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Conserved domains on  [gi|488292233|ref|WP_002363441|]
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MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Enterococcus]

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];
26-626 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1003.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  26 YFIFGNNNQQSPDIDYSTFQQQLEDGKVKDMTIQPTngvyRIEGQYKEKQEVKdtgglslwgstqasskgFTTTVlPSDT 105
Cdd:COG0465    9 FNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGD----RITGTLKDGTKTR-----------------FTTYR-VNDP 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 106 TLAgiqDAAQNNKVKLVVKEQSTSGAWLSLLFSFLPLVIIFFFFYMMMSQQGGGGGgggRVMNFGKSKAKEADKKANRVR 185
Cdd:COG0465   67 ELV---DLLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGG---GAMSFGKSKAKLYDEDKPKVT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGA 265
Cdd:COG0465  141 FDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 266 SRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRP 345
Cdd:COG0465  221 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRP 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 346 GRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEAED 425
Cdd:COG0465  301 GRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAID 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 426 RVIAGPAKKDRVINKKEREMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLL 505
Cdd:COG0465  381 RVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLL 460
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 506 GGRTAEEIIFGVQSTGASNDFEQATGIARSMVTEYGMSDKLGPVQYEGN-HQVFVGRDYGQTKAYSEQVAFEIDQEVRRI 584
Cdd:COG0465  461 GGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESeGEVFLGRDIGQSRNYSEETAREIDEEVRRI 540
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 488292233 585 LMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFE 626
Cdd:COG0465  541 IDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
PTZ00121 super family cl31754
MAEBL; Provisional
579-716 4.62e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  579 QEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFETGKMpegADSDYPSEKEAQTFEEAKRALEEK- 657
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEAKKAEEAKKKAEEAk 1470
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488292233  658 ---EAQKQVEEKQDFEEAKKelhdEAEEVKVESEQTEKEVQSEEKKDSDSNSEYDRNNYEDR 716
Cdd:PTZ00121 1471 kadEAKKKAEEAKKADEAKK----KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
26-626 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1003.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  26 YFIFGNNNQQSPDIDYSTFQQQLEDGKVKDMTIQPTngvyRIEGQYKEKQEVKdtgglslwgstqasskgFTTTVlPSDT 105
Cdd:COG0465    9 FNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGD----RITGTLKDGTKTR-----------------FTTYR-VNDP 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 106 TLAgiqDAAQNNKVKLVVKEQSTSGAWLSLLFSFLPLVIIFFFFYMMMSQQGGGGGgggRVMNFGKSKAKEADKKANRVR 185
Cdd:COG0465   67 ELV---DLLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGG---GAMSFGKSKAKLYDEDKPKVT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGA 265
Cdd:COG0465  141 FDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 266 SRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRP 345
Cdd:COG0465  221 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRP 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 346 GRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEAED 425
Cdd:COG0465  301 GRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAID 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 426 RVIAGPAKKDRVINKKEREMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLL 505
Cdd:COG0465  381 RVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLL 460
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 506 GGRTAEEIIFGVQSTGASNDFEQATGIARSMVTEYGMSDKLGPVQYEGN-HQVFVGRDYGQTKAYSEQVAFEIDQEVRRI 584
Cdd:COG0465  461 GGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESeGEVFLGRDIGQSRNYSEETAREIDEEVRRI 540
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 488292233 585 LMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFE 626
Cdd:COG0465  541 IDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
143-626 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: 812.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  143 VIIFFFFYMMMSQQGGGGGGggRVMNFGKSKAKEADKKANRVRFSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAG 222
Cdd:TIGR01241  13 ILLLVGVWFFFRRQMQGGGG--RAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGG 302
Cdd:TIGR01241  91 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  303 HDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLK 382
Cdd:TIGR01241 171 NDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLK 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  383 VVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEAEDRVIAGPAKKDRVINKKEREMVAYHEAGHTIVGLVLSR 462
Cdd:TIGR01241 251 AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKD 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  463 ARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLLGGRTAEEIIFGVQSTGASNDFEQATGIARSMVTEYGM 542
Cdd:TIGR01241 331 ADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGM 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  543 SDKLGPVQYEGNH-QVFVGRDYGQTKAYSEQVAFEIDQEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAI 621
Cdd:TIGR01241 411 SDKLGPVAYGSDGgDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEI 490

                  ....*
gi 488292233  622 KSLFE 626
Cdd:TIGR01241 491 KELLA 495
ftsH CHL00176
cell division protein; Validated
167-632 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 629.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 167 MNFGKSKA---KEADKKanrVRFSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGE 243
Cdd:CHL00176 163 MNFGKSKArfqMEADTG---ITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 244 AGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGN 323
Cdd:CHL00176 240 AEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGN 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 324 EGVIVIAATNRSDVLDPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEA 403
Cdd:CHL00176 320 KGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEA 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 404 ALVAARRNKKKIDASDVDEAEDRVIAGPAKKDRVINKKEReMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIA 483
Cdd:CHL00176 400 AILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKR-LIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWF 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 484 LPKEDQFLMTKEDMFEQIVGLLGGRTAEEIIFGVQS--TGASNDFEQATGIARSMVTEYGMSdKLGPVQYE--GNHQVFV 559
Cdd:CHL00176 479 TPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEvtTGASNDLQQVTNLARQMVTRFGMS-SIGPISLEsnNSTDPFL 557
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488292233 560 GRDYGQTKAYSEQVAFEIDQEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFET-GKMPE 632
Cdd:CHL00176 558 GRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSyTILPP 631
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
184-354 2.95e-124

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: 366.94  E-value: 2.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 184 VRFSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGV 263
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 264 GASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALL 343
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 488292233 344 RPGRFDRQILV 354
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
436-624 5.67e-91

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 281.80  E-value: 5.67e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  436 RVINKKEREMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLLGGRTAEEIIF 515
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  516 GVQSTGASNDFEQATGIARSMVTEYGMSDKLGPVQYEGNH-QVFVGRDYGQTKAYSEQVAFEIDQEVRRILMDAHTKAHE 594
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 488292233  595 IIEAHREQHKLIAEKLLEYETLDAKAIKSL 624
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
220-358 2.63e-20

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.81  E-value: 2.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233   220 PAGVLLEGPPGTGKTLLAKAVAGEA---GVPFYSISGSDFVE--------------MFVGVGASRVRDLFETAKKNAPAI 282
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233   283 IFIDEIDAvgrqrgagMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPgRFDRQILVGRPD 358
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
PTZ00121 PTZ00121
MAEBL; Provisional
579-716 4.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  579 QEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFETGKMpegADSDYPSEKEAQTFEEAKRALEEK- 657
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEAKKAEEAKKKAEEAk 1470
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488292233  658 ---EAQKQVEEKQDFEEAKKelhdEAEEVKVESEQTEKEVQSEEKKDSDSNSEYDRNNYEDR 716
Cdd:PTZ00121 1471 kadEAKKKAEEAKKADEAKK----KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
626-707 2.25e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  626 ETGKMPEGADSDYPSEKEaQTFEEAKRALEekeaQKQVEEKQDFEEAKKELHDEAEEVKVESEQTEKEvqsEEKKDSDSN 705
Cdd:pfam05262 256 EAKNLPKPADTSSPKEDK-QVAENQKREIE----KAQIEIKKNDEEALKAKDHKAFDLKQESKASEKE---AEDKELEAQ 327

                  ..
gi 488292233  706 SE 707
Cdd:pfam05262 328 KK 329
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
26-626 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1003.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  26 YFIFGNNNQQSPDIDYSTFQQQLEDGKVKDMTIQPTngvyRIEGQYKEKQEVKdtgglslwgstqasskgFTTTVlPSDT 105
Cdd:COG0465    9 FNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGD----RITGTLKDGTKTR-----------------FTTYR-VNDP 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 106 TLAgiqDAAQNNKVKLVVKEQSTSGAWLSLLFSFLPLVIIFFFFYMMMSQQGGGGGgggRVMNFGKSKAKEADKKANRVR 185
Cdd:COG0465   67 ELV---DLLEEKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGG---GAMSFGKSKAKLYDEDKPKVT 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGA 265
Cdd:COG0465  141 FDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 266 SRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRP 345
Cdd:COG0465  221 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRP 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 346 GRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEAED 425
Cdd:COG0465  301 GRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAID 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 426 RVIAGPAKKDRVINKKEREMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLL 505
Cdd:COG0465  381 RVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLL 460
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 506 GGRTAEEIIFGVQSTGASNDFEQATGIARSMVTEYGMSDKLGPVQYEGN-HQVFVGRDYGQTKAYSEQVAFEIDQEVRRI 584
Cdd:COG0465  461 GGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESeGEVFLGRDIGQSRNYSEETAREIDEEVRRI 540
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 488292233 585 LMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFE 626
Cdd:COG0465  541 IDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
143-626 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: 812.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  143 VIIFFFFYMMMSQQGGGGGGggRVMNFGKSKAKEADKKANRVRFSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAG 222
Cdd:TIGR01241  13 ILLLVGVWFFFRRQMQGGGG--RAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGG 302
Cdd:TIGR01241  91 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  303 HDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLK 382
Cdd:TIGR01241 171 NDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLK 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  383 VVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEAEDRVIAGPAKKDRVINKKEREMVAYHEAGHTIVGLVLSR 462
Cdd:TIGR01241 251 AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKD 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  463 ARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLLGGRTAEEIIFGVQSTGASNDFEQATGIARSMVTEYGM 542
Cdd:TIGR01241 331 ADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGM 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  543 SDKLGPVQYEGNH-QVFVGRDYGQTKAYSEQVAFEIDQEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAI 621
Cdd:TIGR01241 411 SDKLGPVAYGSDGgDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEI 490

                  ....*
gi 488292233  622 KSLFE 626
Cdd:TIGR01241 491 KELLA 495
ftsH CHL00176
cell division protein; Validated
167-632 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 629.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 167 MNFGKSKA---KEADKKanrVRFSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGE 243
Cdd:CHL00176 163 MNFGKSKArfqMEADTG---ITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 244 AGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGN 323
Cdd:CHL00176 240 AEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGN 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 324 EGVIVIAATNRSDVLDPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEA 403
Cdd:CHL00176 320 KGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEA 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 404 ALVAARRNKKKIDASDVDEAEDRVIAGPAKKDRVINKKEReMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIA 483
Cdd:CHL00176 400 AILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKR-LIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWF 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 484 LPKEDQFLMTKEDMFEQIVGLLGGRTAEEIIFGVQS--TGASNDFEQATGIARSMVTEYGMSdKLGPVQYE--GNHQVFV 559
Cdd:CHL00176 479 TPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEvtTGASNDLQQVTNLARQMVTRFGMS-SIGPISLEsnNSTDPFL 557
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488292233 560 GRDYGQTKAYSEQVAFEIDQEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFET-GKMPE 632
Cdd:CHL00176 558 GRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSyTILPP 631
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
29-637 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 570.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  29 FGNNNQQSPDIDYSTFQQQLEDGKVKDMtiqptngvyRIEGQykekqEVKdtgglslwgSTQASSKGFTTTVLPSDTTLA 108
Cdd:PRK10733  22 FGPSESNGRKVDYSTFLQEVNQDQVREA---------RINGR-----EIN---------VTKKDSNRYTTYIPVNDPKLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 109 giqDAAQNNKVKLV---VKEQSTSGAWLSLLFSFLPLVIIFFFFYMMMSQQGGGGggggrVMNFGKSKAKEADKKANRVR 185
Cdd:PRK10733  79 ---DNLLTKNVKVVgepPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKG-----AMSFGKSKARMLTEDQIKTT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGA 265
Cdd:PRK10733 151 FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 266 SRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRP 345
Cdd:PRK10733 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRP 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 346 GRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEAED 425
Cdd:PRK10733 311 GRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKD 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 426 RVIAGPAKKDRVINKKEREMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLL 505
Cdd:PRK10733 391 KIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLY 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 506 GGRTAEEIIFGVQ--STGASNDFEQATGIARSMVTEYGMSDKLGPVQY-EGNHQVFVGRDYGQTKAYSEQVAFEIDQEVR 582
Cdd:PRK10733 471 GGRLAEEIIYGPEhvSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYaEEEGEVFLGRSVAKAKHMSDETARIIDQEVK 550
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488292233 583 RILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFETGKM--PEGADSD 637
Cdd:PRK10733 551 ALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVrpPAGWEEP 607
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
184-354 2.95e-124

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: 366.94  E-value: 2.95e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 184 VRFSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGV 263
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 264 GASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALL 343
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 488292233 344 RPGRFDRQILV 354
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
184-436 2.16e-113

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 345.07  E-value: 2.16e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 184 VRFSDVAGAEEEKQELVEVVE-FLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVG 262
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 263 VGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGhdEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPAL 342
Cdd:COG1222  155 EGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPAL 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 343 LRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDE 422
Cdd:COG1222  233 LRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEK 312
                        250
                 ....*....|....
gi 488292233 423 AEDRVIAGPAKKDR 436
Cdd:COG1222  313 AIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
184-447 1.46e-96

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 303.68  E-value: 1.46e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 184 VRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVG 262
Cdd:PRK03992 128 VTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIG 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 263 VGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPAL 342
Cdd:PRK03992 208 EGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAI 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 343 LRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDE 422
Cdd:PRK03992 288 LRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLK 367
                        250       260
                 ....*....|....*....|....*
gi 488292233 423 AEDRVIagpAKKDRVINKKEREMVA 447
Cdd:PRK03992 368 AIEKVM---GKEEKDSMEEPGVMFA 389
Peptidase_M41 pfam01434
Peptidase family M41;
436-624 5.67e-91

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 281.80  E-value: 5.67e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  436 RVINKKEREMVAYHEAGHTIVGLVLSRARVVHKVTIIPRGRAGGYMIALPKEDQFLMTKEDMFEQIVGLLGGRTAEEIIF 515
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  516 GVQSTGASNDFEQATGIARSMVTEYGMSDKLGPVQYEGNH-QVFVGRDYGQTKAYSEQVAFEIDQEVRRILMDAHTKAHE 594
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 488292233  595 IIEAHREQHKLIAEKLLEYETLDAKAIKSL 624
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
175-423 1.40e-83

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: 270.24  E-value: 1.40e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 175 KEADKKANRVRFSDVAGAEEEKQELVEVVE-FLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISG 253
Cdd:COG0464  145 EEELLELREAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 254 SDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGaGMGGGHDEREqtLNQLLVEMDGFdgNEGVIVIAATN 333
Cdd:COG0464  225 SDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEEL--RSDVVVIAATN 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 334 RSDVLDPALLRpgRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKK 413
Cdd:COG0464  300 RPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377
                        250
                 ....*....|
gi 488292233 414 KIDASDVDEA 423
Cdd:COG0464  378 PVTTEDLLEA 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
173-428 1.82e-82

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: 265.89  E-value: 1.82e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  173 KAKEADKKANrVRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSI 251
Cdd:TIGR01242 109 KGMEVEERPN-VSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  252 SGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAA 331
Cdd:TIGR01242 188 VGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAA 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  332 TNRSDVLDPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRN 411
Cdd:TIGR01242 268 TNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREE 347
                         250
                  ....*....|....*..
gi 488292233  412 KKKIDASDVDEAEDRVI 428
Cdd:TIGR01242 348 RDYVTMDDFIKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
184-442 5.89e-73

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 250.98  E-value: 5.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  184 VRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVG 262
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  263 VGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEReqTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPAL 342
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPAL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  343 LRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDE 422
Cdd:TIGR01243 608 LRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEV 687
                         250       260
                  ....*....|....*....|
gi 488292233  423 AEDRVIagpakKDRVINKKE 442
Cdd:TIGR01243 688 GEEEFL-----KDLKVEMRH 702
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
176-416 3.77e-67

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 235.19  E-value: 3.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  176 EADKKANRVRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGS 254
Cdd:TIGR01243 167 EIERKVPKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGP 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  255 DFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGgghDEREQTLNQLLVEMDGFDGNEGVIVIAATNR 334
Cdd:TIGR01243 247 EIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNR 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  335 SDVLDPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARR--NK 412
Cdd:TIGR01243 324 PDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiRE 403

                  ....
gi 488292233  413 KKID 416
Cdd:TIGR01243 404 GKIN 407
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
186-352 1.61e-66

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: 216.82  E-value: 1.61e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVG 264
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 265 ASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLR 344
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                 ....*...
gi 488292233 345 PGRFDRQI 352
Cdd:cd19502  162 PGRFDRKI 169
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
196-354 4.21e-63

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 207.14  E-value: 4.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 196 KQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFETA 275
Cdd:cd19481    2 KASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488292233 276 KKNAPAIIFIDEIDAVGRQRGAgmGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILV 354
Cdd:cd19481   82 RRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
180-428 4.39e-63

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 216.95  E-value: 4.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 180 KANRVRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVE 258
Cdd:PTZ00361 176 KAPLESYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 259 MFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVL 338
Cdd:PTZ00361 256 KYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESL 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 339 DPALLRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDAS 418
Cdd:PTZ00361 336 DPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQA 415
                        250
                 ....*....|
gi 488292233 419 DVDEAEDRVI 428
Cdd:PTZ00361 416 DFRKAKEKVL 425
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
184-428 5.54e-62

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 212.70  E-value: 5.54e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 184 VRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVG 262
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 263 VGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPAL 342
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 343 LRPGRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDE 422
Cdd:PTZ00454 302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEK 381

                 ....*.
gi 488292233 423 AEDRVI 428
Cdd:PTZ00454 382 GYKTVV 387
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
196-354 3.35e-61

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 202.13  E-value: 3.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 196 KQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFET 274
Cdd:cd19511    2 KRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 275 AKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEReqTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILV 354
Cdd:cd19511   82 ARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
186-423 3.28e-59

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 200.11  E-value: 3.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVEVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGA 265
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 266 SRVRDLFETAkKNAPAIIFIDEIDAVGRQRgaGMGGGHDEREQTLNQLLVEMDGFdgNEGVIVIAATNRSDVLDPALLRp 345
Cdd:COG1223   81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDR--GDQNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488292233 346 gRFDRQILVGRPDVKGREAILRVHAKNKPLADDVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDEA 423
Cdd:COG1223  155 -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 ...
188-352 3.11e-58

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 194.43  E-value: 3.11e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGAS 266
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 267 RVRDLFETAKKNAPAIIFIDEIDAVGRQRGAgmggGHDEREQTL-NQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRP 345
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*..
gi 488292233 346 GRFDRQI 352
Cdd:cd19503  157 GRFDREV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
223-356 9.51e-57

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: 188.96  E-value: 9.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGagmGGG 302
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488292233  303 HDEREQTLNQLLVEMDGFDGNEG-VIVIAATNRSDVLDPALLrpGRFDRQILVGR 356
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
196-354 7.22e-55

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 185.39  E-value: 7.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 196 KQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFET 274
Cdd:cd19529    2 KQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 275 AKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEReqTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILV 354
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 ...
188-355 4.58e-51

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: 175.32  E-value: 4.58e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGAS 266
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 267 RVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGgghDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPG 346
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHG---EVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 488292233 347 RFDRQILVG 355
Cdd:cd19519  158 RFDREIDIG 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
196-354 9.96e-51

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: 173.85  E-value: 9.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 196 KQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFET 274
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 275 AKKNAPAIIFIDEIDAVGRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILV 354
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
202-354 1.39e-48

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 168.05  E-value: 1.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 202 VVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPA 281
Cdd:cd19530   12 ILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488292233 282 IIFIDEIDAVGRQRGagmGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILV 354
Cdd:cd19530   92 VIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
188-352 3.66e-48

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 167.20  E-value: 3.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVEVVEFLKDPRR-FAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGAS 266
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 267 RVRDLFETAKKNAPAIIFIDEIDAVGRQRgagMGGGHDEREQTLNQLLVEMDGFDGNE----GVIVIAATNRSDVLDPAL 342
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR---ESAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 488292233 343 LRPGRFDRQI 352
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 ...
196-353 5.94e-45

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 157.98  E-value: 5.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 196 KQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFET 274
Cdd:cd19526    2 KKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSR 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488292233 275 AKKNAPAIIFIDEIDAVGRQRGAGMGGGHDereQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQIL 353
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 ...
196-354 1.33e-42

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 151.51  E-value: 1.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 196 KQELVEVVEF-LKDPRRFAeLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFET 274
Cdd:cd19527    2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 275 AKKNAPAIIFIDEIDAVGRQRGA-GMGGGHDEReqTLNQLLVEMDGF-DGNEGVIVIAATNRSDVLDPALLRPGRFDRQI 352
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 488292233 353 LV 354
Cdd:cd19527  159 YL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
189-354 3.43e-41

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 147.88  E-value: 3.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 189 VAGAEEEKQELVEVVEF-LKDPRRFAeLGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASR 267
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 268 VRDLFETAKKNAPAIIFIDEIDAVGRQRGAgmgGGHDEREQTLNQLLVEMDGF--DGNEGVIVIAATNRSDVLDPALLRp 345
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155

                 ....*....
gi 488292233 346 gRFDRQILV 354
Cdd:cd19509  156 -RFEKRIYI 163
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
184-378 1.68e-39

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 152.94  E-value: 1.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  184 VRFSDVAGAEEEKQELVEVVE--FLKdPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVA--------GEAGVP--FYSI 251
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVElpFLH-PELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGGGKsyFLNI 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  252 SGSDFVEMFVGVGASRVRDLFETAKKNA----PAIIFIDEIDAVGRQRGAGMGGghDEREQTLNQLLVEMDGFDGNEGVI 327
Cdd:TIGR03689 258 KGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGVSS--DVETTVVPQLLAEIDGVESLDNVI 335
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488292233  328 VIAATNRSDVLDPALLRPGRFDRQILVGRPDVKGREAILRVH-AKNKPLADD 378
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYlTDDLPLPED 387
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
184-354 9.31e-38

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: 138.46  E-value: 9.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 184 VRFSDVAGAEEEKQELVEVVEFlkdPRRFAEL--GARIP-AGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMF 260
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 261 VGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMGgghDEREQTLNQLLVEMDGF-DGNEGVIVIAATNRSDVLD 339
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGES---EASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 488292233 340 PALLRpgRFDRQILV 354
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
188-353 4.82e-37

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 136.49  E-value: 4.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVEVVEF-LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAG-----VPFYSISGSDFVEMFV 261
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 262 GVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAgmggghdEREQT----LNQLLVEMDGFDGNEGVIVIAATNRSDV 337
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....*.
gi 488292233 338 LDPALLRPGRFDRQIL 353
Cdd:cd19517  154 LDPALRRPGRFDREFY 169
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
188-348 1.17e-33

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: 126.77  E-value: 1.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVEVVEFlkdPRRFAELGA-----RIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVG 262
Cdd:cd19520    1 DIGGLDEVITELKELVIL---PLQRPELFDnsrllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 263 VGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAgmgGGHDEREQTLNQLLVEMDGF--DGNEGVIVIAATNRSDVLDP 340
Cdd:cd19520   78 ESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDE 154
                        170
                 ....*....|
gi 488292233 341 ALLR--PGRF 348
Cdd:cd19520  155 AILRrmPKRF 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
188-354 1.48e-32

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 123.42  E-value: 1.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVEVVeFLKDPRRFAELGARIPA-GVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGAS 266
Cdd:cd19524    1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 267 RVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMgggHDEREQTLNQLLVEMDGFDGN--EGVIVIAATNRSDVLDPALLR 344
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGE---HEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 488292233 345 pgRFDRQILV 354
Cdd:cd19524  157 --RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
188-354 2.12e-32

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 123.17  E-value: 2.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELVE-VVEFLKDPRRFAelGARIP-AGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGA 265
Cdd:cd19522    1 DIADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 266 SRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAgmGGGHDEREQTLNQLLVEMDGFDG---NEG----VIVIAATNRSDVL 338
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGaseNDDpskmVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 488292233 339 DPALLRpgRFDRQILV 354
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
182-354 2.26e-32

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 123.94  E-value: 2.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 182 NRVRFSDVAGAEEEKQELVEVVEF-LKDPRRFAELGARiPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMF 260
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 261 VGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQRGAGMgggHDEREQTLNQLLVEMDGFD--GNEGVIVIAATNRSDVL 338
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE---HESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEI 172
                        170
                 ....*....|....*.
gi 488292233 339 DPALLRpgRFDRQILV 354
Cdd:cd19525  173 DEAARR--RLVKRLYI 186
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
190-355 2.71e-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: 110.70  E-value: 2.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 190 AGAEEEKQELVEVVEflkdprrfaelgARIPAGVLLEGPPGTGKTLLAKAVAGEA---GVPFYSISGSDFVEMFVG---V 263
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 264 GASRVRDLFETAKKNAPAIIFIDEIDAVGRqrgagmggghDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALL 343
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|..
gi 488292233 344 RPGRFDRQILVG 355
Cdd:cd00009  139 LYDRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
209-352 1.37e-27

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: 109.89  E-value: 1.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 209 PRRFAELGARIPAGVLLEGPPGTGKTLLAKAV-----AGEAGVpfysISGSDFVEMFVGVGASRVRDLFETAKKNAPA-- 281
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488292233 282 ------IIFIDEIDAVGRQRGAgMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQI 352
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGS-MAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
186-403 6.11e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 102.79  E-value: 6.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGAEEEKQELVevveflKDPRRFAE----LGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSIsgsDFVEMF- 260
Cdd:CHL00195 227 ISDIGGLDNLKDWLK------KRSTSFSKqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFg 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 261 --VGVGASRVRDLFETAKKNAPAIIFIDEID-AVGRQRGAGMGGGHDEREQTLNQLLVEMDGFdgnegVIVIAATNRSDV 337
Cdd:CHL00195 298 giVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEKKSP-----VFVVATANNIDL 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488292233 338 LDPALLRPGRFDRQILVGRPDVKGREAILRVH-AKNKPLA-DDVDLKVVAQQTPGFAGADLENVLNEA 403
Cdd:CHL00195 373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHlQKFRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEA 440
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
220-358 2.63e-20

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.81  E-value: 2.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233   220 PAGVLLEGPPGTGKTLLAKAVAGEA---GVPFYSISGSDFVE--------------MFVGVGASRVRDLFETAKKNAPAI 282
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233   283 IFIDEIDAvgrqrgagMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPgRFDRQILVGRPD 358
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
201-354 4.88e-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: 87.41  E-value: 4.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 201 EVVEFLKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDfvemfVGVGASRVRDLFETAKKNAp 280
Cdd:cd19510    4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488292233 281 aIIFIDEIDAV---GRQRGAGMGGGHDEREQTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQILV 354
Cdd:cd19510   78 -IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
188-354 1.07e-19

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 86.86  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 188 DVAGAEEEKQELV-EVVEFLKDPRRFAELgARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGAS 266
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 267 RVRDLFETAKKNAPAIIFIDEIDAV--GRQRGAGMGGghdeREQTlnQLLVEMDGF--DGNEGVIVIAATNRSDVLDPAL 342
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESL 153
                        170
                 ....*....|..
gi 488292233 343 LRpgRFDRQILV 354
Cdd:cd19523  154 RR--YFSKRLLV 163
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
216-350 2.56e-19

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: 85.50  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 216 GARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFETAKKNAPAIIFIDEID-AVGrq 294
Cdd:cd19507   27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFS-- 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233 295 rGAGMGGGHDEREQTLNQLLVEMDgfDGNEGVIVIAATNRSDVLDPALLRPGRFDR 350
Cdd:cd19507  105 -NADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
378-422 1.46e-11

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: 59.47  E-value: 1.46e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 488292233  378 DVDLKVVAQQTPGFAGADLENVLNEAALVAARRNKKKIDASDVDE 422
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
210-423 2.39e-11

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 66.26  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 210 RRFAElgARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFvemfvgvGASRVRDLFETAKKNAPA----IIFI 285
Cdd:PRK13342  28 RRMIE--AGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRSAgrrtILFI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 286 DEIdavgrqrgagmgggHdeReqtLN---Q--LL--VEmdgfDGNegVIVIAAT--NRSDVLDPALLrpgrfDR-QILVG 355
Cdd:PRK13342  99 DEI--------------H--R---FNkaqQdaLLphVE----DGT--ITLIGATteNPSFEVNPALL-----SRaQVFEL 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233 356 RP----DVkgREAILRVHAKNK----PLADDVdLKVVAQqtpgFAGADLENVLNeaALVAARRNKKKIDASDVDEA 423
Cdd:PRK13342 149 KPlseeDI--EQLLKRALEDKErglvELDDEA-LDALAR----LANGDARRALN--LLELAALGVDSITLELLEEA 215
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
223-342 4.69e-11

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 61.39  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFVEMFVGvGASRVRDLFETAKK-NAPAIIFIDEIDAVGRQRgAGMGG 301
Cdd:cd19512   25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-STEKI 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488292233 302 GHDEReQTLNQLLVEMDgfDGNEGVIVIAATNRSDVLDPAL 342
Cdd:cd19512  103 SEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 140
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
223-426 1.88e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISGsdfvemfVGVGASRVRDLFETAKKNA----PAIIFIDEI--------DA 290
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEIhrfnkaqqDA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 291 vgrqrgagmggghdereqtlnqLL--VEmdgfDGNegVIVIAAT--NRSDVLDPALLrpgrfDR-QILVGRP----DVkg 361
Cdd:COG2256  125 ----------------------LLphVE----DGT--ITLIGATteNPSFEVNSALL-----SRcRVFVLKPlseeDL-- 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233 362 REAILRVHA--------KNKPLADDVdLKVVAQqtpgFAGADLENVLN---EAALVAARRNKKKIDASDVDEAEDR 426
Cdd:COG2256  170 EQLLERALAdderglggYKLELDDEA-LEALAR----LADGDARRALNaleLAVLSAPPDGVIEITLELVEEALQR 240
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
214-352 2.63e-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: 56.62  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 214 ELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDFV--------------EMFVGVGASRVRDLFETAKKNA 279
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488292233 280 PAIIFIDEIDAVGRQRgagmgGGHDEREQT------LNQLLVEMDGFDGNEGVIVIAATNRSDVLDPALLRPGRFDRQI 352
Cdd:cd19505   86 PCIIWIPNIHELNVNR-----STQNLEEDPklllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCI 159
PRK04195 PRK04195
replication factor C large subunit; Provisional
185-289 2.96e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.93  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 185 RFSDVAGAEEEKQELVEVVEflkdprrfAELGARIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGSDF-----VEM 259
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE--------SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 488292233 260 FVGvGASRVRDLFETAKKnapaIIFIDEID 289
Cdd:PRK04195  84 VAG-EAATSGSLFGARRK----LILLDEVD 108
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
170-304 1.17e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 55.46  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 170 GKSKAKEADKKANRVRFSDVAGAEEEKQELvevveflkdprrfaelgarIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFY 249
Cdd:cd19498   15 GQDEAKRAVAIALRNRWRRMQLPEELRDEV-------------------TPKNILMIGPTGVGKTEIARRLAKLAGAPFI 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488292233 250 SISGSDFVEM-FVGVGA-SRVRDLFEtakknapAIIFIDEIDAVGRQRGagmGGGHD 304
Cdd:cd19498   76 KVEATKFTEVgYVGRDVeSIIRDLVE-------GIVFIDEIDKIAKRGG---SSGPD 122
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
222-348 8.83e-08

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: 51.52  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  222 GVLLEGPPGTGKTLLAKAVAgEA--GVPFYSISGSDF--VEMFVG------VGASRVRDLFETAKKNApAIIFIDEIDAv 291
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDttEEDLFGrrnidpGGASWVDGPLVRAAREG-EIAVLDEINR- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  292 grqrgagmggGHDEREQTLNQLLVE-----MDGF----DGNEGVIVIAATNRSD----VLDPALLRpgRF 348
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDErrlllPDGGelvkAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
193-427 1.06e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 54.85  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 193 EEEKQELVEVVEFLKDPRRfaelgariPAGVLLEGPPGTGKTLLAKAV-------AGEAGVPF-------------YSI- 251
Cdd:COG1474   32 EEEIEELASALRPALRGER--------PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVrvvyvncrqastrYRVl 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 252 --------SGSDFVEmfVGVGASRVRDLFETA--KKNAPAIIFIDEIDAVgrqrgagmggGHDEREQTLNQLLVEMDGFD 321
Cdd:COG1474  104 srileelgSGEDIPS--TGLSTDELFDRLYEAldERDGVLVVVLDEIDYL----------VDDEGDDLLYQLLRANEELE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 322 GNE-GVIVIaaTNRSDV---LDPAL---LRPG--RFD-------RQILVGR------PDVKGREAILRVhaknkplADdv 379
Cdd:COG1474  172 GARvGVIGI--SNDLEFlenLDPRVkssLGEEeiVFPpydadelRDILEDRaelafyDGVLSDEVIPLI-------AA-- 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488292233 380 dlkvVAQQTPGFA--GADLenvLNEAALVAARRNKKKIDASDVDEAEDRV 427
Cdd:COG1474  241 ----LAAQEHGDArkAIDL---LRVAGEIAEREGSDRVTEEHVREAREKI 283
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
26-126 1.45e-07

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 49.91  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233   26 YFIFGNNNQQSPDIDYSTFQQQLEDGKVKDMTIQPTNGVYRIEGQYKEKQEVKDTgglslwgstqassKGFTTTVLPSDT 105
Cdd:pfam06480  16 LLFLLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFT-------------TYFIPSLPNVDS 82
                          90       100
                  ....*....|....*....|.
gi 488292233  106 TLAGIQDAAQNNKVKLVVKEQ 126
Cdd:pfam06480  83 LLEKLEDALEEKGVKVSVKPP 103
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
223-410 2.25e-07

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: 53.25  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISG------------SDFVEMFvgvGASRVRD--LFETakknapaIIFIDEI 288
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpsdilgtYIYDQQT---GEFEFRPgpLFAN-------VLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 289 DavgrqRGagmggghdeREQTLNQLL-------VEMDG--FDGNEGVIVIAATNRSDV-----LDPALLRpgRFDRQILV 354
Cdd:COG0714  104 N-----RA---------PPKTQSALLeameerqVTIPGgtYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYI 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233 355 GRPDVKGREAILRVHAknkpladdvdlkvvaqqtpGFAGADLENVLNEAALVAARR 410
Cdd:COG0714  168 GYPDAEEEREILRRHT-------------------GRHLAEVEPVLSPEELLALQE 204
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
223-339 4.72e-07

RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 49.04  E-value: 4.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEA---GVPFYSISgsdFVEMFVgvgaSRVRDLfetAKKNAPAIIFIDEIDAVGRQRGAgm 299
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDL---IEEKKLDIIIIDSLSSLARASQG-- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488292233 300 ggghDEREQTLNQLLVEMDGFdGNEGVIVIAATNRSDVLD 339
Cdd:cd01120   69 ----DRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI 103
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
179-293 9.15e-07

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: 49.86  E-value: 9.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 179 KKANRVRFSDVAGAEEEKQElveVVEFLKDPRRFAELGARIpagVLLEGPPGTGKTLLAKAVAGEAGVPFYSIS-G--SD 255
Cdd:cd19500    2 KKARKVLDADHYGLEDVKER---ILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRD 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488292233 256 FVEM------FVGVGASRVRDLFETAKKNAPaIIFIDEIDAVGR 293
Cdd:cd19500   76 EAEIrghrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
223-342 1.92e-06

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: 48.98  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGV---------------------PFYSISGSDFVEMFvgvgaSRVRDLFEtaKKNAPA 281
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELID--DKDALV 127
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488292233 282 IIFIDEIDAVGRQRGAgMGGGHDERE--QTLNQLLVEMDGFDGNEGVIVIAATNRSDVLDPAL 342
Cdd:cd19508  128 FVLIDEVESLAAARSA-SSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
223-288 3.64e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.74  E-value: 3.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISG------SDFVEMFVGVGAsrvRDlfetakknapaIIFIDEI 288
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI 111
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
222-256 1.48e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.04  E-value: 1.48e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 488292233 222 GVLLEGPPGTGKTLLAKAVAGEAG--VPFYSISGSDF 256
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
222-256 1.89e-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: 1.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 488292233  222 GVLLEGPPGTGKTLLAKAVAGEAG--VPFYSISGSDF 256
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
223-288 2.95e-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: 44.80  E-value: 2.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488292233  223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISG------SDFVEMFVGVGAsrvRDlfetakknapaIIFIDEI 288
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpaierpGDLAAILTNLEP---GD-----------VLFIDEI 93
44 PHA02544
clamp loader, small subunit; Provisional
218-292 3.59e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 46.52  E-value: 3.59e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488292233 218 RIPAGVLLEGPPGTGKTLLAKAVAGEAGVPFYSISGS----DFVEMFVGVGASRVrdlfeTAKKNAPAIIfIDEIDAVG 292
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-----SLTGGGKVII-IDEFDRLG 113
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
191-352 3.98e-05

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: 46.76  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  191 GAEEEKQELVEVVEFLKDPRRFAELGARIPAG---VLLEGPPGTGKTLLAKAVAGE-AGVPFYS------ISGSDFVEMF 260
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTsnhMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  261 VGVGASRVRDLFETAkknAPAIIFIDEIDAVGRQRGagmGGGHDEREQTLNQLLVEMDGfDGNEGVIVIAATnrSDVLDP 340
Cdd:TIGR03922 360 IGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGY---GQKDPFGLEAIDTLLARMEN-DRDRLVVIGAGY--RKDLDK 430
                         170
                  ....*....|....*..
gi 488292233  341 AL-----LRpGRFDRQI 352
Cdd:TIGR03922 431 FLevnegLR-SRFTRVI 446
Sigma54_activat pfam00158
Sigma-54 interaction domain;
206-288 4.27e-05

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 44.70  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  206 LKDPRRFAELGARIPAGVLLEGPPGTGKTLLAKAV---AGEAGVPFYSISGSDFV------EMFvGV------GASRVRD 270
Cdd:pfam00158   8 MQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIhqlSPRADGPFVAVNCAAIPeellesELF-GHekgaftGADSDRK 86
                          90
                  ....*....|....*....
gi 488292233  271 -LFETAKKnapAIIFIDEI 288
Cdd:pfam00158  87 gLFELADG---GTLFLDEI 102
PTZ00121 PTZ00121
MAEBL; Provisional
579-716 4.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  579 QEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFETGKMpegADSDYPSEKEAQTFEEAKRALEEK- 657
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEAKKAEEAKKKAEEAk 1470
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488292233  658 ---EAQKQVEEKQDFEEAKKelhdEAEEVKVESEQTEKEVQSEEKKDSDSNSEYDRNNYEDR 716
Cdd:PTZ00121 1471 kadEAKKKAEEAKKADEAKK----KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
223-289 1.43e-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: 42.95  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  223 VLLEGPPGTGKTLLAKAVAGEAGV---PFYSISGSDFVE-----MFVG-----VGASRVRDLFETAKKNAPAIIFIDEID 289
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
186-242 3.44e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 42.52  E-value: 3.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  186 FSDVAGaeeekQELVevveflkdpRRFAELGAripAG---VLLEGPPGTGKTLLAKAVAG 242
Cdd:pfam01078   2 LADVKG-----QEQA---------KRALEIAA---AGghnLLMIGPPGSGKTMLAKRLPG 44
PTZ00121 PTZ00121
MAEBL; Provisional
601-718 4.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  601 EQHKLIAEKLLEYETLDAKAIKSLFETGKMPEGADSDypSEKEAQTFEEAKRALEEK----EAQKQVEEKQDFEEAKKEL 676
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKADELKKAAAAKkkadEAKKKAEEKKKADEAKKKA 1440
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 488292233  677 HD--EAEEVKVESEQTEKEVQSEEKKDSDSNSEYDRNNYEDRYK 718
Cdd:PTZ00121 1441 EEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
PTZ00121 PTZ00121
MAEBL; Provisional
579-707 4.93e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  579 QEVRRILMDAHTKAHEIIEAHR--EQHKLIAEKLLEYETLDAKAIKSLFETGKMPEGADSDYPSE-KEAQTFEEAKRALE 655
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKkaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEE 1288
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488292233  656 EKEAQ--KQVEEKQDFEEAKK---------ELHDEAEEVKVESEQTEKEVQSEEKKDSDSNSE 707
Cdd:PTZ00121 1289 KKKADeaKKAEEKKKADEAKKkaeeakkadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
PTZ00121 PTZ00121
MAEBL; Provisional
591-703 5.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  591 KAHEIIEAHREQHKLIAEKL--LEYETLDAKAIKSLFETGKMPEGADSDYPSEK----EAQTFEEAKRALEEKEAQKQVE 664
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaeELKKAEEENKIKAAEEAKKAEE 1672
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 488292233  665 EKQDFEEAKKELHDE---AEEVKVESEQTEK-----EVQSEEKKDSD 703
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEkkaAEALKKEAEEAKKaeelkKKEAEEKKKAE 1719
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
223-294 5.10e-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: 42.67  E-value: 5.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488292233  223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISG------SDFVEMFVGVGAsrvRDlfetakknapaIIFIDEIDAVGRQ 294
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEIHRLSPA 96
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
186-242 5.63e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.11  E-value: 5.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 186 FSDVAGaeeekQELVevveflkdpRRFAELGAripAG---VLLEGPPGTGKTLLAKAVAG 242
Cdd:COG0606  191 LADVKG-----QEQA---------KRALEIAA---AGghnLLMIGPPGSGKTMLARRLPG 233
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
223-253 6.44e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.38  E-value: 6.44e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGVPFYSISG 253
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
223-288 7.10e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.83  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKT----LLAKAVAGEAG-----VPFY-SISGSDFVEMFVGVGAS---RVRD-LF----ETAKKN--APAI 282
Cdd:COG1401  224 VILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpSWSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNpdKPYV 303

                 ....*.
gi 488292233 283 IFIDEI 288
Cdd:COG1401  304 LIIDEI 309
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
223-293 1.66e-03

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 40.66  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 223 VLLEGPPGTGKTLLAKAVAGEAGVPFySIS-----------GSDfVEmfvgvgaSRVRDLFETAKKNAPA----IIFIDE 287
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPF-AIAdattlteagyvGED-VE-------NILLKLLQAADYDVERaqrgIVYIDE 123

                 ....*.
gi 488292233 288 IDAVGR 293
Cdd:cd19497  124 IDKIAR 129
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
206-289 1.73e-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: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 206 LKDPRRfaelgariPAGVLL-EGPPGTGKTLLAKAVAGE---AGVPFYSISGSDFVEMFVG----------VGASRVRDL 271
Cdd:cd19499   34 LSDPNR--------PIGSFLfLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHSVsrligappgyVGYTEGGQL 105
                         90
                 ....*....|....*...
gi 488292233 272 FETAKKNAPAIIFIDEID 289
Cdd:cd19499  106 TEAVRRKPYSVVLLDEIE 123
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
218-290 1.92e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 40.73  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 218 RIPAGVLLEGPPGTGKTLLAKAVAGE---------------AGVPFYSISGSDFVEMFVGV-----GASRVRDLFETAKK 277
Cdd:COG0470   16 RLPHALLLHGPPGIGKTTLALALARDllcenpeggkacgqcHSRLMAAGNHPDLLELNPEEksdqiGIDQIRELGEFLSL 95
                         90
                 ....*....|....*..
gi 488292233 278 NAPA----IIFIDEIDA 290
Cdd:COG0470   96 TPLEggrkVVIIDEADA 112
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
195-344 2.04e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 41.71  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 195 EKQELVEVVEFLKDPRRFaelgaripagVLLEGPPGTGKTLLAKAVA---------GEAGVPFY--------SISGSDFV 257
Cdd:COG5635  165 ERIESLKRLELLEAKKKR----------LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdlaeEASLEDLL 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 258 EMFVGVGASRVRDLFETAKKNAPAIIFIDEIDAVGRQrgagmggghDEREQTLNQLLVEMDGFDGNEGVIviaaTNRSDV 337
Cdd:COG5635  235 AEALEKRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII----TSRPEG 301

                 ....*..
gi 488292233 338 LDPALLR 344
Cdd:COG5635  302 YDSSELE 308
PTZ00121 PTZ00121
MAEBL; Provisional
586-703 2.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  586 MDAHTKAHEIIEAHREQHKLIAEKLLEY--ETLDAKAIKSLFETGKmpEGADSDYPSEKEAQTFEEAKRALEEK----EA 659
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKaeEKKKADEAKKKAEEDK--KKADELKKAAAAKKKADEAKKKAEEKkkadEA 1436
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 488292233  660 QKQVEEKQDFEEAKKELHD--EAEEVKVESEQTEK----EVQSEEKKDSD 703
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKKadeaKKKAEEAKKAD 1486
PTZ00121 PTZ00121
MAEBL; Provisional
587-701 2.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  587 DAHTKAHEIIEAHREQHKliAEKLLEYETLDAKAIKSLFETGKMPEGADSDYPSEKEAQTFEEAKRALEEK----EAQKQ 662
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKK--ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadEAKKK 1452
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 488292233  663 VEEKQDFEEAKKELHD--EAEEVKVESEQTEKEVQSEEKKD 701
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEakKADEAKKKAEEAKKADEAKKKAE 1493
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
626-707 2.25e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  626 ETGKMPEGADSDYPSEKEaQTFEEAKRALEekeaQKQVEEKQDFEEAKKELHDEAEEVKVESEQTEKEvqsEEKKDSDSN 705
Cdd:pfam05262 256 EAKNLPKPADTSSPKEDK-QVAENQKREIE----KAQIEIKKNDEEALKAKDHKAFDLKQESKASEKE---AEDKELEAQ 327

                  ..
gi 488292233  706 SE 707
Cdd:pfam05262 328 KK 329
PTZ00121 PTZ00121
MAEBL; Provisional
587-715 2.83e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  587 DAHTKAHEIIEAHREQHKLIAEKLLEYETL-DAKAIKSLFETGKMpEGADSDYPSEKEAQTFEEAKRALEEK-----EAQ 660
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKI-KAAEEAKKAEEDKKKAEEAKKAEEDEkkaaeALK 1695
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488292233  661 KQVEEKQDFEEAKKElhdEAEEV-KVESEQTEKEVQSEEKKDSDSNSEYDRNNYED 715
Cdd:PTZ00121 1696 KEAEEAKKAEELKKK---EAEEKkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
PTZ00121 PTZ00121
MAEBL; Provisional
565-712 3.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  565 QTKAYSEQVAFEidQEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIkslfETGKMPEGADSDYPSEKEA 644
Cdd:PTZ00121 1617 EAKIKAEELKKA--EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDEKKA 1690
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  645 QtfEEAKRALEEKEAQKQVEEKQDfEEAKK--ELHDEAEEVKVESEQTEKEVQSEEKKDSDSNSEYDRNN 712
Cdd:PTZ00121 1691 A--EALKKEAEEAKKAEELKKKEA-EEKKKaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
PTZ00121 PTZ00121
MAEBL; Provisional
579-718 3.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  579 QEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKSLFETGKMPEGADSDYPSEKEAQTFEEAKRALEE-- 656
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdk 1404
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488292233  657 ---KEAQKQVEEKQDFEEAKKELHD--EAEEVKVESEQTEKEVQSEEKKDSDSNSEYDRNNYEDRYK 718
Cdd:PTZ00121 1405 kkaDELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
634-703 4.13e-03

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 39.58  E-value: 4.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  634 ADSDYPSEKEAQTFEEAKRALEEKEAQKQVEEKQDFEEAKKELHDEAEEVKVESEQTEKEVQSEEKKDSD 703
Cdd:pfam08597  39 AEEEEEEEKEKAAKAAAAKAKKKKKSKKQKIAEKEAERKAEEEAEEEEELTPEDEAARKLRLRKAEEESD 108
PTZ00121 PTZ00121
MAEBL; Provisional
587-703 4.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233  587 DAHTKAHEIIEAhrEQHKLIAEKLLEYETLDAKA-----IKSLFETGKMPEGADSDYPSEKEAQTFEEAKRALEE----- 656
Cdd:PTZ00121 1422 EAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAeeakkAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkka 1499
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 488292233  657 KEAQKQVEEKQDFEEAKK-ELHDEAEEVKV--ESEQTEKEVQSEEKKDSD 703
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKaEEAKKADEAKKaeEAKKADEAKKAEEKKKAD 1549
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
208-258 5.02e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 39.35  E-value: 5.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488292233  208 DPRRFAELGA----RIPAGVLLEGPPGTGKTLLAKAVAGEA---GVPFYSISGSDFVE 258
Cdd:pfam01695  76 DQRIVAELASlsfiDRAQNVVLLGPPGVGKTHLAIALGVEAcraGYSVRFTSAADLVN 133
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
182-245 5.25e-03

Protein of unknown function (DUF815); This family consists of several bacterial proteins of unknown function.


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 39.44  E-value: 5.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488292233  182 NRVRFSDVAGAEEEKQELVEvveflkDPRRFAElGAriPA-GVLLEGPPGTGKTLLAKAVAGEAG 245
Cdd:pfam05673  23 DPVRLDDLVGIERQKEALIR------NTRRFLA-GL--PAnNVLLWGARGTGKSSLVKALLNEYA 78
TsaE pfam02367
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ...
210-247 6.70e-03

Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).


Pssm-ID: 460540  Cd Length: 127  Bit Score: 37.41  E-value: 6.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 488292233  210 RRFAE-LGARIPAG--VLLEGPPGTGKTLLAKAVAGEAGVP 247
Cdd:pfam02367   8 EALGKrLAALLKPGdvILLSGDLGAGKTTFTRGLARGLGVT 48
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
567-701 9.23e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488292233 567 KAYSEQVAfEIDQEVRRILMDAHTKAHEIIEAHREQHKLIAEKLLEYETLDAKAIKslfetgkmpegadsdypsEKEAQt 646
Cdd:PRK00409 551 EELEEKKE-KLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK------------------AHELI- 610
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488292233 647 feEAKRALeeKEAQKQVEEKQDFEEAKKELHDEAEEVKVESEQTEKEVQSEEKKD 701
Cdd:PRK00409 611 --EARKRL--NKANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDK 661
 
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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