  124 QGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 238 AVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMD 317
Cdd:PRK10733  204 AIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMD 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 318 GFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLEN 397
Cdd:PRK10733  284 GFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLAN 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 398 VLNEAALVAARRNKKVIDASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAG 477
Cdd:PRK10733  364 LVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRAL 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 478 GYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIFNAQ--TTGASNDFEQATAMARAMVTEYGMSEKLGPVQY--EGN 553
Cdd:PRK10733  444 GVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEhvSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYaeEEG 523
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080851426 554 HAMMAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAADIINENRDTHKLIAEALLKYETLDAAQIKSI 622
Cdd:PRK10733  524 EVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDL 592
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
183-353 9.20e-109

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: 325.34  E-value: 9.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 183 VRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 262
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 263 GASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALL 342
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1080851426 343 RPGRFDRKVLV 353
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
435-622 4.46e-87

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 270.24  E-value: 4.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 435 RTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIF 514
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 515 NAQTTGASNDFEQATAMARAMVTEYGMSEKLGPVQYE--GNHAMMAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAAD 592
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEesDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1080851426 593 IINENRDTHKLIAEALLKYETLDAAQIKSI 622
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
219-357 1.99e-17

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: 79.72  E-value: 1.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  219 PAGVLLEGPPGTGKTLLAKAVAGEA---GVPFFSISGSDFVE--------------MFVGVGASRVRSLFEDAKKAERAI 281
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080851426  282 IFIDEIDAVGRRRGagmgggndEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPgRFDRKVLVGQPD 357
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
17-624 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 905.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  17 ILLIIAVITTFQyylkGTSSQNQQISYTKLVKQLKAGEIKSISYQPSggvvEVSGTYKKAKTiksaNSFTflggsvatkv 96
Cdd:COG0465     2 ALLLVLLFNLFS----SSSSSVKEISYSEFLQLVEAGKVKSVTIQGD----RITGTLKDGTK----TRFT---------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  97 tgfnsVILPNDSSiksLVSAAEENNTNIQVKHESSSGTWISYIASFLPLVIMIGFFMMMMNQ-GGGARGAMSFGKNKARS 175
Cdd:COG0465    60 -----TYRVNDPE---LVDLLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRmQGGGGGAMSFGKSKAKL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 176 SSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 255
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 256 VEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSD 335
Cdd:COG0465   212 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPD 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 336 VLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVID 415
Cdd:COG0465   292 VLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVT 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 416 ASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDD 495
Cdd:COG0465   372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEE 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 496 MKEQLAGLMGGRVAEEIIFNAQTTGASNDFEQATAMARAMVTEYGMSEKLGPVQYE--GNHAMMAGQMSPEKSYSAQTAQ 573
Cdd:COG0465   452 LLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGesEGEVFLGRDIGQSRNYSEETAR 531
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080851426 574 LIDDEVRHLLNEARNKAADIINENRDTHKLIAEALLKYETLDAAQIKSIFE 624
Cdd:COG0465   532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
134-624 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: 737.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 134 TWISYIASFLP--LVIMIGFFMMMMNQGGGARGAMSFGKNKARSSSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRY 211
Cdd:TIGR01241   1 SLLGFLFSLLPpiLLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 212 KSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVG 291
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 292 RRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKN 371
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 372 KPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAG 451
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 452 HTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIFNAQTTGASNDFEQATAM 531
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 532 ARAMVTEYGMSEKLGPVQY--EGNHAMMAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAADIINENRDTHKLIAEALL 609
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYgsDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1080851426 610 KYETLDAAQIKSIFE 624
Cdd:TIGR01241 481 EKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
158-622 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 554.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 158 QGGGARGAMSFGKNKARSSSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAK 237
Cdd:PRK10733  124 QGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 238 AVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMD 317
Cdd:PRK10733  204 AIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMD 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 318 GFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLEN 397
Cdd:PRK10733  284 GFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLAN 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 398 VLNEAALVAARRNKKVIDASDIDEAEDRVIAGPSKKDRTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAG 477
Cdd:PRK10733  364 LVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRAL 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 478 GYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIFNAQ--TTGASNDFEQATAMARAMVTEYGMSEKLGPVQY--EGN 553
Cdd:PRK10733  444 GVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEhvSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYaeEEG 523
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080851426 554 HAMMAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAADIINENRDTHKLIAEALLKYETLDAAQIKSI 622
Cdd:PRK10733  524 EVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDL 592
ftsH CHL00176
cell division protein; Validated
10-632 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 554.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  10 LKNSFIYILLI------IAVITTFQYYLKG--------------TSSQNQQISYTKLVKQLKAGEIKSISYqpsggvvev 69
Cdd:CHL00176    1 MKEQSKYAILIslplivEKFTVWDVFYYSSvedglkspnnpdvvQNKASSRMTYGRFLEYLDMGWIKKVDL--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  70 sgtYKKAKTIKSANSFTFLGGSVATKvtgfnSVILPNDSSikSLVSAAEENNTNIQvKHESSSGTWISYIASFL--PL-- 145
Cdd:CHL00176   72 ---YDNGRTAIVEASSPELGNRPQRI-----RVELPVGAS--ELIQKLKEANIDFD-AHPPVLKSNIVTILSNLllPLil 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 146 --VIMIGFFMMMMNQGGGARGAMSFGKNKARSSSKDEVKVRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVL 223
Cdd:CHL00176  141 igVLWFFFQRSSNFKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 224 LEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGND 303
Cdd:CHL00176  221 LVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGND 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 304 EREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVV 383
Cdd:CHL00176  301 EREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELI 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 384 AQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDEAEDRVIAGPSKKDRTISeRERAMVAYHEAGHTIVGLILSNAR 463
Cdd:CHL00176  381 ARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHD 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 464 VVHKVTIVPRGRAGGYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIFNAQ--TTGASNDFEQATAMARAMVTEYGM 541
Cdd:CHL00176  460 PVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTevTTGASNDLQQVTNLARQMVTRFGM 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 542 SeKLGPVQYEGNHAM---MAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAADIINENRDTHKLIAEALLKYETLDAAQ 618
Cdd:CHL00176  540 S-SIGPISLESNNSTdpfLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDE 618
                         650
                  ....*....|....*
gi 1080851426 619 IKSIFET-GKMPETE 632
Cdd:CHL00176  619 FREIVNSyTILPPKK 633
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
183-353 9.20e-109

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: 325.34  E-value: 9.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 183 VRFSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 262
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 263 GASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALL 342
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1080851426 343 RPGRFDRKVLV 353
Cdd:cd19501   161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
175-435 2.21e-104

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 320.03  E-value: 2.21e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 175 SSSKDEVKVRFSDVAGAEEEKQELIEVV-DFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGS 253
Cdd:COG1222    67 AVPAESPDVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 254 DFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGggNDEREQTLNQLLIEMDGFEGNESIIVIAATNR 333
Cdd:COG1222   147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGT--SGEVQRTVNQLLAELDGFESRGDVLIIAATNR 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 334 SDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKV 413
Cdd:COG1222   225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304
                         250       260
                  ....*....|....*....|..
gi 1080851426 414 IDASDIDEAEDRVIAGPSKKDR 435
Cdd:COG1222   305 VTMEDLEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
182-446 2.34e-87

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 278.25  E-value: 2.34e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 182 KVRFSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 260
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 261 GVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPA 340
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 341 LLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDID 420
Cdd:PRK03992  287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFL 366
                         250       260
                  ....*....|....*....|....*.
gi 1080851426 421 EAEDRVIagpSKKDRTISERERAMVA 446
Cdd:PRK03992  367 KAIEKVM---GKEEKDSMEEPGVMFA 389
Peptidase_M41 pfam01434
Peptidase family M41;
435-622 4.46e-87

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 270.24  E-value: 4.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 435 RTISERERAMVAYHEAGHTIVGLILSNARVVHKVTIVPRGRAGGYMIALPKEDQMLLSKDDMKEQLAGLMGGRVAEEIIF 514
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 515 NAQTTGASNDFEQATAMARAMVTEYGMSEKLGPVQYE--GNHAMMAGQMSPEKSYSAQTAQLIDDEVRHLLNEARNKAAD 592
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEesDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1080851426 593 IINENRDTHKLIAEALLKYETLDAAQIKSI 622
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
184-422 5.02e-74

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: 243.66  E-value: 5.02e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 184 RFSDVAGAEEEKQELIEVVD-FLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 262
Cdd:COG0464   155 ILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 263 GASRVRSLFEDAKKAERAIIFIDEIDAVgrrrGAGMGGGNDEREQT-LNQLLIEMDGFEGNesIIVIAATNRSDVLDPAL 341
Cdd:COG0464   235 TEKNLREVFDKARGLAPCVLFIDEADAL----AGKRGEVGDGVGRRvVNTLLTEMEELRSD--VVVIAATNRPDLLDPAL 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 342 LRpgRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDE 421
Cdd:COG0464   309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLE 386

                  .
gi 1080851426 422 A 422
Cdd:COG0464   387 A 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
182-427 1.33e-73

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: 241.24  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 182 KVRFSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 260
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 261 GVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPA 340
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 341 LLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDID 420
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFI 357

                  ....*..
gi 1080851426 421 EAEDRVI 427
Cdd:TIGR01242 358 KAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
183-427 1.45e-68

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: 237.50  E-value: 1.45e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 183 VRFSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 261
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 262 VGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEReqTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPAL 341
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPAL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 342 LRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDE 421
Cdd:TIGR01243 608 LRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEV 687

                  ....*.
gi 1080851426 422 AEDRVI 427
Cdd:TIGR01243 688 GEEEFL 693
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
182-424 5.13e-62

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 219.78  E-value: 5.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 182 KVRFSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 260
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 261 GVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMgggNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPA 340
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT---GEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 341 LLRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRnkkVIDASDID 420
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR---FIREGKIN 407

                  ....*
gi 1080851426 421 -EAED 424
Cdd:TIGR01243 408 fEAEE 412
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
185-351 4.24e-59

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: 196.02  E-value: 4.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 185 FSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 263
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 264 ASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLR 343
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                  ....*...
gi 1080851426 344 PGRFDRKV 351
Cdd:cd19502   162 PGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
183-436 1.29e-56

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 196.91  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 183 VRFSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 261
Cdd:PTZ00454  142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 262 VGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPAL 341
Cdd:PTZ00454  222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 342 LRPGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDE 421
Cdd:PTZ00454  302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEK 381
                         250
                  ....*....|....*
gi 1080851426 422 AEDRVIagpSKKDRT 436
Cdd:PTZ00454  382 GYKTVV---RKTDRD 393
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
195-353 2.88e-55

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: 185.18  E-value: 2.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 195 KQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDA 274
Cdd:cd19481     2 KASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080851426 275 KKAERAIIFIDEIDAVgrRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLV 353
Cdd:cd19481    82 RRLAPCILFIDEIDAI--GRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
185-422 8.80e-54

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 184.32  E-value: 8.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 185 FSDVAGAEEEKQELIEVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 264
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 265 SRVRSLFEDAKKAeRAIIFIDEIDAVgrrrGAGMGGGNDERE--QTLNQLLIEMDGFegNESIIVIAATNRSDVLDPALL 342
Cdd:COG1223    81 RNLRKLFDFARRA-PCVIFFDEFDAI----AKDRGDQNDVGEvkRVVNALLQELDGL--PSGSVVIAATNHPELLDSALW 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 343 RpgRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDEA 422
Cdd:COG1223   154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
187-351 7.97e-53

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: 179.02  E-value: 7.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAS 265
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 266 RVRSLFEDAKKAERAIIFIDEIDAVgrrrgaGMGGGNDEREQ---TLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALL 342
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDAL------APKREEDQREVerrVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALR 154

                  ....*....
gi 1080851426 343 RPGRFDRKV 351
Cdd:cd19503   155 RPGRFDREV 163
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
195-353 9.59e-53

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: 178.63  E-value: 9.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 195 KQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFED 273
Cdd:cd19511     2 KRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 274 AKKAERAIIFIDEIDAVGRRRGAGMGGGNDEReqTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLV 353
Cdd:cd19511    82 ARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
185-427 1.79e-52

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 186.90  E-value: 1.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 185 FSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 263
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 264 ASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLR 343
Cdd:PTZ00361  262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 344 PGRFDRKVLVGQPDVKGREAILRVHAKNKPLADNVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDEAE 423
Cdd:PTZ00361  342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAK 421

                  ....
gi 1080851426 424 DRVI 427
Cdd:PTZ00361  422 EKVL 425
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
222-354 1.16e-48

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: 166.61  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVgrrRGAGMGGG 301
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL---AGSRGSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1080851426 302 NDEREQTLNQLLIEMDGFEGNES-IIVIAATNRSDVLDPALLrpGRFDRKVLVG 354
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
195-353 7.06e-48

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 165.36  E-value: 7.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 195 KQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFED 273
Cdd:cd19529     2 KQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 274 AKKAERAIIFIDEIDAVGRRRGAGMGGGNDEReqTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLV 353
Cdd:cd19529    82 ARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 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 ...
187-354 5.69e-47

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: 163.38  E-value: 5.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAS 265
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 266 RVRSLFEDAKKAERAIIFIDEIDAVgrrrGAGMGGGNDEREQTL-NQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRP 344
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAI----APKREKTHGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156
                         170
                  ....*....|
gi 1080851426 345 GRFDRKVLVG 354
Cdd:cd19519   157 GRFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
205-353 3.05e-45

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: 158.42  E-value: 3.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 205 LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFEDAKKAERAIIFI 284
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080851426 285 DEIDAVgrrRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLV 353
Cdd:cd19530    96 DEVDAL---VPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
195-353 1.86e-43

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: 153.43  E-value: 1.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 195 KQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFED 273
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 274 AKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLV 353
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
187-351 5.78e-41

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: 146.78  E-value: 5.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEVVDFLKDPKR-YKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAS 265
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 266 RVRSLFEDAKKAERAIIFIDEIDAVgrrRGAGMGGGNDEREQTLNQLLIEMDGFEGNES----IIVIAATNRSDVLDPAL 341
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAI---TPKRESAQREMERRIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPAL 157
                         170
                  ....*....|
gi 1080851426 342 LRPGRFDRKV 351
Cdd:cd19518   158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
195-352 9.32e-40

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 142.95  E-value: 9.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 195 KQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFED 273
Cdd:cd19526     2 KKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSR 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080851426 274 AKKAERAIIFIDEIDAVGRRRGAGMGGGNDereQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVL 352
Cdd:cd19526    82 AQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
195-353 8.43e-36

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 132.25  E-value: 8.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 195 KQELIEVVDF-LKDPKRYkSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRSLFED 273
Cdd:cd19527     2 KKEILDTIQLpLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 274 AKKAERAIIFIDEIDAVGRRRGAGMGGGNdEREQTLNQLLIEMDGFE-GNESIIVIAATNRSDVLDPALLRPGRFDRKVL 352
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                  .
gi 1080851426 353 V 353
Cdd:cd19527   160 L 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
188-353 1.80e-34

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: 128.62  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 188 VAGAEEEKQELIEVVDF-LKDPKRYkSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 266
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 267 VRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGggndEREQTL-NQLLIEMDGFEGNES--IIVIAATNRSDVLDPALLR 343
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEH----EASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155
                         170
                  ....*....|
gi 1080851426 344 pgRFDRKVLV 353
Cdd:cd19509   156 --RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
187-350 6.46e-34

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: 127.24  E-value: 6.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEVVDF-LKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAG-----VPFFSISGSDFVEMFV 260
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 261 GVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRRgagmgggNDEREQT----LNQLLIEMDGFEGNESIIVIAATNRSDV 336
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                         170
                  ....*....|....
gi 1080851426 337 LDPALLRPGRFDRK 350
Cdd:cd19517   154 LDPALRRPGRFDRE 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
182-353 2.63e-32

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: 122.66  E-value: 2.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 182 KVRFSDVAGAEEEKQELIEVVDF-LKDPKRYKslGARIP-AGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 259
Cdd:cd19521     3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 260 VGVGASRVRSLFEDAKKAERAIIFIDEIDAVgrrRGAGMGGGNDEREQTLNQLLIEMDGF-EGNESIIVIAATNRSDVLD 338
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSL---CGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                         170
                  ....*....|....*
gi 1080851426 339 PALLRpgRFDRKVLV 353
Cdd:cd19521   158 SAIRR--RFEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
187-353 2.88e-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: 116.87  E-value: 2.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEVVdFLKDPKRYKSLGARIPA-GVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAS 265
Cdd:cd19524     1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 266 RVRSLFEDAKKAERAIIFIDEIDAVgrrRGAGMGGGNDEREQTLNQLLIEMDGFEGN--ESIIVIAATNRSDVLDPALLR 343
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSL---LSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR 156
                         170
                  ....*....|
gi 1080851426 344 pgRFDRKVLV 353
Cdd:cd19524   157 --RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
189-355 6.64e-28

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: 109.54  E-value: 6.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 189 AGAEEEKQELIEVVDflkdpkrykslgARIPAGVLLEGPPGTGKTLLAKAVAGEA---GVPFFSISGSDFVEMFVG---V 262
Cdd:cd00009     1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 263 GASRVRSLFEDAKKAERAIIFIDEIDAVgrrrgagmggGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALL 342
Cdd:cd00009    69 GHFLVRLLFELAEKAKPGVLFIDEIDSL----------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                         170
                  ....*....|...
gi 1080851426 343 RPGRFDRKVLVGQ 355
Cdd:cd00009   139 LYDRLDIRIVIPL 151
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
187-347 7.53e-28

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: 109.82  E-value: 7.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEVVDF-LKDPKRYKS---LGAriPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 262
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNsrlLQP--PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 263 GASRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGmgggndEREQTL---NQLLIEMDGF--EGNESIIVIAATNRSDVL 337
Cdd:cd19520    79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLstDGNCRVIVMGATNRPQDL 152
                         170
                  ....*....|..
gi 1080851426 338 DPALLR--PGRF 347
Cdd:cd19520   153 DEAILRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
183-353 2.58e-27

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: 109.31  E-value: 2.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 183 VRFSDVAGAEEEKQELIEVVDF-LKDPKRYKSLGARiPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 261
Cdd:cd19525    19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 262 VGASRVRSLFEDAKKAERAIIFIDEIDAVgrrRGAGMGGGNDEREQTLNQLLIEMDGF--EGNESIIVIAATNRSDVLDP 339
Cdd:cd19525    98 EGEKMVRALFSVARCKQPAVIFIDEIDSL---LSQRGEGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDE 174
                         170
                  ....*....|....
gi 1080851426 340 ALLRpgRFDRKVLV 353
Cdd:cd19525   175 AARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
187-353 6.10e-27

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: 107.38  E-value: 6.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIE-VVDFLKDPKRYKslGARIP-AGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 264
Cdd:cd19522     1 DIADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 265 SRVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEREQTlnQLLIEMDGFEGNES-------IIVIAATNRSDVL 337
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKS--ELLVQMDGVGGASEnddpskmVMVLAATNFPWDI 156
                         170
                  ....*....|....*.
gi 1080851426 338 DPALLRpgRFDRKVLV 353
Cdd:cd19522   157 DEALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
208-351 2.49e-24

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: 100.26  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 208 PKRYKSLGARIPAGVLLEGPPGTGKTLLAKAV-----AGEAGVpffsISGSDFVEMFVGVGASRVRSLFEDAKKAERA-- 280
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080851426 281 ------IIFIDEIDAVGRRRGAGMGGGNdEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKV 351
Cdd:cd19504   100 ansglhIIIFDEIDAICKQRGSMAGSTG-VHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
181-402 2.07e-20

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 94.70  E-value: 2.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 181 VKVRFSDVAGAEEEKqelievvDFLKdpKRYKSLGAR-------IPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSIsgs 253
Cdd:CHL00195  223 VNEKISDIGGLDNLK-------DWLK--KRSTSFSKQasnyglpTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL--- 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 254 DFVEMF---VGVGASRVRSLFEDAKKAERAIIFIDEIDavgrRRGAGMGGGNDEreQTLNQLLIEMDGF--EGNESIIVI 328
Cdd:CHL00195  291 DVGKLFggiVGESESRMRQMIRIAEALSPCILWIDEID----KAFSNSESKGDS--GTTNRVLATFITWlsEKKSPVFVV 364
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080851426 329 AATNRSDVLDPALLRPGRFDRKVLVGQPDVKGREAILRVH-AKNKPLA-DNVDLKVVAQQTPGFVGADLENVLNEA 402
Cdd:CHL00195  365 ATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHlQKFRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEA 440
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
200-353 6.11e-20

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 87.02  E-value: 6.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 200 EVVDFLKDPKRYKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDfvemfVGVGASRVRSLFEDAKKaeR 279
Cdd:cd19510     4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPK--Q 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080851426 280 AIIFIDEIDAV---GRRRGAGMGGGNDEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPGRFDRKVLV 353
Cdd:cd19510    77 SIILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
187-353 5.15e-18

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 81.85  E-value: 5.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELI-EVVDFLKDPKRYKSLgARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAS 265
Cdd:cd19523     1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 266 RVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNdeREQTlnQLLIEMDGF--EGNESIIVIAATNRSDVLDPALLR 343
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
                         170
                  ....*....|
gi 1080851426 344 pgRFDRKVLV 353
Cdd:cd19523   156 --YFSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
219-357 1.99e-17

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: 79.72  E-value: 1.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  219 PAGVLLEGPPGTGKTLLAKAVAGEA---GVPFFSISGSDFVE--------------MFVGVGASRVRSLFEDAKKAERAI 281
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080851426  282 IFIDEIDAVGRRRGagmgggndEREQTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPALLRPgRFDRKVLVGQPD 357
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
187-349 1.22e-15

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: 74.71  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQEL-IEVVDFLKDPKRYkslGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAS 265
Cdd:cd19507     1 DVGGLDNLKDWLkKRKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 266 RVRSLFEDAKKAERAIIFIDEIDAVGRRRGAGMGGGNDEReqTLNQLLIEMDgfEGNESIIVIAATNRSDVLDPALLRPG 345
Cdd:cd19507    78 RLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSR--VLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153

                  ....
gi 1080851426 346 RFDR 349
Cdd:cd19507   154 RFDE 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
377-421 2.71e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 61.40  E-value: 2.71e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1080851426 377 NVDLKVVAQQTPGFVGADLENVLNEAALVAARRNKKVIDASDIDE 421
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 ...
222-351 7.53e-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: 60.62  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGvGASRVRSLFEDAKKAERA-IIFIDEIDAVgrRRGAGMGG 300
Cdd:cd19512    25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTSRRGlLLFVDEADAF--LRKRSTEK 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080851426 301 GNDEREQTLNQLLIEMDgfEGNESIIVIAATNRSDVLDPALlrPGRFDRKV 351
Cdd:cd19512   102 ISEDLRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
PRK04195 PRK04195
replication factor C large subunit; Provisional
184-288 4.15e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 62.63  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 184 RFSDVAGAEEEKQELIEVVDFLKDPKRYKSlgaripagVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDF-----VEM 258
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIESWLKGKPKKA--------LLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 1080851426 259 FVGvGASRVRSLFEDAKKaeraIIFIDEID 288
Cdd:PRK04195   84 VAG-EAATSGSLFGARRK----LILLDEVD 108
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
211-287 2.03e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 211 YKSLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFvemfvgvGASRVRSLFEDAKKAERA----IIFIDE 286
Cdd:PRK13342   28 RRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRSAgrrtILFIDE 100

                  .
gi 1080851426 287 I 287
Cdd:PRK13342  101 I 101
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
13-127 2.14e-09

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 55.30  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426  13 SFIYILLIIAVITTFQYYLKGTSSQNQQISYTKLVKQLKAGEIKSISYQPSggvvEVSGTYKKAKTIKSANSFTflggsv 92
Cdd:pfam06480   1 LLLWLLILLVLLLLFLLFLLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDD----EILPTGVVEGTLKDGSKFT------ 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1080851426  93 atkvTGFNSVILPNDSSIKSLVSAAEENNTNIQVK 127
Cdd:pfam06480  71 ----TYFIPSLPNVDSLLEKLEDALEEKGVKVSVK 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
222-287 4.13e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 59.30  E-value: 4.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISGsdfvemfVGVGASRVRSLFEDAKKA----ERAIIFIDEI 287
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERraygRRTILFVDEI 114
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
222-410 4.22e-09

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: 58.26  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISG------SDfvemFVGVgasrvrSLFEDAKKAER--------AIIFIDEI 287
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpSD----ILGT------YIYDQQTGEFEfrpgplfaNVLLADEI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 288 D-AvgrrrgagmgggndeREQTLNQLLIEMDGFE---GNESI------IVIAATNRSDV-----LDPALLRpgRFDRKVL 352
Cdd:COG0714   104 NrA---------------PPKTQSALLEAMEERQvtiPGGTYklpepfLVIATQNPIEQegtypLPEAQLD--RFLLKLY 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080851426 353 VGQPDVKGREAILRVHAKNKP--------LADNVDLKVVAQQTPgfVGADLENVLneAALVAARRN 410
Cdd:COG0714   167 IGYPDAEEEREILRRHTGRHLaevepvlsPEELLALQELVRQVH--VSEAVLDYI--VDLVRATRE 228
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
221-347 5.05e-09

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 54.99  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 221 GVLLEGPPGTGKTLLAKAVAgEA--GVPFFSISGSDF--VEMFVG------VGASRVRSLFEDAKKaERAIIFIDEIDav 290
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDttEEDLFGrrnidpGGASWVDGPLVRAAR-EGEIAVLDEIN-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 291 grrrgagmgGGNDEREQTLNQLLIE-----MDGFE----GNESIIVIAATNRSD----VLDPALLRpgRF 347
Cdd:pfam07728  77 ---------RANPDVLNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDrglnELSPALRS--RF 135
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
214-349 8.87e-09

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: 55.07  E-value: 8.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 214 LGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV--------------EMFVGVGASRVRSLFEDAKKAER 279
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080851426 280 AIIFIDEIDAVGRRRGAGMGGGNDereQTLNQLLIEM--DGFEGNE--SIIVIAATNRSDVLDPALLRPGRFDR 349
Cdd:cd19505    87 CIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
218-290 7.03e-07

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: 50.07  E-value: 7.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080851426 218 IPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVGVGASRVRSLFEDAKKaerAIIFIDEIDAV 290
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE--VGYVGRDVESIIRDLVE---GIVFIDEIDKI 112
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
222-288 9.87e-07

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 51.59  E-value: 9.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFfSIS-----------GSDfVEmfvgvgaSRVRSLFE----DAKKAERAIIFIDE 286
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvGED-VE-------NILLKLLQaadyDVEKAERGIIYIDE 182

                  ..
gi 1080851426 287 ID 288
Cdd:COG1219   183 ID 184
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
222-288 1.98e-06

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 50.54  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFfSIS-----------GSDfVEMFVgvgasrVRSLFE---DAKKAERAIIFIDEI 287
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvGED-VENIL------LKLLQAadyDVEKAQRGIVYIDEI 182

                  .
gi 1080851426 288 D 288
Cdd:PRK05342  183 D 183
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
222-287 3.06e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.74  E-value: 3.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISG------SDFVEMFVGVGasrvrslfedakkaERAIIFIDEI 287
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLE--------------EGDVLFIDEI 111
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
222-288 3.79e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 48.75  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPfFSIS-----------GSDfVEmfvgvgaSRVRSLFEDA----KKAERAIIFIDE 286
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VE-------NILLKLLQAAdydvERAQRGIVYIDE 123

                  ..
gi 1080851426 287 ID 288
Cdd:cd19497   124 ID 125
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
221-255 8.78e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.81  E-value: 8.78e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1080851426 221 GVLLEGPPGTGKTLLAKAVAGEAG--VPFFSISGSDF 255
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
44 PHA02544
clamp loader, small subunit; Provisional
217-288 1.39e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 47.68  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080851426 217 RIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFFSISGS----DFVEMFVGVGASRVrSLFEDAKkaeraIIFIDEID 288
Cdd:PHA02544   41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-SLTGGGK-----VIIIDEFD 110
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
221-255 1.71e-05

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: 47.30  E-value: 1.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1080851426 221 GVLLEGPPGTGKTLLAKAVAGEAG--VPFFSISGSDF 255
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
222-338 3.82e-05

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: 43.65  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEA---GVPFFSISgsdFVEMFVgvgaSRVRSLFEDAKkaeRAIIFIDEIDAVgrrrgaGM 298
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSL------AR 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1080851426 299 GGGNDEREQTLNQLLIEMDGFeGNESIIVIAATNRSDVLD 338
Cdd:cd01120    65 ASQGDRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI 103
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
222-287 3.88e-05

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: 44.41  E-value: 3.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISG------SDFVEMFVGVgasrvrslfedakkAERAIIFIDEI 287
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpaierpGDLAAILTNL--------------EPGDVLFIDEI 93
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
194-343 5.18e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 46.72  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 194 EKQELIEVVDFLKDPKRYkslgaripagVLLEGPPGTGKTLLAKAVA---------GEAGVPFF----SISGS----DFV 256
Cdd:COG5635   165 ERIESLKRLELLEAKKKR----------LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrDLAEEasleDLL 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 257 EMFVGVGASRVRSLFEDAKKAERAIIFIDEIDAVGRRrgagmgggnDEREQTLNQLLIEMDGFEGNeSIIViaaTNRSDV 336
Cdd:COG5635   235 AEALEKRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKA-RVII---TSRPEG 301

                  ....*..
gi 1080851426 337 LDPALLR 343
Cdd:COG5635   302 YDSSELE 308
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
187-288 7.52e-05

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 44.09  E-value: 7.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 187 DVAGAEEEKQELIEvvdFLKDPKRYKSLGARIpagVLLEGPPGTGKTLLAKAVAGEAGVPFFSIS-G--SDFVEM----- 258
Cdd:cd19500    11 DHYGLEDVKERILE---YLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghrr 84
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1080851426 259 -FVGVGASRVRSLFEDAKKaERAIIFIDEID 288
Cdd:cd19500    85 tYVGAMPGRIIQALKKAGT-NNPVFLLDEID 114
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
222-341 1.14e-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: 43.59  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGV---------------------PFFSISGSDFVEMFvgvgaSRVRSLFEDakkaERA 280
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDD----KDA 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080851426 281 IIF--IDEIDAVgRRRGAGMGGGNDERE--QTLNQLLIEMDGFEGNESIIVIAATNRSDVLDPAL 341
Cdd:cd19508   126 LVFvlIDEVESL-AAARSASSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
Sigma54_activat pfam00158
Sigma-54 interaction domain;
216-287 2.45e-04

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 42.00  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 216 ARIPAGVLLEGPPGTGKTLLAKAV---AGEAGVPFFSISGSDFV------EMFvGV------GASRVRS-LFEdakKAER 279
Cdd:pfam00158  19 APTDAPVLITGESGTGKELFARAIhqlSPRADGPFVAVNCAAIPeellesELF-GHekgaftGADSDRKgLFE---LADG 94

                  ....*...
gi 1080851426 280 AIIFIDEI 287
Cdd:pfam00158  95 GTLFLDEI 102
PRK13341 PRK13341
AAA family ATPase;
223-287 3.96e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.50  E-value: 3.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 223 LLEGPPGTGKTLLAKAVAGEAGVPFFSISGsdfvemfVGVGASRVRSLFEDAKK-----AERAIIFIDEI 287
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDEV 118
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
190-351 4.63e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 43.29  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 190 GAEEEKQELIEVVDFLKDPKRYKSLGARIPAG---VLLEGPPGTGKTLLAKAVAGE-AGVPFFS------ISGSDFVEMF 259
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTsnhMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 260 VGVGASRVRSLFEdakKAERAIIFIDEIDAVgrrRGAGMGGGNDEREQTLNQLLIEMDGfeGNESIIVIAATNRSDvLDP 339
Cdd:TIGR03922 360 IGESEAKTNEIID---SALGGVLFLDEAYTL---VETGYGQKDPFGLEAIDTLLARMEN--DRDRLVVIGAGYRKD-LDK 430
                         170
                  ....*....|....*..
gi 1080851426 340 AL-----LRpGRFDRKV 351
Cdd:TIGR03922 431 FLevnegLR-SRFTRVI 446
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
219-426 7.06e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.53  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 219 PAGVLLEGPPGTGKTLLAKAV-------AGEAGVPF-------------FSI---------SGSDFVEmfVGVGASRVRS 269
Cdd:COG1474    51 PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVrvvyvncrqastrYRVlsrileelgSGEDIPS--TGLSTDELFD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 270 LFEDA--KKAERAIIFIDEIDAVgrrrgagmggGNDEREQTLNQLLiEMDGFEGNESIIVIAATNRSDV---LDPALLRp 344
Cdd:COG1474   129 RLYEAldERDGVLVVVLDEIDYL----------VDDEGDDLLYQLL-RANEELEGARVGVIGISNDLEFlenLDPRVKS- 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 345 gRFDRKVLVGQP-DVKGREAILRVHAKnKPLADNV------DLkvVAQQTPGFVG-A----DLenvLNEAALVAARRNKK 412
Cdd:COG1474   197 -SLGEEEIVFPPyDADELRDILEDRAE-LAFYDGVlsdeviPL--IAALAAQEHGdArkaiDL---LRVAGEIAEREGSD 269
                         250
                  ....*....|....
gi 1080851426 413 VIDASDIDEAEDRV 426
Cdd:COG1474   270 RVTEEHVREAREKI 283
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
222-290 7.20e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 42.29  E-value: 7.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISG------SDFVEMFVGVgasrvrslfedakkAERAIIFIDEIDAV 290
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNL--------------EEGDVLFIDEIHRL 93
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
222-288 7.41e-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: 40.64  E-value: 7.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGV---PFFSISGSDFVE-----MFVG-----VGASRVRSLFEDAKKAERAIIFIDEID 288
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
222-252 1.30e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 41.60  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1080851426 222 VLLEGPPGTGKTLLAKAVAGEAGVPFFSISG 252
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
205-288 1.55e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 39.85  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 205 LKDPKRykslgariPAGVLL-EGPPGTGKTLLAKAVAGE---AGVPFFSISGSDFVEMFVG----------VGASRVRSL 270
Cdd:cd19499    34 LSDPNR--------PIGSFLfLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHSVsrligappgyVGYTEGGQL 105
                          90
                  ....*....|....*...
gi 1080851426 271 FEDAKKAERAIIFIDEID 288
Cdd:cd19499   106 TEAVRRKPYSVVLLDEIE 123
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
217-289 4.62e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 39.57  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 217 RIPAGVLLEGPPGTGKTLLAKAVAGE---------------AGVPFFSISGSDFVEMFVGV-----GASRVRSLFEDAKK 276
Cdd:COG0470    16 RLPHALLLHGPPGIGKTTLALALARDllcenpeggkacgqcHSRLMAAGNHPDLLELNPEEksdqiGIDQIRELGEFLSL 95
                          90
                  ....*....|....*..
gi 1080851426 277 ----AERAIIFIDEIDA 289
Cdd:COG0470    96 tpleGGRKVVIIDEADA 112
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
198-241 4.63e-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: 40.02  E-value: 4.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080851426 198 LIEVVDFLKDPKRYKSLGARIP---------------------------AG---VLLEGPPGTGKTLLAKAVAG 241
Cdd:COG0606   160 LLEVVAFLRGEQPLPPAEPDAPpaeppyepdladvkgqeqakraleiaaAGghnLLMIGPPGSGKTMLARRLPG 233
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
185-241 5.88e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.67  E-value: 5.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 185 FSDVAGAEEEKQELiEVVdflkdpkrykslgariPAG---VLLEGPPGTGKTLLAKAVAG 241
Cdd:pfam01078   2 LADVKGQEQAKRAL-EIA----------------AAGghnLLMIGPPGSGKTMLAKRLPG 44
AAA_22 pfam13401
AAA domain;
222-337 6.63e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKTLLAKAVA---GEAGVPFFSI------SGSDFVEMFV---------GVGASRVRSLFEDA--KKAERAI 281
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1080851426 282 IFIDEIDAVgrrrgagmgggndeREQTLNQLLIEMDGFEGNESIIVIAATNRSDVL 337
Cdd:pfam13401  88 LIIDEAQHL--------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
222-287 8.65e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.98  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080851426 222 VLLEGPPGTGKT----LLAKAVAGEAG-----VPFF-SISGSDFVEMFVGVGAS----RVRSLFEDA-KKAERA-----I 281
Cdd:COG1401   224 VILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpSWSYEDFLLGYRPSLDEgkyePTPGIFLRFcLKAEKNpdkpyV 303

                  ....*.
gi 1080851426 282 IFIDEI 287
Cdd:COG1401   304 LIIDEI 309
 
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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