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Conserved domains on  [gi|1622912852|ref|XP_028696725|]
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paraplegin isoform X6 [Macaca mulatta]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 1000290)

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

Gene Ontology:  GO:0016020
PubMed:  31988523|29097521|22498346|19656850|16966379|10788805

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflB super family cl33892
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
144-593 2.03e-170

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


The actual alignment was detected with superfamily member COG0465:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 496.48  E-value: 2.03e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 144 LLVIAVVMSLLNALSTGGGSISWNDFVhEMLAKGEVQRVQVVPesDMVEVYLHPGAvvfgrprlALMYRMQVANIDKFEE 223
Cdd:COG0465     2 ALLLVLLFNLFSSSSSSVKEISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 224 KLRAAEDELNIEAKDRipvsyrrTGFFGNALYSVGMTAVGLAILWCVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTGk 303
Cdd:COG0465    71 LLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 304 gVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:COG0465   139 -VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGA 463
Cdd:COG0465   218 VGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPA 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 464 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQ---PSTfysqrLAELTPGFSGADIANICNEAALHAAREGHTSVH 540
Cdd:COG0465   297 LLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPdvdLEV-----IARRTPGFSGADLANLVNEAALLAARRNKKAVT 371

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622912852 541 TLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGWMLEHTEAVMKV 593
Cdd:COG0465   372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKV 424
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
144-593 2.03e-170

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 496.48  E-value: 2.03e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 144 LLVIAVVMSLLNALSTGGGSISWNDFVhEMLAKGEVQRVQVVPesDMVEVYLHPGAvvfgrprlALMYRMQVANIDKFEE 223
Cdd:COG0465     2 ALLLVLLFNLFSSSSSSVKEISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 224 KLRAAEDELNIEAKDRipvsyrrTGFFGNALYSVGMTAVGLAILWCVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTGk 303
Cdd:COG0465    71 LLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 304 gVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:COG0465   139 -VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGA 463
Cdd:COG0465   218 VGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPA 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 464 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQ---PSTfysqrLAELTPGFSGADIANICNEAALHAAREGHTSVH 540
Cdd:COG0465   297 LLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPdvdLEV-----IARRTPGFSGADLANLVNEAALLAARRNKKAVT 371

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622912852 541 TLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGWMLEHTEAVMKV 593
Cdd:COG0465   372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKV 424
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 264-593 7.47e-151

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: 443.27  E-value: 7.47e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 264 LAILWCVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPK 342
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 343 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSG 422
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 423 fSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQpsT 502
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAP--D 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 503 FYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGW 582
Cdd:TIGR01241 247 VDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGL 326

                         330
                  ....*....|.
gi 1622912852 583 MLEHTEAVMKV 593
Cdd:TIGR01241 327 LLKDADPVHKV 337
ftsH CHL00176
cell division protein; Validated
 264-593 2.61e-118

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 364.76  E-value: 2.61e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 264 LAILWCVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVP 341
Cdd:CHL00176  141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 342 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMS 421
Cdd:CHL00176  217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 422 GfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 501
Cdd:CHL00176  297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 502 TFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFEYAVERVLAGTAKKSKILSKeEQKVVAFHESGHALVG 581
Cdd:CHL00176  376 SL--ELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVG 452

                         330
                  ....*....|..
gi 1622912852 582 WMLEHTEAVMKV 593
Cdd:CHL00176  453 TLLPNHDPVQKV 464
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 305-476 1.81e-105

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: 314.94  E-value: 1.81e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 384
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 385 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGAL 464
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159

                         170
                  ....*....|..
gi 1622912852 465 MRPGRLDRHVFI 476
Cdd:cd19501   160 LRPGRFDRQVYV 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 345-478 4.39e-46

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: 158.53  E-value: 4.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfs 424
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS-- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622912852 425 ntEEEQTLNQLLVEMDGM-GTTDHVIVLASTNRADILDGALMrpGRLDRHVFIDL 478
Cdd:pfam00004  80 --ESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
305-534 6.18e-41

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 152.58  E-value: 6.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:NF041006  100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTTMSGfsnteEEQTLNQLLVEMDGM---GTTDHVIVLASTN 455
Cdd:NF041006  177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLqdkSENYHVYVIGATN 251

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622912852 456 RADILDGALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFysQRLAELTPGFSGADIANICNEAALHAARE 534
Cdd:NF041006  252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTASDIRDIVQAAHMRVVKE 326
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 341-480 2.67e-15

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: 73.18  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852  341 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 403
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622912852  404 VYIDEIDAVGKKRSttmsgfsntEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPgRLDRHVFIDLPT 480
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 345-409 8.72e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.22  E-value: 8.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEViggLGAARV-RSLFKEAR--ARAPCIVyIDEI 409
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAA-----CRQGyrvrfttaADLVEQ---LAQARAdGRLGRLLRrlARYDLLI-IDEL 160
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
144-593 2.03e-170

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 496.48  E-value: 2.03e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 144 LLVIAVVMSLLNALSTGGGSISWNDFVhEMLAKGEVQRVQVVPesDMVEVYLHPGAvvfgrprlALMYRMQVANIDKFEE 223
Cdd:COG0465     2 ALLLVLLFNLFSSSSSSVKEISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELVD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 224 KLRAAEDELNIEAKDRipvsyrrTGFFGNALYSVGMTAVGLAILWCVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTGk 303
Cdd:COG0465    71 LLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 304 gVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:COG0465   139 -VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGA 463
Cdd:COG0465   218 VGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPA 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 464 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQ---PSTfysqrLAELTPGFSGADIANICNEAALHAAREGHTSVH 540
Cdd:COG0465   297 LLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPdvdLEV-----IARRTPGFSGADLANLVNEAALLAARRNKKAVT 371

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622912852 541 TLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGWMLEHTEAVMKV 593
Cdd:COG0465   372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKV 424
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 264-593 7.47e-151

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: 443.27  E-value: 7.47e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 264 LAILWCVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPK 342
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 343 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSG 422
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 423 fSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQpsT 502
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAP--D 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 503 FYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGW 582
Cdd:TIGR01241 247 VDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGL 326

                         330
                  ....*....|.
gi 1622912852 583 MLEHTEAVMKV 593
Cdd:TIGR01241 327 LLKDADPVHKV 337
ftsH CHL00176
cell division protein; Validated
 264-593 2.61e-118

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 364.76  E-value: 2.61e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 264 LAILWCVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVP 341
Cdd:CHL00176  141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 342 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMS 421
Cdd:CHL00176  217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 422 GfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 501
Cdd:CHL00176  297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 502 TFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFEYAVERVLAGTAKKSKILSKeEQKVVAFHESGHALVG 581
Cdd:CHL00176  376 SL--ELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVG 452

                         330
                  ....*....|..
gi 1622912852 582 WMLEHTEAVMKV 593
Cdd:CHL00176  453 TLLPNHDPVQKV 464
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 305-476 1.81e-105

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: 314.94  E-value: 1.81e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 384
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 385 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGAL 464
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159

                         170
                  ....*....|..
gi 1622912852 465 MRPGRLDRHVFI 476
Cdd:cd19501   160 LRPGRFDRQVYV 171
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
267-593 3.93e-100

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 317.75  E-value: 3.93e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 267 LWcVFRLAGMTGREG-GFSAFNQLKMARFTIVDGKTgkgvSFKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGAL 345
Cdd:PRK10733  115 VW-IFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKT----TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 346 LLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSN 425
Cdd:PRK10733  190 MVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGG-GH 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 426 TEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSTFYS 505
Cdd:PRK10733  269 DEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLA--PDIDA 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 506 QRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFEYAVERVLAGTAKKSKILSKEEQKVVAFHESGHALVGWMLE 585
Cdd:PRK10733  347 AIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVP 426


                  ....*...
gi 1622912852 586 HTEAVMKV 593
Cdd:PRK10733  427 EHDPVHKV 434
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 304-558 6.28e-100

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 306.55  E-value: 6.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 304 GVSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 382
Cdd:COG1222    74 DVTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 383 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSttmSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDG 462
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRT---DDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 463 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTL 542
Cdd:COG1222   231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL--DKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTME 308

                         250
                  ....*....|....*.
gi 1622912852 543 NFEYAVERVLAGTAKK 558
Cdd:COG1222   309 DLEKAIEKVKKKTETA 324
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 304-560 5.31e-85

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 270.16  E-value: 5.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 304 GVSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 382
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 383 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRstTMSGFSNTEEEQ-TLNQLLVEMDGMGTTDHVIVLASTNRADILD 461
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKR--TDSGTSGDREVQrTLMQLLAEMDGFDPRGNVKIIAATNRIDILD 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 462 GALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHT 541
Cdd:PRK03992  285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL--EELAELTEGASGADLKAICTEAGMFAIRDDRTEVTM 362

                         250
                  ....*....|....*....
gi 1622912852 542 LNFEYAVERVLAGTAKKSK 560
Cdd:PRK03992  363 EDFLKAIEKVMGKEEKDSM 381
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 307-551 1.01e-72

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: 238.66  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 307 FKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFV-EVIGGL 384
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVsKYVGET 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 385 gAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGFSNTEeeqtLNQLLVEMDGMgtTDHVIVLASTNRADILDGAL 464
Cdd:COG0464   236 -EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRV----VNTLLTEMEEL--RSDVVVIAATNRPDLLDPAL 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 465 MRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSTFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNF 544
Cdd:COG0464   309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD--EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384


                  ....*..
gi 1622912852 545 EYAVERV 551
Cdd:COG0464   385 LEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 305-569 5.29e-66

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: 229.02  E-value: 5.29e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTmsgFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGA 463
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGAR---FDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 464 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLN 543
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL--EELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEK 684

                         250       260
                  ....*....|....*....|....*.
gi 1622912852 544 FEYAVERVLAGTAKKSKILSKEEQKV 569
Cdd:TIGR01243 685 LEVGEEEFLKDLKVEMRHFLEALKKV 710
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 306-474 7.59e-59

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 194.09  E-value: 7.59e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 306 SFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 384
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 385 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGAL 464
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTG-GDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPAL 159

                         170
                  ....*....|
gi 1622912852 465 MRPGRLDRHV 474
Cdd:cd19502   160 LRPGRFDRKI 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 316-476 1.56e-58

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: 192.88  E-value: 1.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 316 AKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 394
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 395 EARARAPCIVYIDEIDAVGKKRSTTMSGfsnTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHV 474
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSS---GVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157


                  ..
gi 1622912852 475 FI 476
Cdd:cd19511   158 YV 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
307-550 1.87e-58

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 195.87  E-value: 1.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 307 FKDVAGMHEAKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMagpEFVEVIG---G 383
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTV---RLDSLIGsylG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARaRAPCIVYIDEIDAVGKKRsttmsGFSNTEEE--QTLNQLLVEMDGMgtTDHVIVLASTNRADILD 461
Cdd:COG1223    78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDR-----GDQNDVGEvkRVVNALLQELDGL--PSGSVVIAATNHPELLD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 462 GALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLtqPSTFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHT 541
Cdd:COG1223   150 SALWR--RFDEVIEFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTK 225


                  ....*....
gi 1622912852 542 LNFEYAVER 550
Cdd:COG1223   226 EDLEEALKQ 234
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 305-533 2.12e-56

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: 202.44  E-value: 2.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTmsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGA 463
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEV----TGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 464 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFysQRLAELTPGFSGADIANICNEAALHAAR 533
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL--DKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 316-476 2.63e-56

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: 186.72  E-value: 2.63e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 316 AKQEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 395
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 396 ARARAPCIVYIDEIDAVGKKRSttmSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVF 475
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRD---SSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                  .
gi 1622912852 476 I 476
Cdd:cd19481   158 F 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 305-552 3.82e-56

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 194.60  E-value: 3.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:PTZ00454  142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGA 463
Cdd:PTZ00454  222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTG-ADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 464 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTF--YSQRLAELtpgfSGADIANICNEAALHAAREGHTSVHT 541
Cdd:PTZ00454  301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLedFVSRPEKI----SAADIAAICQEAGMQAVRKNRYVILP 376

                         250
                  ....*....|.
gi 1622912852 542 LNFEYAVERVL 552
Cdd:PTZ00454  377 KDFEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 306-552 2.98e-54

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 190.37  E-value: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 306 SFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 384
Cdd:PTZ00361  181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 385 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGAL 464
Cdd:PTZ00361  261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSG-GEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 465 MRPGRLDRHVFIDLPTLQERREIFEQHLKglKLTQPSTFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNF 544
Cdd:PTZ00361  340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTS--KMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417


                  ....*...
gi 1622912852 545 EYAVERVL 552
Cdd:PTZ00361  418 RKAKEKVL 425
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 317-476 8.20e-54

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: 180.40  E-value: 8.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 317 KQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 395
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 396 ARARAPCIVYIDEIDAVGKKRSTTMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVF 475
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGD-AGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160


                  .
gi 1622912852 476 I 476
Cdd:cd19528   161 I 161
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 309-476 1.23e-51

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: 174.79  E-value: 1.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 387
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 388 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTTmsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRP 467
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREED----QREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156


                  ....*....
gi 1622912852 468 GRLDRHVFI 476
Cdd:cd19503   157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 316-476 1.68e-51

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: 174.22  E-value: 1.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 316 AKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 394
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 395 EARARAPCIVYIDEIDAVGKKR-STTMSGFSnteeEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRH 473
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVT----ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRL 156


                  ...
gi 1622912852 474 VFI 476
Cdd:cd19529   157 IYI 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 309-474 4.67e-49

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 167.97  E-value: 4.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDYLKS-PERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 387
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILpPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 388 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTTmsgfSNTEEEQTLNQLLVEMDGMG----TTDHVIVLASTNRADILDGA 463
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESA----QREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156

                         170
                  ....*....|.
gi 1622912852 464 LMRPGRLDRHV 474
Cdd:cd19518   157 LRRAGRFDREI 167
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 309-476 2.32e-48

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: 166.07  E-value: 2.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 387
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 388 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTTmsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRP 467
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT----HGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156


                  ....*....
gi 1622912852 468 GRLDRHVFI 476
Cdd:cd19519   157 GRFDREIDI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 345-478 4.39e-46

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: 158.53  E-value: 4.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGfs 424
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS-- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622912852 425 ntEEEQTLNQLLVEMDGM-GTTDHVIVLASTNRADILDGALMrpGRLDRHVFIDL 478
Cdd:pfam00004  80 --ESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 327-476 1.39e-44

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: 155.72  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 327 LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 406
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 407 DEIDAVGKKRSTTMSGFSnteeEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFI 476
Cdd:cd19530    96 DEVDALVPKRGDGGSWAS----ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
cell_div_CdvC NF041006
cell division protein CdvC;
305-534 6.18e-41

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 152.58  E-value: 6.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 383
Cdd:NF041006  100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 384 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTTMSGfsnteEEQTLNQLLVEMDGM---GTTDHVIVLASTN 455
Cdd:NF041006  177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLqdkSENYHVYVIGATN 251

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622912852 456 RADILDGALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFysQRLAELTPGFSGADIANICNEAALHAARE 534
Cdd:NF041006  252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTASDIRDIVQAAHMRVVKE 326
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 316-475 1.08e-40

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 144.88  E-value: 1.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 316 AKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 394
Cdd:cd19526     1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 395 EARARAPCIVYIDEIDAVGKKRSTTMSGFSnteeEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHV 474
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVT----DRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156


                  .
gi 1622912852 475 F 475
Cdd:cd19526   157 Y 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 317-476 7.16e-38

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: 137.26  E-value: 7.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 317 KQEVREFVDY-LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 395
Cdd:cd19527     2 KKEILDTIQLpLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 396 ARARAPCIVYIDEIDAVGKKRSTtmSGFSNTEEEQTLNQLLVEMDGM-GTTDHVIVLASTNRADILDGALMRPGRLDRHV 474
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGN--SGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158


                  ..
gi 1622912852 475 FI 476
Cdd:cd19527   159 YL 160
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 305-493 4.90e-36

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 141.38  E-value: 4.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATE-AQVP---------FLAMA 373
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAARIgaegggksyFLNIK 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 374 GPEFVEVIGGLGAARVRSLFKEARARA----PCIVYIDEIDAVGKKRSttmSGFSNTEEEQTLNQLLVEMDGMGTTDHVI 449
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRG---SGVSSDVETTVVPQLLAEIDGVESLDNVI 335

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622912852 450 VLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLK 493
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 310-476 2.18e-35

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: 130.55  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 310 VAGMHEAKQEVREFVDY-LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAAR 388
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 389 VRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGFSNTEEeqtlNQLLVEMDGMGTT--DHVIVLASTNRADILDGALMR 466
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVK----TEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR 155

                         170
                  ....*....|
gi 1622912852 467 pgRLDRHVFI 476
Cdd:cd19509   156 --RFEKRIYI 163
ycf46 CHL00195
Ycf46; Provisional
 305-534 1.77e-29

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 122.05  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKqevrefvDYLKS-----PERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAM-AGPEFV 378
Cdd:CHL00195  225 EKISDIGGLDNLK-------DWLKKrstsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLdVGKLFG 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 379 EVIGGlGAARVRSLFKEARARAPCIVYIDEIDavgkkrsttmSGFSNTE---EEQTLNQLLvemdgmGT--------TDH 447
Cdd:CHL00195  298 GIVGE-SESRMRQMIRIAEALSPCILWIDEID----------KAFSNSEskgDSGTTNRVL------ATfitwlsekKSP 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 448 VIVLASTNRADILDGALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSTFYSQRLAELTPGFSGADIANICNEA 527
Cdd:CHL00195  361 VFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEA 440


                  ....*..
gi 1622912852 528 ALHAARE 534
Cdd:CHL00195  441 MYIAFYE 447
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 309-476 7.17e-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: 112.77  E-value: 7.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLqlGAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 386
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 387 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTtmsGFSNTEEEQTLNQLLVEMDGMGTTDH-------VIVLASTNRADI 459
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT---SEEHEASRRVKSELLVQMDGVGGASEnddpskmVMVLAATNFPWD 155

                         170
                  ....*....|....*..
gi 1622912852 460 LDGALMRpgRLDRHVFI 476
Cdd:cd19522   156 IDEALRR--RLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 305-476 1.06e-28

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: 112.26  E-value: 1.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 305 VSFKDVAGMHEAKQEVREFVDYlksPERFLQL--GAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVI 381
Cdd:cd19521     4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 382 GGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGFSnteeEQTLNQLLVEMDGMGT-TDHVIVLASTNRADIL 460
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEAS----RRIKTELLVQMNGVGNdSQGVLVLGATNIPWQL 156

                         170
                  ....*....|....*.
gi 1622912852 461 DGALMRpgRLDRHVFI 476
Cdd:cd19521   157 DSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 309-472 2.51e-28

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: 111.06  E-value: 2.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEA-----QVPFLAMAGPEFVEVIG 382
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 383 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTtmsgfsntEEEQT----LNQLLVEMDGMGTTDHVIVLASTNRAD 458
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS--------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPD 152

                         170
                  ....*....|....
gi 1622912852 459 ILDGALMRPGRLDR 472
Cdd:cd19517   153 ALDPALRRPGRFDR 166
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 321-476 7.11e-28

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 110.27  E-value: 7.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 321 REFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVAT--EAQVPFLaMAGPEFVEVIGGLGAARVRSLFKEA-- 396
Cdd:cd19504    15 RAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKmlNAREPKI-VNGPEILNKYVGESEANIRKLFADAee 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 397 --RARAPC----IVYIDEIDAVGKKRSTTMSGfsNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRL 470
Cdd:cd19504    94 eqRRLGANsglhIIIFDEIDAICKQRGSMAGS--TGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRL 171


                  ....*.
gi 1622912852 471 DRHVFI 476
Cdd:cd19504   172 EVQMEI 177
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 309-476 1.15e-27

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: 109.17  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 387
Cdd:cd19524     1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 388 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTtmsgfSNTEEEQTL-NQLLVEMDGM--GTTDHVIVLASTNRADILDGAL 464
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSE-----GEHEASRRLkTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAV 154

                         170
                  ....*....|..
gi 1622912852 465 MRpgRLDRHVFI 476
Cdd:cd19524   155 LR--RFTKRVYV 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 302-476 2.30e-27

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 108.92  E-value: 2.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 302 GKGVSFKDVAGMHEAKQEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEV 380
Cdd:cd19525    16 GPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 381 IGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTTmsgfSNTEEEQTLNQLLVEMDGMGTT--DHVIVLASTNRAD 458
Cdd:cd19525    95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG----EHESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQ 170

                         170
                  ....*....|....*...
gi 1622912852 459 ILDGALMRpgRLDRHVFI 476
Cdd:cd19525   171 EIDEAARR--RLVKRLYI 186
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 309-470 3.40e-27

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: 107.90  E-value: 3.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLQLG-AKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 386
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 387 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTtmsgfsnTEEEQTL---NQLLVEMDGMGTTDH--VIVLASTNRADILD 461
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS-------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLD 153

                         170
                  ....*....|.
gi 1622912852 462 GALMR--PGRL 470
Cdd:cd19520   154 EAILRrmPKRF 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 311-478 2.08e-24

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: 99.53  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 311 AGMHEAKQEVREFVDYlksperflqlgaKVPKGALLLGPPGCGKTLLAKAVATEA---QVPFLAMAGPEFVE---VIGGL 384
Cdd:cd00009     1 VGQEEAIEALREALEL------------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEglvVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 385 GAARVRSLFKEARARAPCIVYIDEIDAVGKKrsttmsgfsntEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGAL 464
Cdd:cd00009    69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRG-----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137

                         170
                  ....*....|....
gi 1622912852 465 MRPGRLDRHVFIDL 478
Cdd:cd00009   138 ALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 309-476 8.51e-19

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 83.57  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQ--EVREfVDYLKSPERFlqlGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 386
Cdd:cd19507     1 DVGGLDNLKDwlKKRK-AAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 387 ARVRSLFKEARARAPCIVYIDEID-AVGKKRSTTMSGFSNteeeQTLNQLLVEMDgmGTTDHVIVLASTNRADILDGALM 465
Cdd:cd19507    77 SRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSS----RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELL 150

                         170
                  ....*....|.
gi 1622912852 466 RPGRLDRHVFI 476
Cdd:cd19507   151 RKGRFDEIFFV 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 320-476 4.11e-17

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: 78.55  E-value: 4.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 320 VREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfveviGGLGAARVRSLFKEARAR 399
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622912852 400 ApcIVYIDEIDAVGKKRSTTMSGFSNTEEEQ--TLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDRHVFI 476
Cdd:cd19510    77 S--IILLEDIDAAFESREHNKKNPSAYGGLSrvTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 309-466 2.32e-16

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: 76.85  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 309 DVAGMHEAKQEVREFVDY-LKSPERFLQLgAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 387
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 388 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTTMSGFSNTEEEqtlnqLLVEMDGMGTT--DHVIVLASTNRADILDGALM 465
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154


                  .
gi 1622912852 466 R 466
Cdd:cd19523   155 R 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 341-480 2.67e-15

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: 73.18  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852  341 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 403
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622912852  404 VYIDEIDAVGKKRSttmsgfsntEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPgRLDRHVFIDLPT 480
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 334-472 1.16e-11

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: 63.16  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 334 LQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMA-------GPEFVEVIGGLGAA-------RVRSLFKEARAR 399
Cdd:cd19505     5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynKPDFGNDDWIDGMLilkeslhRLNLQFELAKAM 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622912852 400 APCIVYIDEIDAVGKKRSTTMSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADILDGALMRPGRLDR 472
Cdd:cd19505    85 SPCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 506-545 1.67e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 59.09  E-value: 1.67e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622912852 506 QRLAELTPGFSGADIANICNEAALHAAREGHTSVHTLNFE 545
Cdd:pfam17862   5 EELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
Peptidase_M41 pfam01434
Peptidase family M41;
560-593 4.07e-11

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 62.23  E-value: 4.07e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622912852 560 KILSKEEQKVVAFHESGHALVGWMLEHTEAVMKV 593
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKV 34
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 345-464 5.79e-10

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: 57.92  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfVEVIGGLGAARVRSLFKEA-RARAPCIVYIDEIDAVGKKRSTT-MSg 422
Cdd:cd19512    26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEkIS- 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622912852 423 fsnTEEEQTLNQLLVEMdGMGTTDHVIVLAStNRADILDGAL 464
Cdd:cd19512   104 ---EDLRAALNAFLYRT-GEQSNKFMLVLAS-NQPEQFDWAI 140
PRK04195 PRK04195
replication factor C large subunit; Provisional
 306-410 1.21e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 54.54  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 306 SFKDVAGMHEAKQEVREFVdylkspERFLQlgaKVPKGALLL-GPPGCGKTLLAKAVATEaqvpflamAGPEFVE----- 379
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWI------ESWLK---GKPKKALLLyGPPGVGKTSLAHALAND--------YGWEVIElnasd 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622912852 380 ---------VIGglGAARVRSLFKEARArapcIVYIDEID 410
Cdd:PRK04195   75 qrtadvierVAG--EAATSGSLFGARRK----LILLDEVD 108
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 345-415 1.26e-07

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 54.28  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA---RARAPC-IVYIDEI 409
Cdd:COG1219   113 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydVEKAERgIIYIDEI 183


                  ....*.
gi 1622912852 410 DAVGKK 415
Cdd:COG1219   184 DKIARK 189
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 345-458 2.43e-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: 49.98  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVAtEA--QVPFLAMAGPEFVEV--------IGGLGAARVRSLFKEArARAPCIVYIDEIDAVGK 414
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTEedlfgrrnIDPGGASWVDGPLVRA-AREGEIAVLDEINRANP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622912852 415 krSTTMSGFSNTEEEQtlnqlLVEMDGMGTTDH----VIVLASTNRAD 458
Cdd:pfam07728  81 --DVLNSLLSLLDERR-----LLLPDGGELVKAapdgFRLIATMNPLD 121
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 345-415 2.56e-07

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: 52.22  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPF-------LAMAG--PEFVEVIgglgaarVRSLFKEAR---ARAP-CIVYIDEIDA 411
Cdd:cd19497    54 LLIGPTGSGKTLLAQTLAKILDVPFaiadattLTEAGyvGEDVENI-------LLKLLQAADydvERAQrGIVYIDEIDK 126


                  ....
gi 1622912852 412 VGKK 415
Cdd:cd19497   127 IARK 130
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 308-487 2.90e-07

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 50.84  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 308 KDVAGMHEAKQEVrefVDYLKSPERFLQLGAK-----VPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVig 382
Cdd:cd19498    11 KYIIGQDEAKRAV---AIALRNRWRRMQLPEElrdevTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEV-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 383 GLGAARVRSLFKEArarAPCIVYIDEIDAVGKKRSTTMSGFSNTEEEQTLNQlLVEMD------GMGTTDHVIVLAStnr 456
Cdd:cd19498    86 GYVGRDVESIIRDL---VEGIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLP-IVEGStvstkyGPVKTDHILFIAA--- 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622912852 457 adildGA--LMRPGRLdrhvfidLPTLQERREI 487
Cdd:cd19498   159 -----GAfhVAKPSDL-------IPELQGRFPI 179
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
345-415 5.34e-07

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 52.08  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA-----RA-RApcIVYID 407
Cdd:PRK05342  112 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydveKAqRG--IVYID 180


                  ....*...
gi 1622912852 408 EIDAVGKK 415
Cdd:PRK05342  181 EIDKIARK 188
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 345-409 2.26e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.08  E-value: 2.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 409
Cdd:PRK13342   40 ILWGPPGTGKTTLARIIAGATDAPFEALSA-----VTSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 345-409 4.06e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 49.28  E-value: 4.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 409
Cdd:COG2256    53 ILWGPPGTGKTTLARLIANATDAEFVALSA-----VTSGV--KDIREVIEEARERRaygrRTILFVDEI 114
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
 144-241 8.96e-06

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 44.90  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 144 LLVIAVVMSLLNALSTGGGS----ISWNDFVhEMLAKGEVQRVQVVPesDMVEVYLHPGAVVFGRPRLALMYRMQVANID 219
Cdd:pfam06480   5 LLILLVLLLLFLLFLLSSSSstkeISYSEFL-EYLEAGKVKKVVVQD--DEILPTGVVEGTLKDGSKFTTYFIPSLPNVD 81

                          90       100
                  ....*....|....*....|..
gi 1622912852 220 KFEEKLRAAEDELNIEAKDRIP 241
Cdd:pfam06480  82 SLLEKLEDALEEKGVKVSVKPP 103
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 308-414 2.90e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 44.86  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 308 KDVAGMHEAKQEVREFVDYLKsperflqLGAKVpKGALLL--GPPGCGKTLLAKAVATeaqvpflAMaGPEFVEV-IGGL 384
Cdd:cd19500    10 ADHYGLEDVKERILEYLAVRK-------LKGSM-KGPILClvGPPGVGKTSLGKSIAR-------AL-GRKFVRIsLGGV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622912852 385 --------------GA--ARVRSLFKEARARAPCIVyIDEIDAVGK 414
Cdd:cd19500    74 rdeaeirghrrtyvGAmpGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 312-459 1.06e-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: 45.22  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 312 GMHEAKQEVREFVDYLKSPERFLQLGAKVPKGA---LLLGPPGCGKTLLAKAVATeaqvpFLAMAG----PEFVEV---- 380
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAK-----IYCGLGvlrkPLVREVsrad 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 381 -IG---GLGAARVRSLFKEARARapcIVYIDEIDAVGKKRSTTMSGFSNteeeQTLNQLLVEMDgmGTTDHVIVLASTNR 456
Cdd:TIGR03922 355 lIGqyiGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGL----EAIDTLLARME--NDRDRLVVIGAGYR 425


                  ...
gi 1622912852 457 ADI 459
Cdd:TIGR03922 426 KDL 428
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
342-377 1.32e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 1.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622912852 342 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 377
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 345-553 2.54e-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: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPF-------------------LAMAGPEFVEVIGGLGAArvrslfkeararapcIVY 405
Cdd:COG0714    35 LLEGVPGVGKTTLAKALARALGLPFiriqftpdllpsdilgtyiYDQQTGEFEFRPGPLFAN---------------VLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 406 IDEIDavgkkRSTtmsgfsnteeEQTLNQLLVEMDGM-----GTT----DHVIVLASTNRADI-----LDGALmrpgrLD 471
Cdd:COG0714   100 ADEIN-----RAP----------PKTQSALLEAMEERqvtipGGTyklpEPFLVIATQNPIEQegtypLPEAQ-----LD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 472 R---HVFIDLPTLQERREIFEQHLKGlkltqpstfysqRLAELTPGFSGADIAnicneAALHAAREGHTSVHTLnfEYAV 548
Cdd:COG0714   160 RfllKLYIGYPDAEEEREILRRHTGR------------HLAEVEPVLSPEELL-----ALQELVRQVHVSEAVL--DYIV 220


                  ....*
gi 1622912852 549 ERVLA 553
Cdd:COG0714   221 DLVRA 225
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 345-462 4.79e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.18  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIgglgAARVRSLFKEARaraPCIVYIDEIDAVgkkrsttMSGFS 424
Cdd:cd01120     2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTI----LEAIEDLIEEKK---LDIIIIDSLSSL-------ARASQ 67

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622912852 425 NTEEEQTLNQLLVEMDGMGTTdHVIVLASTNRADILDG 462
Cdd:cd01120    68 GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDID 104
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 342-377 5.79e-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: 42.30  E-value: 5.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622912852 342 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 377
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 345-375 2.90e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGP 375
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGP 67
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
342-409 3.07e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 3.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622912852 342 KGALLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEvigGLGAARV-RSLFKEAR--ARAPCIVyIDEI 409
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEA-----CRAGyrvrfttaPDLVN---ELKEARAdGRLERLLKrlAKVDLLI-LDEL 169
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 306-414 3.74e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.59  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912852 306 SFKDVAGMHEAKQEVREFVDylksperflqlGAKVPKGA----LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFvEVI 381
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIE-----------AAKMRQEAldhlLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL-EKP 69

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622912852 382 GGLGAArvRSLFKEARarapcIVYIDEIDAVGK 414
Cdd:TIGR00635  70 GDLAAI--LTNLEEGD-----VLFIDEIHRLSP 95
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 345-409 8.72e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.22  E-value: 8.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622912852 345 LLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEViggLGAARV-RSLFKEAR--ARAPCIVyIDEI 409
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAA-----CRQGyrvrfttaADLVEQ---LAQARAdGRLGRLLRrlARYDLLI-IDEL 160
 
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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