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Conserved domains on  [gi|1907130708|ref|XP_036017167|]
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AFG3-like protein 2 isoform X2 [Mus musculus]

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];
1-498 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 786.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   1 MGSFLLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFKDVAGCEEAKLEIMEFVNFLK 79
Cdd:COG0465    90 LLSLLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFDDVAGVDEAKEELQEIVDFLK 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  80 NPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDE 159
Cdd:COG0465   163 DPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDE 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 160 IDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFK 239
Cdd:COG0465   243 IDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILK 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 240 VHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEK 319
Cdd:COG0465   323 VHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEK 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 320 KTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQ 398
Cdd:COG0465   399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGAS 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 399 DDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVRILISDAYRRTVALLTEKKAD 473
Cdd:COG0465   479 NDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDK 558
                         490       500
                  ....*....|....*....|....*
gi 1907130708 474 VEKVALLLLEKEVLDKNDMVQLLGP 498
Cdd:COG0465   559 LDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
1-498 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 786.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   1 MGSFLLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFKDVAGCEEAKLEIMEFVNFLK 79
Cdd:COG0465    90 LLSLLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFDDVAGVDEAKEELQEIVDFLK 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  80 NPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDE 159
Cdd:COG0465   163 DPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDE 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 160 IDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFK 239
Cdd:COG0465   243 IDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILK 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 240 VHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEK 319
Cdd:COG0465   323 VHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEK 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 320 KTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQ 398
Cdd:COG0465   399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGAS 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 399 DDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVRILISDAYRRTVALLTEKKAD 473
Cdd:COG0465   479 NDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDK 558
                         490       500
                  ....*....|....*....|....*
gi 1907130708 474 VEKVALLLLEKEVLDKNDMVQLLGP 498
Cdd:COG0465   559 LDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
4-497 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: 729.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   4 FLLSMLPTVLIIAFLLYTIRRGPAGIGrtgrgmGGLFSVGETTAKVLKDE-IDVKFKDVAGCEEAKLEIMEFVNFLKNPK 82
Cdd:TIGR01241   5 FLFSLLPPILLLVGVWFFFRRQMQGGG------GRAFSFGKSKAKLLNEEkPKVTFKDVAGIDEAKEELMEIVDFLKNPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  83 QYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDA 162
Cdd:TIGR01241  79 KFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 163 VGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHL 242
Cdd:TIGR01241 159 VGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 243 RPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTV 322
Cdd:TIGR01241 239 KNKKLAPDVDLKAVAR----RTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 323 AYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDL 401
Cdd:TIGR01241 315 AYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 402 RKVTQSAYAQIVQFGMNEKVGQISFDlPRQGDMVL------EKPYSEATARMIDDEVRILISDAYRRTVALLTEKKADVE 475
Cdd:TIGR01241 395 KQATNIARAMVTEWGMSDKLGPVAYG-SDGGDVFLgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELE 473
                         490       500
                  ....*....|....*....|..
gi 1907130708 476 KVALLLLEKEVLDKNDMVQLLG 497
Cdd:TIGR01241 474 LLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
3-508 1.44e-180

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 523.07  E-value: 1.44e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   3 SFLLsmLPtVLIIAFLLYTIRRG---PAGIGRtgrgmgGLFSVGETTAKVLKD-EIDVKFKDVAGCEEAKLEIMEFVNFL 78
Cdd:CHL00176  132 SNLL--LP-LILIGVLWFFFQRSsnfKGGPGQ------NLMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  79 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 158
Cdd:CHL00176  203 KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFID 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 159 EIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIF 238
Cdd:CHL00176  283 EIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 239 KVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEkKTQVLQPEE 318
Cdd:CHL00176  363 KVHARNKKLSPDVSLELIARR----TPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKN 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 319 KKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLP-KEQYLYTKEQLLDRMCMTLGGRVSEEIFFG--RITT 395
Cdd:CHL00176  438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTT 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 396 GAQDDLRKVTQSAYAQIVQFGMNeKVGQISFDLPRQGD------MVLEKPYSEATARMIDDEVRILISDAYRRTVALLTE 469
Cdd:CHL00176  518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1907130708 470 KKADVEKVALLLLEKEVLDKNDMVQLLGPR-PFTEKSTYE 508
Cdd:CHL00176  597 NRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
56-226 1.72e-117

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: 344.22  E-value: 1.72e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  56 VKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 135
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 136 GPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALL 215
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1907130708 216 RPGRFDRQIFI 226
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
313-495 4.89e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 269.47  E-value: 4.89e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 313 VLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYTKEQLLDRMCMTLGGRVSEEIFFG 391
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 392 RITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDlPRQG------DMVLEKPYSEATARMIDDEVRILISDAYRRTVA 465
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907130708 466 LLTEKKADVEKVALLLLEKEVLDKNDMVQL 495
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
92-230 1.82e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.42  E-value: 1.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   92 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDLFALARKNAPCI 154
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907130708  155 LFIDEIDAVGRKRgrgnfggqSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPgRFDRQIFIGPPD 230
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
1-498 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 786.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   1 MGSFLLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFKDVAGCEEAKLEIMEFVNFLK 79
Cdd:COG0465    90 LLSLLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFDDVAGVDEAKEELQEIVDFLK 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  80 NPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDE 159
Cdd:COG0465   163 DPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDE 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 160 IDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFK 239
Cdd:COG0465   243 IDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILK 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 240 VHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEK 319
Cdd:COG0465   323 VHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEK 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 320 KTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQ 398
Cdd:COG0465   399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGAS 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 399 DDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVRILISDAYRRTVALLTEKKAD 473
Cdd:COG0465   479 NDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDK 558
                         490       500
                  ....*....|....*....|....*
gi 1907130708 474 VEKVALLLLEKEVLDKNDMVQLLGP 498
Cdd:COG0465   559 LDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
4-497 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: 729.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   4 FLLSMLPTVLIIAFLLYTIRRGPAGIGrtgrgmGGLFSVGETTAKVLKDE-IDVKFKDVAGCEEAKLEIMEFVNFLKNPK 82
Cdd:TIGR01241   5 FLFSLLPPILLLVGVWFFFRRQMQGGG------GRAFSFGKSKAKLLNEEkPKVTFKDVAGIDEAKEELMEIVDFLKNPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  83 QYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDA 162
Cdd:TIGR01241  79 KFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 163 VGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHL 242
Cdd:TIGR01241 159 VGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 243 RPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTV 322
Cdd:TIGR01241 239 KNKKLAPDVDLKAVAR----RTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 323 AYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDL 401
Cdd:TIGR01241 315 AYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 402 RKVTQSAYAQIVQFGMNEKVGQISFDlPRQGDMVL------EKPYSEATARMIDDEVRILISDAYRRTVALLTEKKADVE 475
Cdd:TIGR01241 395 KQATNIARAMVTEWGMSDKLGPVAYG-SDGGDVFLgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELE 473
                         490       500
                  ....*....|....*....|..
gi 1907130708 476 KVALLLLEKEVLDKNDMVQLLG 497
Cdd:TIGR01241 474 LLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
3-508 1.44e-180

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 523.07  E-value: 1.44e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   3 SFLLsmLPtVLIIAFLLYTIRRG---PAGIGRtgrgmgGLFSVGETTAKVLKD-EIDVKFKDVAGCEEAKLEIMEFVNFL 78
Cdd:CHL00176  132 SNLL--LP-LILIGVLWFFFQRSsnfKGGPGQ------NLMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  79 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 158
Cdd:CHL00176  203 KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFID 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 159 EIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIF 238
Cdd:CHL00176  283 EIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 239 KVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEkKTQVLQPEE 318
Cdd:CHL00176  363 KVHARNKKLSPDVSLELIARR----TPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKN 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 319 KKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLP-KEQYLYTKEQLLDRMCMTLGGRVSEEIFFG--RITT 395
Cdd:CHL00176  438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTT 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 396 GAQDDLRKVTQSAYAQIVQFGMNeKVGQISFDLPRQGD------MVLEKPYSEATARMIDDEVRILISDAYRRTVALLTE 469
Cdd:CHL00176  518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1907130708 470 KKADVEKVALLLLEKEVLDKNDMVQLLGPR-PFTEKSTYE 508
Cdd:CHL00176  597 NRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
1-520 1.15e-162

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 477.60  E-value: 1.15e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   1 MGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRtgrgmgGLFSVGETTAKVL-KDEIDVKFKDVAGCEEAKLEIMEFVNFLK 79
Cdd:PRK10733   99 LASIFISWFPMLLLIGVWIFFMRQMQGGGGK------GAMSFGKSKARMLtEDQIKTTFADVAGCDEAKEEVAELVEYLR 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  80 NPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDE 159
Cdd:PRK10733  173 EPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDE 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 160 IDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFK 239
Cdd:PRK10733  253 IDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILK 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 240 VHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEK 319
Cdd:PRK10733  333 VHMRRVPLAPDIDAAIIARG----TPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQK 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 320 KTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTL-GGRVSEEIFFG--RITTG 396
Cdd:PRK10733  409 ESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLyGGRLAEEIIYGpeHVSTG 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 397 AQDDLRKVTQSAYAQIVQFGMNEKVGQISFdLPRQGDMVL------EKPYSEATARMIDDEVRILISDAYRRTVALLTEK 470
Cdd:PRK10733  489 ASNDIKVATNLARNMVTQWGFSEKLGPLLY-AEEEGEVFLgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDN 567
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907130708 471 KADVEKVALLLLEKEVLDKNDMVQLLGPRPFTEKSTYEEfVEGTGSLDED 520
Cdd:PRK10733  568 MDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEE-PGASNNSDDN 616
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
56-226 1.72e-117

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: 344.22  E-value: 1.72e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  56 VKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 135
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 136 GPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALL 215
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1907130708 216 RPGRFDRQIFI 226
Cdd:cd19501   161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
55-311 3.99e-112

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 336.59  E-value: 3.99e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFV-NFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 133
Cdd:COG1222    74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 213
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 214 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 293
Cdd:COG1222   232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAK----LTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307
                         250
                  ....*....|....*...
gi 1907130708 294 KHFEQAIERVIGGLEKKT 311
Cdd:COG1222   308 EDLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
55-310 2.02e-95

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 295.97  E-value: 2.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 133
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 213
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 214 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 293
Cdd:PRK03992  287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAE----LTEGASGADLKAICTEAGMFAIRDDRTEVTM 362
                         250
                  ....*....|....*..
gi 1907130708 294 KHFEQAIERVIGGLEKK 310
Cdd:PRK03992  363 EDFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
313-495 4.89e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 269.47  E-value: 4.89e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 313 VLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYTKEQLLDRMCMTLGGRVSEEIFFG 391
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 392 RITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDlPRQG------DMVLEKPYSEATARMIDDEVRILISDAYRRTVA 465
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907130708 466 LLTEKKADVEKVALLLLEKEVLDKNDMVQL 495
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
55-304 2.10e-80

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: 256.26  E-value: 2.10e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 133
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 213
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 214 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 293
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAK----MTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 1907130708 294 KHFEQAIERVI 304
Cdd:TIGR01242 354 DDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
58-303 3.00e-78

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: 251.75  E-value: 3.00e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  58 FKDVAGCEEAKLEIMEFVN-FLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 136
Cdd:COG0464   156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 137 PARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQentLNQLLVEMDGFntTTNVVILAGTNRPDILDPALLR 216
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRV---VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 217 pgRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHF 296
Cdd:COG0464   311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEA----TEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384

                  ....*..
gi 1907130708 297 EQAIERV 303
Cdd:COG0464   385 LEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
48-309 5.95e-71

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 241.35  E-value: 5.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  48 KVLKDEIDVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGS 126
Cdd:TIGR01243 442 EVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 127 EFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNR 206
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNR 599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 207 PDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARH 286
Cdd:TIGR01243 600 PDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEM----TEGYTGADIEAVCREAAMAALRE 675
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907130708 287 LSDA------------------INEKHFEQAIERVIGGLEK 309
Cdd:TIGR01243 676 SIGSpakeklevgeeeflkdlkVEMRHFLEALKKVKPSVSK 716
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
58-224 9.81e-69

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: 219.13  E-value: 9.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  58 FKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 136
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 137 PARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLR 216
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                  ....*...
gi 1907130708 217 PGRFDRQI 224
Cdd:cd19502   162 PGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
55-304 6.55e-65

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 216.94  E-value: 6.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 133
Cdd:PTZ00454  141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 213
Cdd:PTZ00454  221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 214 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALE-KDKLARklaslTPGFSGADVANVCNEAALIAARHLSDAIN 292
Cdd:PTZ00454  301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDlEDFVSR-----PEKISAADIAAICQEAGMQAVRKNRYVIL 375
                         250
                  ....*....|..
gi 1907130708 293 EKHFEQAIERVI 304
Cdd:PTZ00454  376 PKDFEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
49-304 1.64e-62

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 211.55  E-value: 1.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  49 VLKDEIDV-------------KFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAG 114
Cdd:PTZ00361  160 ILLDEVDPlvsvmkvdkapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVAN 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 115 EANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNT 194
Cdd:PTZ00361  240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDS 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 195 TTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKL--DSALE-----KDKLarklasltpgf 267
Cdd:PTZ00361  320 RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLaeDVDLEefimaKDEL----------- 388
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907130708 268 SGADVANVCNEAALIAARHLSDAINEKHFEQAIERVI 304
Cdd:PTZ00361  389 SGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVL 425
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
55-287 1.26e-61

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 215.93  E-value: 1.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 133
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQEnTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 213
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVEKR-VVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907130708 214 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRplklDSALEKDKLARKLASLTPGFSGADVANVCNEAALIAARHL 287
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTR----NMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRF 400
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
67-226 3.20e-61

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: 199.05  E-value: 3.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  67 AKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 146
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 147 ARKNAPCILFIDEIDAVGRKRGRGnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 226
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSS--GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
58-302 3.20e-61

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 202.04  E-value: 3.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  58 FKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 137
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 138 ARVRDLFALARkNAPCILFIDEIDAVGRKRGRGNFGGqsEQENTLNQLLVEMDGFNttTNVVILAGTNRPDILDPALLRp 217
Cdd:COG1223    81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 218 gRFDRQIFIGPPDIKGRASIFKVHLRPLKldsaLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFE 297
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFP----LPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229

                  ....*
gi 1907130708 298 QAIER 302
Cdd:COG1223   230 EALKQ 234
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
67-226 1.36e-60

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: 197.51  E-value: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  67 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFA 145
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 146 LARKNAPCILFIDEIDAVGRKRGrGNFGGQSeQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 225
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRG-QSDSSGV-TDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                  .
gi 1907130708 226 I 226
Cdd:cd19511   159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
60-226 3.49e-57

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: 188.65  E-value: 3.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 138
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 139 RVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRP 217
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                  ....*....
gi 1907130708 218 GRFDRQIFI 226
Cdd:cd19503   157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
67-226 9.78e-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: 181.92  E-value: 9.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  67 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFA 145
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 146 LARKNAPCILFIDEIDAVGRKRGRGnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 225
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGTT--GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                  .
gi 1907130708 226 I 226
Cdd:cd19529   159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
68-226 2.19e-53

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: 178.47  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  68 KLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 146
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 147 ARKNAPCILFIDEIDAVGRKRGrGNFGGQS-EQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 225
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARG-GNIGDAGgAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                  .
gi 1907130708 226 I 226
Cdd:cd19528   161 I 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
96-227 2.68e-52

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 174.32  E-value: 2.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfGGQ 175
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907130708 176 SEQENTLNQLLVEMDGF-NTTTNVVILAGTNRPDILDPALLrpGRFDRQIFIG 227
Cdd:pfam00004  79 SESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
60-227 5.51e-50

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 169.54  E-value: 5.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 138
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 139 RVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQEnTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPG 218
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                  ....*....
gi 1907130708 219 RFDRQIFIG 227
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
72-226 1.08e-49

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: 168.82  E-value: 1.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  72 MEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNA 151
Cdd:cd19530    10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907130708 152 PCILFIDEIDAVGRKRGRgnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 226
Cdd:cd19530    90 PCVIFFDEVDALVPKRGD---GGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
60-224 4.72e-46

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: 159.11  E-value: 4.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNFLKNPKQ-YQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 138
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 139 RVRDLFALARKNAPCILFIDEIDAVGRKRGrgnfGGQSEQENTL-NQLLVEMDGFN----TTTNVVILAGTNRPDILDPA 213
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRE----SAQREMERRIvSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                         170
                  ....*....|.
gi 1907130708 214 LLRPGRFDRQI 224
Cdd:cd19518   157 LRRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
79-225 4.55e-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: 156.43  E-value: 4.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  79 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 158
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907130708 159 EIDAVGRKRGRGNFGgqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 225
Cdd:cd19526    94 EFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
68-226 2.54e-41

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: 146.12  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  68 KLEIMEFVNF-LKNPKQYQDlGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 146
Cdd:cd19527     2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 147 ARKNAPCILFIDEIDAVGRKRGR-GNFGGQSEQenTLNQLLVEMDGFNTTT-NVVILAGTNRPDILDPALLRPGRFDRQI 224
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                  ..
gi 1907130708 225 FI 226
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 ...
61-226 9.35e-38

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: 136.71  E-value: 9.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  61 VAGCEEAKLEIMEFVNF-LKNPKQYQdLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 139
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 140 VRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTN--VVILAGTNRPDILDPALLR 216
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155
                         170
                  ....*....|
gi 1907130708 217 pgRFDRQIFI 226
Cdd:cd19509   156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
55-226 2.60e-34

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 127.67  E-value: 2.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 132
Cdd:cd19521     3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 133 VGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGF-NTTTNVVILAGTNRPDIL 210
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIkTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                         170
                  ....*....|....*.
gi 1907130708 211 DPALLRpgRFDRQIFI 226
Cdd:cd19521   157 DSAIRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
60-220 1.28e-31

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 119.84  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLG-AKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 137
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 138 ARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfggqSEQENTL---NQLLVEMDGFNTTTN--VVILAGTNRPDILDP 212
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDE 154
                         170
                  ....*....|
gi 1907130708 213 ALLR--PGRF 220
Cdd:cd19520   155 AILRrmPKRF 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
60-225 1.59e-31

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: 119.92  E-value: 1.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEAN-----VPFITVSGSEFLEMFV 133
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfggQSEQENT----LNQLLVEMDGFNTTTNVVILAGTNRPDI 209
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                         170
                  ....*....|....*.
gi 1907130708 210 LDPALLRPGRFDRQIF 225
Cdd:cd19517   154 LDPALRRPGRFDREFY 169
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
55-226 7.54e-31

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 118.55  E-value: 7.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 133
Cdd:cd19525    18 PINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 134 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfgGQSEQENTL---NQLLVEMDGFNTTTN--VVILAGTNRPD 208
Cdd:cd19525    97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR------GEGEHESSRrikTEFLVQLDGATTSSEdrILVVGATNRPQ 170
                         170
                  ....*....|....*...
gi 1907130708 209 ILDPALLRpgRFDRQIFI 226
Cdd:cd19525   171 EIDEAARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
81-226 2.14e-29

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 114.12  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  81 PKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANV--PFItVSGSEFLEMFVGVGPARVRDLFALA-----RKNAPC 153
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAeeeqrRLGANS 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907130708 154 ---ILFIDEIDAVGRKRGRGNfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 226
Cdd:cd19504   103 glhIIIFDEIDAICKQRGSMA-GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
60-226 2.40e-29

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: 113.93  E-value: 2.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 137
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 138 ARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfGGQSEQENTL---NQLLVEMDGF-NTTTN------VVILAGTNRP 207
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR-----GTSEEHEASRrvkSELLVQMDGVgGASENddpskmVMVLAATNFP 153
                         170
                  ....*....|....*....
gi 1907130708 208 DILDPALLRpgRFDRQIFI 226
Cdd:cd19522   154 WDIDEALRR--RLEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
60-226 9.76e-29

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: 111.87  E-value: 9.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 138
Cdd:cd19524     1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 139 RVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTN--VVILAGTNRPDILDPALL 215
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155
                         170
                  ....*....|.
gi 1907130708 216 RpgRFDRQIFI 226
Cdd:cd19524   156 R--RFTKRVYV 164
ycf46 CHL00195
Ycf46; Provisional
55-294 1.18e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 119.35  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  55 DVKFKDVAGCEEAKleimEFVNFLKN--PKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 132
Cdd:CHL00195  224 NEKISDIGGLDNLK----DWLKKRSTsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 133 VGVGPARVRDLFALARKNAPCILFIDEID-AVGRKRGRGNFGGQSEQENTLNQLLVEmdgfnTTTNVVILAGTNRPDILD 211
Cdd:CHL00195  300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLP 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 212 PALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDklARKLASLTPGFSGADVanvcnEAALIAARHLsdAI 291
Cdd:CHL00195  375 LEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYD--IKKLSKLSNKFSGAEI-----EQSIIEAMYI--AF 445

                  ...
gi 1907130708 292 NEK 294
Cdd:CHL00195  446 YEK 448
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
92-228 1.16e-25

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: 102.99  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  92 PKGAILTGPPGTGKTLLAKATAGEA---NVPFITVSGSEFLEMFVG---VGPARVRDLFALARKNAPCILFIDEIDAVGR 165
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907130708 166 KrgrgnfggqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGP 228
Cdd:cd00009    99 G----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
82-226 1.04e-22

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: 94.74  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  82 KQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEID 161
Cdd:cd19507    21 KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907130708 162 avgrkRGRGNFGGQSEQENT---LNQLLVEMDgfNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 226
Cdd:cd19507   101 -----KGFSNADSKGDSGTSsrvLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
77-226 2.71e-19

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: 84.71  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  77 FLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEflemfVGVGPARVRDLFALARKNApcILF 156
Cdd:cd19510     8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907130708 157 IDEIDA--VGRKR-GRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 226
Cdd:cd19510    81 LEDIDAafESREHnKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
92-230 1.82e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.42  E-value: 1.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708   92 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDLFALARKNAPCI 154
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907130708  155 LFIDEIDAVGRKRgrgnfggqSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPgRFDRQIFIGPPD 230
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
87-226 2.31e-15

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 73.56  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  87 LGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFL--------------EMFVGVGPARVRDLFALARKNAP 152
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130708 153 CILFIDEIDAVGRKRgrgnFGGQSEQENT-----LNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 226
Cdd:cd19505    87 CIIWIPNIHELNVNR----STQNLEEDPKlllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
60-226 1.18e-14

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: 71.84  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  60 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLgAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 138
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 139 RVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQentlNQLLVEMDGFNTTT--NVVILAGTNRPDILDPALLR 216
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQ----VELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
                         170
                  ....*....|
gi 1907130708 217 pgRFDRQIFI 226
Cdd:cd19523   156 --YFSKRLLV 163
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
259-298 6.64e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 60.24  E-value: 6.64e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907130708 259 KLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQ 298
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
96-160 4.68e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 61.64  E-value: 4.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDLFALARKNA----PCILFIDEI 160
Cdd:PRK13342   40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
96-160 5.90e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 61.61  E-value: 5.90e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDLFALARKNA----PCILFIDEI 160
Cdd:COG2256    53 ILWGPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
57-177 2.77e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.55  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  57 KFKDVAGCEEAKLEIMEFV-NFLKNpkqyqdlgaKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEF-----LE 130
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907130708 131 MFVGVGpARVRDLFALARKnapcILFIDEIDAVgrkRGRGNFGGQSE 177
Cdd:PRK04195   83 RVAGEA-ATSGSLFGARRK----LILLDEVDGI---HGNEDRGGARA 121
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
91-220 7.35e-09

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: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  91 IPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVGvgparvRDLFALARKNAPCILFIDEIDAVGRKRGR 169
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGS 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907130708 170 GnfGGQSEQENTLNQLL--VEMDGFNTTTNVV-------ILAGT---NRPDILDPALlrPGRF 220
Cdd:cd19498   119 S--GPDVSREGVQRDLLpiVEGSTVSTKYGPVktdhilfIAAGAfhvAKPSDLIPEL--QGRF 177
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
96-214 7.43e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 54.84  E-value: 7.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGvGPARVRDLFALARK-NAPCILFIDEIDAVGRKRgrgNFGG 174
Cdd:cd19512    26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR---STEK 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907130708 175 QSE-QENTLNQLLVEMdGFNTTTNVVILAgTNRPDILDPAL 214
Cdd:cd19512   102 ISEdLRAALNAFLYRT-GEQSNKFMLVLA-SNQPEQFDWAI 140
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
92-161 9.66e-09

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: 54.89  E-value: 9.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  92 PKGAIL-TGPPGTGKTLLAKATAGEANV---PFITVSGSEFLE-----MFVGVGPARVR-----DLFALARKNAPCILFI 157
Cdd:pfam07724   2 PIGSFLfLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                  ....
gi 1907130708 158 DEID 161
Cdd:pfam07724  82 DEIE 85
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
59-165 5.81e-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: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  59 KDVAGCEEAKLEIMEFVNFLKnpkqyqdLGAKIpKGAIL--TGPPGTGKTLLAKATAGEANVPFITVS-G--SEFLEM-- 131
Cdd:cd19500    10 ADHYGLEDVKERILEYLAVRK-------LKGSM-KGPILclVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrg 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907130708 132 ----FVGVGPARVRDLFALARKNAPCILfIDEIDAVGR 165
Cdd:cd19500    82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
96-220 7.40e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 48.44  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAKATAgEA--NVPFITVSGSEFLE-------MFVGVGPARVRD--LFALARKnaPCILFIDEIDavg 164
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130708 165 rkrgRGNfggqSEQENTLNQLLVE-----MDGFNTT----TNVVILAGTNRPDI----LDPALLRpgRF 220
Cdd:pfam07728  77 ----RAN----PDVLNSLLSLLDErrlllPDGGELVkaapDGFRLIATMNPLDRglneLSPALRS--RF 135
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
70-303 1.13e-06

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 49.95  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  70 EIMEFVNFLKNpkqYQDLGakipkgaILTGPPGTGKTLLAKATAGE-ANVPFITVSGS----EFL-----EMFVGVGPAR 139
Cdd:COG2842    38 RFAEALDEARA---LPGIG-------VVYGESGVGKTTAAREYANRnPNVIYVTASPSwtskELLeelaeELGIPAPPGT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 140 VRDLF-ALARKNAPCI--LFIDEIDAVGRKrgrgnfggqseqenTLNQLlveMDGFNTTTNVVILAGTNRPdildPALLR 216
Cdd:COG2842   108 IADLRdRILERLAGTGrlLIIDEADHLKPK--------------ALEEL---RDIHDETGVGVVLIGMERL----PAKLK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 217 pgRFDRqifigppdIKGRASiFKVHLRPLKLDSA---------LEKDKLARKLASLTpgfSGA--DVANVCNEAALIAAR 285
Cdd:COG2842   167 --RYEQ--------LYSRIG-FWVEFKPLSLEDVralaeawgeLTDPDLLELLHRIT---RGNlrRLDRTLRLAARAAKR 232
                         250
                  ....*....|....*...
gi 1907130708 286 HLSDAINEKHFEQAIERV 303
Cdd:COG2842   233 NGLTKITLDHVRAAALML 250
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
64-160 1.57e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 50.92  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  64 CEEAKLEIMEFVNFLKNPKQyqdlgakipkgAILTGPPGTGKTLLAKATA------GEANVPFITV----SGSEFLEMFV 133
Cdd:COG1401   204 REKFEETLEAFLAALKTKKN-----------VILAGPPGTGKTYLARRLAealggeDNGRIEFVQFhpswSYEDFLLGYR 272
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907130708 134 --------GVGPARVRDLFALARKN--APCILFIDEI 160
Cdd:COG1401   273 psldegkyEPTPGIFLRFCLKAEKNpdKPYVLIIDEI 309
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
96-211 1.13e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 44.80  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEA---NVPFITVSgseFLEMFvgvgparVRDLFALARKNAPCILFIDEIDAVGRKRGRGnf 172
Cdd:cd01120     2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTI-------LEAIEDLIEEKKLDIIIIDSLSSLARASQGD-- 69
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907130708 173 ggqsEQENTLNQLLVEMDGFNtTTNVVILAGTNRPDILD 211
Cdd:cd01120    70 ----RSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
93-128 2.18e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 46.89  E-value: 2.18e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1907130708  93 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF 128
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
AAA_22 pfam13401
AAA domain;
96-211 2.94e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 43.87  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAK---ATAGEANVPFITV------SGSEFLEMFV------GVGPARVRDLFA-----LARKNAPCIL 155
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAalqqlLLALAVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907130708 156 FIDEIDAVgrkrgrgnfggqseQENTLNqLLVEMDGFNTTTNVVILAGTnrPDILD 211
Cdd:pfam13401  89 IIDEAQHL--------------SLEALE-ELRDLLNLSSKLLQLILVGT--PELRE 127
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
96-160 4.12e-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: 44.03  E-value: 4.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFA-LARKNAPCILFIDEI 160
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAieRPGDLAAiLTNLEPGDVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
97-160 5.84e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 5.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907130708  97 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFAL---ARKNApcILFIDEI 160
Cdd:PRK00080   56 LYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAleKPGDLAAIltnLEEGD--VLFIDEI 111
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
93-131 1.09e-04

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: 44.61  E-value: 1.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907130708  93 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF--LEM 131
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVysLEM 93
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
78-166 1.26e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 43.74  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  78 LKNPKQYQDLGAKIPKGAI-LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPARVRDLFA------LA 147
Cdd:cd19497    35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKLLQAadydveRA 114
                          90
                  ....*....|....*....
gi 1907130708 148 RKNapcILFIDEIDAVGRK 166
Cdd:cd19497   115 QRG---IVYIDEIDKIARK 130
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
63-224 1.42e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 44.45  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  63 GCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGA---ILTGPPGTGKTLLAKATA------GEANVPFIT-VSGSEFLEMF 132
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAkiycglGVLRKPLVReVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 133 VGVGPARVRDLF--ALARknapcILFIDEIDA-VGRKRGRGN-FGGQSeqentLNQLLVEMDGfNTTTNVVILAGTNrpD 208
Cdd:TIGR03922 360 IGESEAKTNEIIdsALGG-----VLFLDEAYTlVETGYGQKDpFGLEA-----IDTLLARMEN-DRDRLVVIGAGYR--K 426
                         170       180
                  ....*....|....*....|.
gi 1907130708 209 ILDPAL-----LRpGRFDRQI 224
Cdd:TIGR03922 427 DLDKFLevnegLR-SRFTRVI 446
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
90-162 1.65e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 42.23  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  90 KIPKGAI--LTGPPGTGKTLLAKATAGEANVP--FITVSGSEFLEMFVGVGPARV----------RDLFALARK--NAPC 153
Cdd:cd00267    21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                  ....*....
gi 1907130708 154 ILFIDEIDA 162
Cdd:cd00267   101 LLLLDEPTS 109
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
96-161 1.69e-04

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: 42.55  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAKATA-----GEANvpFITVSGSEFLEMF-----VGVGPARV----RDLFALA-RKNAPCILFIDEI 160
Cdd:cd19499    45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122

                  .
gi 1907130708 161 D 161
Cdd:cd19499   123 E 123
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
97-293 2.47e-04

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: 43.23  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  97 LTGPPGTGKTLLAKATAGEANVPFITVSGSE----------------FLEMFVGVGParvrdLFAlarknapCILFIDEI 160
Cdd:COG0714    36 LEGVPGVGKTTLAKALARALGLPFIRIQFTPdllpsdilgtyiydqqTGEFEFRPGP-----LFA-------NVLLADEI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 161 DAVGRKrgrgnfggqseqenTLNQLLVEMD------GFNT-----------TTNVVILAGTNR-PDildpALLRpgRFDR 222
Cdd:COG0714   104 NRAPPK--------------TQSALLEAMEerqvtiPGGTyklpepflviaTQNPIEQEGTYPlPE----AQLD--RFLL 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907130708 223 QIFIGPPDIKGRASIFKVHLRplkldsalekdklaRKLASLTPGFSGADVANVcneAALIAARHLSDAINE 293
Cdd:COG0714   164 KLYIGYPDAEEEREILRRHTG--------------RHLAEVEPVLSPEELLAL---QELVRQVHVSEAVLD 217
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
97-160 6.20e-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: 41.99  E-value: 6.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  97 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFA----LARKNapcILFIDEI 160
Cdd:COG2255    59 LYGPPGLGKTTLAHIIANEMGVNIRITS-----------GPAieKPGDLAAiltnLEEGD---VLFIDEI 114
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
88-165 9.49e-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: 41.52  E-value: 9.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  88 GAKIPKGAI----LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLemfvgvgpaRVRDLFA-LARKNAPCILFIDEIDA 162
Cdd:TIGR00635  22 AAKMRQEALdhllLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAiLTNLEEGDVLFIDEIHR 92

                  ...
gi 1907130708 163 VGR 165
Cdd:TIGR00635  93 LSP 95
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
96-166 1.17e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 41.30  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  96 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPARVRDLFA------LARKNapcILFIDEIDAVGRK 166
Cdd:PRK05342  112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVGedVENILLKLLQAadydveKAQRG---IVYIDEIDKIARK 188
PRK13341 PRK13341
AAA family ATPase;
95-160 7.03e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 7.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  95 AILTGPPGTGKTLLAKATAGEANVPFI----TVSGSEFLEMFVGVGPARvrdlfaLARKNAPCILFIDEI 160
Cdd:PRK13341   55 LILYGPPGVGKTTLARIIANHTRAHFSslnaVLAGVKDLRAEVDRAKER------LERHGKRTILFIDEV 118
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
80-210 9.97e-03

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 37.20  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708  80 NPKQYQDLGAKIPKGAIL--TGPPGTGKTLLAKA-------TAGEANVPFITVS--GSEFLEMFVGVGPARVRdLFA--- 145
Cdd:cd03246    14 EPPVLRNVSFSIEPGESLaiIGPSGSGKSTLARLilgllrpTSGRVRLDGADISqwDPNELGDHVGYLPQDDE-LFSgsi 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130708 146 --------------LAR---KNaPCILFIDEIDAvgrkrgrgNFGGQSEQenTLNQLLVEMDGFNTTTnVVIlagTNRPD 208
Cdd:cd03246    93 aenilsggqrqrlgLARalyGN-PRILVLDEPNS--------HLDVEGER--ALNQAIAALKAAGATR-IVI---AHRPE 157

                  ..
gi 1907130708 209 IL 210
Cdd:cd03246   158 TL 159
 
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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