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Conserved domains on  [gi|518229806|ref|WP_019400014|]
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ATP-dependent zinc metalloprotease FtsH [Pseudoxanthomonas sp. GW2]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-598 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 962.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  14 VAGLLLLTLQNYWQAAKTVEPVPYSEFEKALAEGRVAEVLVSDRTVTGRLKSPDSQGKTTIVATrvEPDLAERLSKYDVP 93
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTRFTTYRVN--DPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  94 YA--RVVESTWLRDVLSWILPAVAFFGVWFFLFRRFAekQGMGGFLSIGKSRAKVFMEKNTGVTFADVAGVDEAKAELVE 171
Cdd:COG0465   79 VTakPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQ--GGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 172 IVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPA 251
Cdd:COG0465  157 IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPC 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 252 IIFIDELDALGRARGVGGPiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLVDRPDKK 331
Cdd:COG0465  237 IIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 332 GRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAAIERIVAGLERKNRVLNP 411
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 412 KERETVAYHEMGHALVALALPGTDPVHKISIVPRGiGALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLVFGELS 491
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 492 TGASDDLARATDIARDMITRFGMDEGLGYVAFEAQRPRFLDAPELVQGGcRVAESTQTRIDQAIRDIVMGVFDRAYRILE 571
Cdd:COG0465  475 TGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSR-NYSEETAREIDEEVRRIIDEAYERAKEILT 553
                        570       580
                 ....*....|....*....|....*..
gi 518229806 572 INREVLERCARELLARETLDEYSIRQL 598
Cdd:COG0465  554 ENRDKLDALAEALLEKETLDGEELEEI 580
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-598 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 962.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  14 VAGLLLLTLQNYWQAAKTVEPVPYSEFEKALAEGRVAEVLVSDRTVTGRLKSPDSQGKTTIVATrvEPDLAERLSKYDVP 93
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTRFTTYRVN--DPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  94 YA--RVVESTWLRDVLSWILPAVAFFGVWFFLFRRFAekQGMGGFLSIGKSRAKVFMEKNTGVTFADVAGVDEAKAELVE 171
Cdd:COG0465   79 VTakPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQ--GGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 172 IVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPA 251
Cdd:COG0465  157 IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPC 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 252 IIFIDELDALGRARGVGGPiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLVDRPDKK 331
Cdd:COG0465  237 IIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 332 GRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAAIERIVAGLERKNRVLNP 411
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 412 KERETVAYHEMGHALVALALPGTDPVHKISIVPRGiGALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLVFGELS 491
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 492 TGASDDLARATDIARDMITRFGMDEGLGYVAFEAQRPRFLDAPELVQGGcRVAESTQTRIDQAIRDIVMGVFDRAYRILE 571
Cdd:COG0465  475 TGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSR-NYSEETAREIDEEVRRIIDEAYERAKEILT 553
                        570       580
                 ....*....|....*....|....*..
gi 518229806 572 INREVLERCARELLARETLDEYSIRQL 598
Cdd:COG0465  554 ENRDKLDALAEALLEKETLDGEELEEI 580
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
101-598 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 714.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  101 TWLRDVLSWILPAVAFFGVWFFLFRRfaeKQGMGG-FLSIGKSRAKVFMEKNTGVTFADVAGVDEAKAELVEIVDFLKNP 179
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQ---MQGGGGrAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  180 QDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPAIIFIDELD 259
Cdd:TIGR01241  78 SKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEID 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  260 ALGRARGVGgPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLVDRPDKKGRLDILKV 339
Cdd:TIGR01241 158 AVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  340 HVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAAIERIVAGLERKNRVLNPKERETVAY 419
Cdd:TIGR01241 237 HAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  420 HEMGHALVALALPGTDPVHKISIVPRGIgALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLVFGELSTGASDDLA 499
Cdd:TIGR01241 317 HEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  500 RATDIARDMITRFGMDEGLGYVAFEAQRprflDAPELVQGGCR---VAESTQTRIDQAIRDIVMGVFDRAYRILEINREV 576
Cdd:TIGR01241 396 QATNIARAMVTEWGMSDKLGPVAYGSDG----GDVFLGRGFAKakeYSEETAREIDEEVKRIIEEAYKRAKQILTENRDE 471
                         490       500
                  ....*....|....*....|..
gi 518229806  577 LERCARELLARETLDEYSIRQL 598
Cdd:TIGR01241 472 LELLAKALLEKETITREEIKEL 493
ftsH CHL00176
cell division protein; Validated
78-598 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 603.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  78 RVE-----PDLAERLSKYDV---PYARVVESTWLRDVLSWILPAVAFFGVWFFLFRRFAEKQGMG-GFLSIGKSRAKVFM 148
Cdd:CHL00176  95 RVElpvgaSELIQKLKEANIdfdAHPPVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGqNLMNFGKSKARFQM 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 149 EKNTGVTFADVAGVDEAKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVE 228
Cdd:CHL00176 175 EADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVE 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 229 MFVGVGAARVRDLFEQARGQAPAIIFIDELDALGRARGVG-GpiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPE 307
Cdd:CHL00176 255 MFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiG--GGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVD 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 308 ILDQALLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVE 387
Cdd:CHL00176 333 ILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATIT 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 388 LQDFTAAIERIVAGLERKNRVLNpKERETVAYHEMGHALVALALPGTDPVHKISIVPRGiGALGYTLQRPTEDRFLMTRA 467
Cdd:CHL00176 413 MKEIDTAIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRG-QAKGLTWFTPEEDQSLVSRS 490
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 468 DLEHKIAVLLGGRAAEKLVFG--ELSTGASDDLARATDIARDMITRFGMDeGLGYVAFEAQRPRFLDAPELVQGGCRVAE 545
Cdd:CHL00176 491 QILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLGRFMQRNSEYSE 569
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518229806 546 STQTRIDQAIRDIVMGVFDRAYRILEINREVLERCARELLARETLDEYSIRQL 598
Cdd:CHL00176 570 EIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREI 622
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
154-325 2.75e-115

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: 340.75  E-value: 2.75e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 154 VTFADVAGVDEAKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGV 233
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 234 GAARVRDLFEQARGQAPAIIFIDELDALGRARGVGGpIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQAL 313
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGL-GGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 518229806 314 LRAGRFDRQVLV 325
Cdd:cd19501  160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
407-598 4.80e-71

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 227.48  E-value: 4.80e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  407 RVLNPKERETVAYHEMGHALVALALPGTDPVHKISIVPRGIgALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLV 486
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQ-ALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  487 FGELSTGASDDLARATDIARDMITRFGMDEGLGYVAFEAQRprflDAPELVQGGCRV---AESTQTRIDQAIRDIVMGVF 563
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESD----GNVFLGRGMGKRkpySEETADIIDEEVKRLLEEAY 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 518229806  564 DRAYRILEINREVLERCARELLARETLDEYSIRQL 598
Cdd:pfam01434 156 ERAKEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
190-329 1.18e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806   190 PKGVLLVGPPGTGKTLLAKAVAGEA---GVPFFSISGSEFVE--------------MFVGVGAARVRDLFEQARGQAPAI 252
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518229806   253 IFIDELDALGRARGvggpigghdEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAgRFDRQVLVDRPD 329
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-598 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 962.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  14 VAGLLLLTLQNYWQAAKTVEPVPYSEFEKALAEGRVAEVLVSDRTVTGRLKSPDSQGKTTIVATrvEPDLAERLSKYDVP 93
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTRFTTYRVN--DPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  94 YA--RVVESTWLRDVLSWILPAVAFFGVWFFLFRRFAekQGMGGFLSIGKSRAKVFMEKNTGVTFADVAGVDEAKAELVE 171
Cdd:COG0465   79 VTakPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQ--GGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 172 IVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPA 251
Cdd:COG0465  157 IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPC 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 252 IIFIDELDALGRARGVGGPiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLVDRPDKK 331
Cdd:COG0465  237 IIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 332 GRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAAIERIVAGLERKNRVLNP 411
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 412 KERETVAYHEMGHALVALALPGTDPVHKISIVPRGiGALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLVFGELS 491
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 492 TGASDDLARATDIARDMITRFGMDEGLGYVAFEAQRPRFLDAPELVQGGcRVAESTQTRIDQAIRDIVMGVFDRAYRILE 571
Cdd:COG0465  475 TGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSR-NYSEETAREIDEEVRRIIDEAYERAKEILT 553
                        570       580
                 ....*....|....*....|....*..
gi 518229806 572 INREVLERCARELLARETLDEYSIRQL 598
Cdd:COG0465  554 ENRDKLDALAEALLEKETLDGEELEEI 580
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
101-598 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 714.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  101 TWLRDVLSWILPAVAFFGVWFFLFRRfaeKQGMGG-FLSIGKSRAKVFMEKNTGVTFADVAGVDEAKAELVEIVDFLKNP 179
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQ---MQGGGGrAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  180 QDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPAIIFIDELD 259
Cdd:TIGR01241  78 SKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEID 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  260 ALGRARGVGgPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLVDRPDKKGRLDILKV 339
Cdd:TIGR01241 158 AVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  340 HVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAAIERIVAGLERKNRVLNPKERETVAY 419
Cdd:TIGR01241 237 HAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  420 HEMGHALVALALPGTDPVHKISIVPRGIgALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLVFGELSTGASDDLA 499
Cdd:TIGR01241 317 HEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  500 RATDIARDMITRFGMDEGLGYVAFEAQRprflDAPELVQGGCR---VAESTQTRIDQAIRDIVMGVFDRAYRILEINREV 576
Cdd:TIGR01241 396 QATNIARAMVTEWGMSDKLGPVAYGSDG----GDVFLGRGFAKakeYSEETAREIDEEVKRIIEEAYKRAKQILTENRDE 471
                         490       500
                  ....*....|....*....|..
gi 518229806  577 LERCARELLARETLDEYSIRQL 598
Cdd:TIGR01241 472 LELLAKALLEKETITREEIKEL 493
ftsH CHL00176
cell division protein; Validated
78-598 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 603.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  78 RVE-----PDLAERLSKYDV---PYARVVESTWLRDVLSWILPAVAFFGVWFFLFRRFAEKQGMG-GFLSIGKSRAKVFM 148
Cdd:CHL00176  95 RVElpvgaSELIQKLKEANIdfdAHPPVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGqNLMNFGKSKARFQM 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 149 EKNTGVTFADVAGVDEAKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVE 228
Cdd:CHL00176 175 EADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVE 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 229 MFVGVGAARVRDLFEQARGQAPAIIFIDELDALGRARGVG-GpiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPE 307
Cdd:CHL00176 255 MFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiG--GGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVD 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 308 ILDQALLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVE 387
Cdd:CHL00176 333 ILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATIT 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 388 LQDFTAAIERIVAGLERKNRVLNpKERETVAYHEMGHALVALALPGTDPVHKISIVPRGiGALGYTLQRPTEDRFLMTRA 467
Cdd:CHL00176 413 MKEIDTAIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRG-QAKGLTWFTPEEDQSLVSRS 490
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 468 DLEHKIAVLLGGRAAEKLVFG--ELSTGASDDLARATDIARDMITRFGMDeGLGYVAFEAQRPRFLDAPELVQGGCRVAE 545
Cdd:CHL00176 491 QILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLGRFMQRNSEYSE 569
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518229806 546 STQTRIDQAIRDIVMGVFDRAYRILEINREVLERCARELLARETLDEYSIRQL 598
Cdd:CHL00176 570 EIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREI 622
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
8-607 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 527.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806   8 NIGYWIVAGLLLLTL-QNYWQAAKTVEPVPYSEFEKALAEGRVAEVLVSDRTVTgrLKSPDSQGKTTIVATRvEPDLAER 86
Cdd:PRK10733   4 NLILWLVIAVVLMSVfQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREIN--VTKKDSNRYTTYIPVN-DPKLLDN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  87 LSKYDVpyaRVV-----ESTWLRDV-LSWiLPAVAFFGVWFFLFRRFaekQGMGG--FLSIGKSRAKVFMEKNTGVTFAD 158
Cdd:PRK10733  81 LLTKNV---KVVgeppeEPSLLASIfISW-FPMLLLIGVWIFFMRQM---QGGGGkgAMSFGKSKARMLTEDQIKTTFAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 159 VAGVDEAKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARV 238
Cdd:PRK10733 154 VAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 239 RDLFEQARGQAPAIIFIDELDALGRARGVGGPiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGR 318
Cdd:PRK10733 234 RDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 319 FDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAAIERI 398
Cdd:PRK10733 313 FDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKI 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 399 VAGLERKNRVLNPKERETVAYHEMGHALVALALPGTDPVHKISIVPRGiGALGYTLQRPTEDRFLMTRADLEHKIAVLLG 478
Cdd:PRK10733 393 MMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRG-RALGVTFFLPEGDAISASRQKLESQISTLYG 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 479 GRAAEKLVFG--ELSTGASDDLARATDIARDMITRFGMDEGLGYVAF-EAQRPRFLDAPelVQGGCRVAESTQTRIDQAI 555
Cdd:PRK10733 472 GRLAEEIIYGpeHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYaEEEGEVFLGRS--VAKAKHMSDETARIIDQEV 549
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518229806 556 RDIVMGVFDRAYRILEINREVLERCARELLARETLDEYSIRQLTQGLQLESP 607
Cdd:PRK10733 550 KALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPP 601
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
154-325 2.75e-115

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: 340.75  E-value: 2.75e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 154 VTFADVAGVDEAKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGV 233
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 234 GAARVRDLFEQARGQAPAIIFIDELDALGRARGVGGpIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQAL 313
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGL-GGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 518229806 314 LRAGRFDRQVLV 325
Cdd:cd19501  160 LRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
153-405 8.18e-109

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 330.04  E-value: 8.18e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 153 GVTFADVAGVDEAKAELVE-IVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFV 231
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 232 GVGAARVRDLFEQARGQAPAIIFIDELDALGRARGVGGPIGghdEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQ 311
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG---EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 312 ALLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDF 391
Cdd:COG1222  231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDL 310
                        250
                 ....*....|....
gi 518229806 392 TAAIERIVAGLERK 405
Cdd:COG1222  311 EKAIEKVKKKTETA 324
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
142-406 1.93e-96

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 300.60  E-value: 1.93e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 142 SRAKVF-MEKNTGVTFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFF 219
Cdd:PRK03992 115 PRVQAMeVIESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFI 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 220 SISGSEFVEMFVGVGAARVRDLFEQARGQAPAIIFIDELDALGrARGVGGPIGGHDEREQTLNQLLTEMDGFDSSVGLII 299
Cdd:PRK03992 195 RVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIA-AKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKI 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 300 LAATNRPEILDQALLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNAT 379
Cdd:PRK03992 274 IAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
                        250       260
                 ....*....|....*....|....*..
gi 518229806 380 RRKAQAVELQDFTAAIERIVAGLERKN 406
Cdd:PRK03992 354 RDDRTEVTMEDFLKAIEKVMGKEEKDS 380
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
156-404 4.70e-76

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: 247.90  E-value: 4.70e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 156 FADVAGVDEAKAELVEIVD-FLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVG 234
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 235 AARVRDLFEQARGQAPAIIFIDELDALGRARGVGGpiGGHDEREqtLNQLLTEMDGFDSSVglIILAATNRPEILDQALL 314
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG--DGVGRRV--VNTLLTEMEELRSDV--VVIAATNRPDLLDPALL 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 315 RagRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTAA 394
Cdd:COG0464  310 R--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEA 387
                        250
                 ....*....|
gi 518229806 395 IERIVAGLER 404
Cdd:COG0464  388 LEREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
154-407 2.94e-72

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: 246.74  E-value: 2.94e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  154 VTFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVG 232
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  233 VGAARVRDLFEQARGQAPAIIFIDELDALGRARGVGGpigGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQA 312
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF---DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  313 LLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFT 392
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLE 686
                         250
                  ....*....|....*
gi 518229806  393 AAIERIVAGLERKNR 407
Cdd:TIGR01243 687 VGEEEFLKDLKVEMR 701
Peptidase_M41 pfam01434
Peptidase family M41;
407-598 4.80e-71

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 227.48  E-value: 4.80e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  407 RVLNPKERETVAYHEMGHALVALALPGTDPVHKISIVPRGIgALGYTLQRPTEDRFLMTRADLEHKIAVLLGGRAAEKLV 486
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQ-ALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  487 FGELSTGASDDLARATDIARDMITRFGMDEGLGYVAFEAQRprflDAPELVQGGCRV---AESTQTRIDQAIRDIVMGVF 563
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESD----GNVFLGRGMGKRkpySEETADIIDEEVKRLLEEAY 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 518229806  564 DRAYRILEINREVLERCARELLARETLDEYSIRQL 598
Cdd:pfam01434 156 ERAKEILTEHRDELEALAEALLEKETLDAEEIREL 190
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
154-381 1.10e-63

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: 223.25  E-value: 1.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  154 VTFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVG 232
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  233 VGAARVRDLFEQARGQAPAIIFIDELDALGRARGvggPIGGHDEReQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQA 312
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE---EVTGEVEK-RVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806  313 LLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRR 381
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
156-413 1.21e-62

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 207.43  E-value: 1.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 156 FADVAGVDEAKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGA 235
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 236 ARVRDLFEQARgQAPAIIFIDELDALGRARG----VGgpigghdEREQTLNQLLTEMDGFDSSVglIILAATNRPEILDQ 311
Cdd:COG1223   81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGdqndVG-------EVKRVVNALLQELDGLPSGS--VVIAATNHPELLDS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 312 ALLRagRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDF 391
Cdd:COG1223  151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDL 228
                        250       260
                 ....*....|....*....|..
gi 518229806 392 TAAIErivaglERKNRVLNPKE 413
Cdd:COG1223  229 EEALK------QRKERKKEPKK 244
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
155-323 1.95e-61

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: 201.41  E-value: 1.95e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 155 TFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGV 233
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 234 GAARVRDLFEQARGQAPAIIFIDELDALGRARGVGGpIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQAL 313
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSG-TGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPAL 159
                        170
                 ....*....|
gi 518229806 314 LRAGRFDRQV 323
Cdd:cd19502  160 LRPGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
148-404 1.28e-59

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 204.23  E-value: 1.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 148 MEKNTGVTFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEF 226
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 227 VEMFVGVGAARVRDLFEQARGQAPAIIFIDELDALGRARgVGGPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRP 306
Cdd:PTZ00454 216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKR-FDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRA 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 307 EILDQALLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAV 386
Cdd:PTZ00454 295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVI 374
                        250
                 ....*....|....*...
gi 518229806 387 ELQDFTAAIERIVAGLER 404
Cdd:PTZ00454 375 LPKDFEKGYKTVVRKTDR 392
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
165-325 2.32e-59

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: 195.58  E-value: 2.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 165 AKAELVEIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQ 244
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 245 ARGQAPAIIFIDELDALGRARgvgGPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVL 324
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKR---DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 518229806 325 V 325
Cdd:cd19481  158 F 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
155-398 1.00e-58

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 203.08  E-value: 1.00e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 155 TFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGV 233
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 234 GAARVRDLFEQARGQAPAIIFIDELDALGRARgVGGPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQAL 313
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKR-YDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 314 LRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLAQDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTA 393
Cdd:PTZ00361 340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRK 419

                 ....*
gi 518229806 394 AIERI 398
Cdd:PTZ00361 420 AKEKV 424
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
165-325 4.54e-57

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: 189.42  E-value: 4.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 165 AKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFE 243
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 244 QARGQAPAIIFIDELDALGRARGVGGPIGGHDereQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQV 323
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTD---RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                 ..
gi 518229806 324 LV 325
Cdd:cd19511  158 YV 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
158-323 1.86e-55

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: 185.19  E-value: 1.86e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELDALGRARgvggpigGHDEREQ---TLNQLLTEMDGFDSSVGLIILAATNRPEILDQAL 313
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKR-------EEDQREVerrVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPAL 153
                        170
                 ....*....|
gi 518229806 314 LRAGRFDRQV 323
Cdd:cd19503  154 RRPGRFDREV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
193-327 1.01e-52

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 176.63  E-value: 1.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPAIIFIDELDALGRARGVggpiG 272
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS----G 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 518229806  273 GHDEREQTLNQLLTEMDGFDSSVG-LIILAATNRPEILDQALLraGRFDRQVLVDR 327
Cdd:pfam00004  77 GDSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
165-325 3.92e-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: 173.45  E-value: 3.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 165 AKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFE 243
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 244 QARGQAPAIIFIDELDALGRARGVGgpiGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQV 323
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTT---GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157

                 ..
gi 518229806 324 LV 325
Cdd:cd19529  158 YI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
166-325 3.24e-50

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: 171.15  E-value: 3.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 166 KAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQ 244
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 245 ARGQAPAIIFIDELDALGRARG--VGGPIGGHDereQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQ 322
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGgnIGDAGGAAD---RVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQL 158

                 ...
gi 518229806 323 VLV 325
Cdd:cd19528  159 IYI 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
158-323 1.45e-46

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: 161.45  E-value: 1.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELDALGRARgvgGPIGGHDEReQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRA 316
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR---EKTHGEVER-RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                 ....*..
gi 518229806 317 GRFDRQV 323
Cdd:cd19519  157 GRFDREI 163
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
172-325 2.02e-46

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: 161.12  E-value: 2.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 172 IVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPA 251
Cdd:cd19530   12 ILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518229806 252 IIFIDELDALGRARGVGGPIGGhderEQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLV 325
Cdd:cd19530   92 VIFFDEVDALVPKRGDGGSWAS----ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
158-323 5.40e-46

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 160.26  E-value: 5.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDFLK-NPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELDALGRARGVggpiGGHDEREQTLNQLLTEMDGF----DSSVGLIILAATNRPEILDQA 312
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRES----AQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156
                        170
                 ....*....|.
gi 518229806 313 LLRAGRFDRQV 323
Cdd:cd19518  157 LRRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
165-324 4.54e-42

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: 149.12  E-value: 4.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 165 AKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFE 243
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 244 QARGQAPAIIFIDELDALGRARgvggpigGHDER---EQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFD 320
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKR-------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLD 153

                 ....
gi 518229806 321 RQVL 324
Cdd:cd19526  154 KLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
171-325 6.62e-42

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 148.82  E-value: 6.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 171 EIVDFLKNPQDYGRL---GARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARG 247
Cdd:cd19527    4 EILDTIQLPLEHPELfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806 248 QAPAIIFIDELDALGRARGVGGPIGGHDEReqTLNQLLTEMDGF-DSSVGLIILAATNRPEILDQALLRAGRFDRQVLV 325
Cdd:cd19527   84 AKPCVIFFDELDSLAPSRGNSGDSGGVMDR--VVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
159-325 7.33e-42

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: 148.65  E-value: 7.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 159 VAGVDEAKAELVEIVDF-LKNPQDYgRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAAR 237
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 238 VRDLFEQARGQAPAIIFIDELDALGRARGVggpiGGHDEREQTLNQLLTEMDGF--DSSVGLIILAATNRPEILDQALLR 315
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 518229806 316 agRFDRQVLV 325
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
154-325 2.71e-37

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: 136.53  E-value: 2.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 154 VTFADVAGVDEAKAELVEIVDF-LKNPQDYgrLGARIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFV 231
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVILpVKFPHLF--TGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 232 GVGAARVRDLFEQARGQAPAIIFIDELDALGRARGVggpiGGHDEREQTLNQLLTEMDGF-DSSVGLIILAATNRPEILD 310
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 518229806 311 QALLRagRFDRQVLV 325
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
148-325 7.84e-37

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: 135.89  E-value: 7.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 148 MEKNTGVTFADVAGVDEAKAELVEIVDF-LKNPQDYGRLGARiPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEF 226
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 227 VEMFVGVGAARVRDLFEQARGQAPAIIFIDELDALGRARGVggpiGGHDEREQTLNQLLTEMDGFDSSVG--LIILAATN 304
Cdd:cd19525   92 TSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE----GEHESSRRIKTEFLVQLDGATTSSEdrILVVGATN 167
                        170       180
                 ....*....|....*....|.
gi 518229806 305 RPEILDQALLRagRFDRQVLV 325
Cdd:cd19525  168 RPQEIDEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
158-325 1.22e-35

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: 132.03  E-value: 1.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDFLKNPQDYGRlGARIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK-GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELDALGRARGVGGPiggHDEREQTLNQLLTEMDGF-------DSSVGLIILAATNRPEIL 309
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEE---HEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 518229806 310 DQALLRagRFDRQVLV 325
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
158-315 6.90e-32

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: 121.38  E-value: 6.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDF-LKNPQ--DYGRLgARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVG 234
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPElfDNSRL-LQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 235 AARVRDLFEQARGQAPAIIFIDELDALGRARGVggpiGGHDEREQTLNQLLTEMDGFDSSVG--LIILAATNRPEILDQA 312
Cdd:cd19520   80 QKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS----TDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEA 155

                 ...
gi 518229806 313 LLR 315
Cdd:cd19520  156 ILR 158
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
158-325 2.54e-31

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: 119.57  E-value: 2.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVdFLKNPQDYGRLGARIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19524    1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELDALGRARGVggpiGGHDEREQTLNQLLTEMDGFDSSVG--LIILAATNRPEILDQALL 314
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 518229806 315 RagRFDRQVLV 325
Cdd:cd19524  156 R--RFTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
158-322 9.19e-31

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 118.38  E-value: 9.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDF-LKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAG-----VPFFSISGSEFVEMFV 231
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 232 GVGAARVRDLFEQARGQAPAIIFIDELDALGRARGvggpigghDEREQT----LNQLLTEMDGFDSSVGLIILAATNRPE 307
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRS--------SKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPD 152
                        170
                 ....*....|....*
gi 518229806 308 ILDQALLRAGRFDRQ 322
Cdd:cd19517  153 ALDPALRRPGRFDRE 167
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
179-323 6.49e-27

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 107.58  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 179 PQDYGRLGARIPKGVLLVGPPGTGKTLLAKAV-----AGEAGVpffsISGSEFVEMFVGVGAARVRDLF------EQARG 247
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeeQRRLG 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806 248 QAPA--IIFIDELDALGRARG-VGGPIGGHDereQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQV 323
Cdd:cd19504  100 ANSGlhIIIFDEIDAICKQRGsMAGSTGVHD---TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
160-326 4.15e-25

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 101.45  E-value: 4.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 160 AGVDEAKAELVEIVDflknpqdygrlgARIPKGVLLVGPPGTGKTLLAKAVAGEA---GVPFFSISGSEFVEMFVG---V 233
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 234 GAARVRDLFEQARGQAPAIIFIDELDALGRargvggpigghDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQAL 313
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR-----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                        170
                 ....*....|...
gi 518229806 314 LRAGRFDRQVLVD 326
Cdd:cd00009  138 ALYDRLDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
151-406 1.27e-22

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 101.63  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 151 NTGVTFADVAGVDEAKAELVEIVD-FLKNPQDYGrlgARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEM 229
Cdd:CHL00195 222 SVNEKISDIGGLDNLKDWLKKRSTsFSKQASNYG---LPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 230 FVGVGAARVRDLFEQARGQAPAIIFIDELD---ALGRARGVGGPIGghdereQTLNQLLTEMDGFDSSVglIILAATNRP 306
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDkafSNSESKGDSGTTN------RVLATFITWLSEKKSPV--FVVATANNI 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 307 EILDQALLRAGRFDRQVLVDRPDKKGRLDILKVHVKKVTLA--QDIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQ 384
Cdd:CHL00195 371 DLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKRE 450
                        250       260
                 ....*....|....*....|....
gi 518229806 385 aVELQDFTAAIERIV--AGLERKN 406
Cdd:CHL00195 451 -FTTDDILLALKQFIplAQTEKEQ 473
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
158-325 1.45e-21

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: 91.87  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAELVEIVDF-LKNPQDYGRLgARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELDALGRARGVGGPIGGhdeREQTlnQLLTEMDGFDSSV--GLIILAATNRPEILDQALL 314
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG---RLQV--ELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLR 154
                        170
                 ....*....|.
gi 518229806 315 RagRFDRQVLV 325
Cdd:cd19523  155 R--YFSKRLLV 163
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
171-325 7.21e-21

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: 89.33  E-value: 7.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 171 EIVDFLKNPQDYGRLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEfvemfVGVGAARVRDLFEQARGQap 250
Cdd:cd19510    4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ-- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518229806 251 AIIFIDELDA--LGRARGVGGPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDRQVLV 325
Cdd:cd19510   77 SIILLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
158-321 3.45e-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: 84.73  E-value: 3.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 158 DVAGVDEAKAEL-VEIVDFLKNPQDYGrlgARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAA 236
Cdd:cd19507    1 DVGGLDNLKDWLkKRKAAFSKQASAYG---LPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 237 RVRDLFEQARGQAPAIIFIDELD-ALGRARGVGGpiGGHDEReqTLNQLLTEMDGFDSSVglIILAATNRPEILDQALLR 315
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGD--SGTSSR--VLGTFLTWLQEKKKPV--FVVATANNVQSLPPELLR 151

                 ....*.
gi 518229806 316 AGRFDR 321
Cdd:cd19507  152 KGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
190-329 1.18e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806   190 PKGVLLVGPPGTGKTLLAKAVAGEA---GVPFFSISGSEFVE--------------MFVGVGAARVRDLFEQARGQAPAI 252
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518229806   253 IFIDELDALGRARGvggpigghdEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAgRFDRQVLVDRPD 329
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
349-393 8.28e-13

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 62.94  E-value: 8.28e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 518229806  349 DIDLEQVAALTTGFSGADLANLVNEAALNATRRKAQAVELQDFTA 393
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
191-323 2.38e-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: 59.08  E-value: 2.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 191 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGvGAARVRDLFEQA-RGQAPAIIFIDELDALGRARGVGG 269
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518229806 270 PigGHDEReQTLNQLLTEMDgfDSSVGLIILAATNRPEILDQALlrAGRFDRQV 323
Cdd:cd19512  102 I--SEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
PRK04195 PRK04195
replication factor C large subunit; Provisional
155-266 3.92e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 62.25  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 155 TFADVAGVDEAKAELVE-IVDFLKNpqdygrlgaRIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEF-----VE 228
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREwIESWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518229806 229 MFVGvGAARVRDLFEQARgqapAIIFIDELDAL-GRA-RG 266
Cdd:PRK04195  83 RVAG-EAATSGSLFGARR----KLILLDEVDGIhGNEdRG 117
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
184-321 6.45e-10

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 58.16  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 184 RLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFV--------------EMFVGVGAARVRDLFEQARGQA 249
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518229806 250 PAIIFIDELDALGRARgvggpiGGHDEREQT------LNQLLTEMDGFDSSVGLIILAATNRPEILDQALLRAGRFDR 321
Cdd:cd19505   86 PCIIWIPNIHELNVNR------STQNLEEDPklllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
189-270 7.22e-10

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: 58.55  E-value: 7.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 189 IPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEM-FVGvgaarvRDLFEQARGQAPAIIFIDELDALGRARGV 267
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGS 118

                 ...
gi 518229806 268 GGP 270
Cdd:cd19498  119 SGP 121
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
183-226 1.42e-08

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 57.29  E-value: 1.42e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 518229806 183 GRLGARipkGVLLVGPPGTGKTLLAKAVAGEAG--VPFFSISGSEF 226
Cdd:COG1224   60 GKMAGK---GILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
193-257 1.68e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.02  E-value: 1.68e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSefvemFVGVgaARVRDLFEQAR-----GQAPaIIFIDE 257
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARqrrsaGRRT-ILFIDE 100
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
193-257 1.98e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 56.99  E-value: 1.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGsefvemfVGVGAARVRDLFEQARGQA----PAIIFIDE 257
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
172-226 3.44e-08

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: 55.78  E-value: 3.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518229806  172 IVDFLKNpqdyGRLGARipkGVLLVGPPGTGKTLLAKAVAGEAG--VPFFSISGSEF 226
Cdd:pfam06068  39 IVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
ycf2 CHL00206
Ycf2; Provisional
184-442 5.92e-08

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 56.07  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  184 RLGARIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVE----------------------------------- 228
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDnkpkgfliddididdsddiddsddidrdldtellt 1703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  229 --------MFVGVGAARVRDLFEQARGQAPAIIFIDELDALGRargvggpiggHDEREQTLNQLLTEM--DGFDSSVG-L 297
Cdd:CHL00206 1704 mmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNV----------NESNYLSLGLLVNSLsrDCERCSTRnI 1773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  298 IILAATNRPEILDQALLRAGRFDRQVLVDR---PDKKGRLDILkVHVKKVTLAQDI-DLEQVAALTTGFSGADLANLVNE 373
Cdd:CHL00206 1774 LVIASTHIPQKVDPALIAPNKLNTCIKIRRlliPQQRKHFFTL-SYTRGFHLEKKMfHTNGFGSITMGSNARDLVALTNE 1852
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806  374 AALNATRRKAQAVELQDFTAAIERIVAGLerKNRVLNPKERETVAYhEMGHALVALALPGTDPVHKISI 442
Cdd:CHL00206 1853 ALSISITQKKSIIDTNTIRSALHRQTWDL--RSQVRSVQDHGILFY-QIGRAVAQNVLLSNCPIDPISI 1918
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
193-331 1.73e-06

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 48.98  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGV---------------------PFFSISGSEFVEMFvgvgaARVRDLFEQARgqapA 251
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDDKD----A 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 252 IIF--IDELDALGRARGVGGPIGGHDEREQTLNQLLTEMDGFDSSVGLIILAATNRPEILDQAllragrfdrqvLVDRPD 329
Cdd:cd19508  126 LVFvlIDEVESLAAARSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA-----------FVDRAD 194

                 ..
gi 518229806 330 KK 331
Cdd:cd19508  195 IK 196
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
193-358 3.24e-06

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: 49.40  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPFF----------------SISGSEFVEMFVGVGAarvrdLFEQargqapaIIFID 256
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGP-----LFAN-------VLLAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 257 ELDalgRArgvggpigghdeREQTLNQLLTEMDGFDSSVG---------LIILAATNRPEI-----LDQALLRagRFDRQ 322
Cdd:COG0714  102 EIN---RA------------PPKTQSALLEAMEERQVTIPggtyklpepFLVIATQNPIEQegtypLPEAQLD--RFLLK 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 518229806 323 VLVDRPDKKGRLDILKVHV--KKVTLAQDIDLEQVAAL 358
Cdd:COG0714  165 LYIGYPDAEEEREILRRHTgrHLAEVEPVLSPEELLAL 202
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
190-259 3.54e-06

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 47.58  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  190 PKGV-LLVGPPGTGKTLLAKAVAGEAGV---PFFSISGSEFVE-----MFVGVGAARVR-----DLFEQARGQAPAIIFI 255
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                  ....
gi 518229806  256 DELD 259
Cdd:pfam07724  82 DEIE 85
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
9-94 5.56e-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: 45.29  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806    9 IGYWIVAGLLLLTLQNY-WQAAKTVEPVPYSEFEKALAEGRVAEVLVSDRTVTGRL-----KSPDSQGKTTIVATRVEPD 82
Cdd:pfam06480   2 LLWLLILLVLLLLFLLFlLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILPTGvvegtLKDGSKFTTYFIPSLPNVD 81
                          90
                  ....*....|....*..
gi 518229806   83 -----LAERLSKYDVPY 94
Cdd:pfam06480  82 sllekLEDALEEKGVKV 98
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
192-319 7.50e-06

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: 45.75  E-value: 7.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  192 GVLLVGPPGTGKTLLAKAVAgEA--GVPFFSISGSEFVE-------MFVGVGAARVRDLFEQARGQAPAIIFIDELDalg 262
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDGPLVRAAREGEIAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518229806  263 RARG-----VGGPIgghDEREQTLNQLLTEMDGFDSSVGLIilAATNRPEI----LDQALLRagRF 319
Cdd:pfam07728  77 RANPdvlnsLLSLL---DERRLLLPDGGELVKAAPDGFRLI--ATMNPLDRglneLSPALRS--RF 135
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
190-437 1.88e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 190 PKGVLLVGPPGTGKTLLAKAV-------AGEAGVPF-------------FSISgSEFVEMFV--------GVGAARVRDL 241
Cdd:COG1474   51 PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVrvvyvncrqastrYRVL-SRILEELGsgedipstGLSTDELFDR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 242 FEQA--RGQAPAIIFIDELDALgrargvggpigGHDEREQTLNQLLTEMDGFDSS-VGLIilAATNRPEI---LDQALLR 315
Cdd:COG1474  130 LYEAldERDGVLVVVLDEIDYL-----------VDDEGDDLLYQLLRANEELEGArVGVI--GISNDLEFlenLDPRVKS 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 316 agRF-DRQVLVDRPDKKGRLDILKVHVKKV----TLAQDIdLEQVAALTTGFSG-ADLA-NLVNEAALNATRRKAQAVEL 388
Cdd:COG1474  197 --SLgEEEIVFPPYDADELRDILEDRAELAfydgVLSDEV-IPLIAALAAQEHGdARKAiDLLRVAGEIAEREGSDRVTE 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518229806 389 QDFTAAIERIvagleRKNRV------LNPKERETVAyhemghALVALALPGTDPV 437
Cdd:COG1474  274 EHVREAREKI-----ERDRLlevlrgLPTHEKLVLL------AIAELLKDGEDPV 317
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
193-310 5.05e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 42.88  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEA---GVPFFSISgseFVEMFVgvgaARVRDLFEQARgqaPAIIFIDELDALGRARgvgg 269
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARAS---- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518229806 270 pigGHDEREQTLNQLLTEMDGFDSSvGLIILAATNRPEILD 310
Cdd:cd01120   67 ---QGDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDI 103
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
194-289 8.14e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 45.61  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  194 LLVGPPGTGKTLLAKAVAGE-AGVPFFS------ISGSEFVEMFVGVGAARVRDLFEQARGqapAIIFIDELDAL-GRAR 265
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLvETGY 392
                          90       100
                  ....*....|....*....|....
gi 518229806  266 GVGGPIGGhdereQTLNQLLTEMD 289
Cdd:TIGR03922 393 GQKDPFGL-----EAIDTLLARME 411
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
159-269 1.07e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 44.13  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 159 VAGVDEAKAEL-VEIVDFLK---NPQDYGRLGARIPKG-VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEM-FVG 232
Cdd:cd19497   14 VIGQERAKKVLsVAVYNHYKrirNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVG 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 518229806 233 --VGAARVRDL----FEQARGQApAIIFIDELDALGRA-------RGVGG 269
Cdd:cd19497   94 edVENILLKLLqaadYDVERAQR-GIVYIDEIDKIARKsenpsitRDVSG 142
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
193-223 2.25e-04

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: 42.10  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 518229806  193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 223
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
193-223 2.40e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.58  E-value: 2.40e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 223
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 84
44 PHA02544
clamp loader, small subunit; Provisional
188-264 2.59e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.44  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 188 RIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEfvemfvgvgaARVRDLFEQARGQA--------PAIIFIDELD 259
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD----------CRIDFVRNRLTRFAstvsltggGKVIIIDEFD 110

                 ....*
gi 518229806 260 ALGRA 264
Cdd:PHA02544 111 RLGLA 115
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
157-222 3.36e-04

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: 41.78  E-value: 3.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518229806 157 ADVAGVDEAKAElveIVDFLKNPQDYGRLGARIpkgVLLVGPPGTGKTLLAKAVAGEAGVPFFSIS 222
Cdd:cd19500   10 ADHYGLEDVKER---ILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRIS 69
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
185-318 8.90e-04

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 40.66  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 185 LGARIPKG--VLLVGPPGTGKTLLAKAVAGEA----------GVPFFSISGSEF----------VEMFVGV-------GA 235
Cdd:cd03246   21 VSFSIEPGesLAIIGPSGSGKSTLARLILGLLrptsgrvrldGADISQWDPNELgdhvgylpqdDELFSGSiaenilsGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 236 ARVRDLFEQARGQAPAIIFIDE----LDalgrargvggpigghDEREQTLNQLLTEMDGFDSSVGLIilaaTNRPEILDQ 311
Cdd:cd03246  101 QRQRLGLARALYGNPRILVLDEpnshLD---------------VEGERALNQAIAALKAAGATRIVI----AHRPETLAS 161
                        170
                 ....*....|.
gi 518229806 312 A----LLRAGR 318
Cdd:cd03246  162 AdrilVLEDGR 172
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
191-257 1.04e-03

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. 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: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 40.20  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806 191 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGAAR--VRDLFEQARGQAPAIIFIDE 257
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGD 95
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
193-218 1.21e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 41.57  E-value: 1.21e-03
                         10        20
                 ....*....|....*....|....*.
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPF 218
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVPF 137
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
193-223 1.23e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 41.22  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 223
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
193-218 1.38e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 41.30  E-value: 1.38e-03
                         10        20
                 ....*....|....*....|....*.
gi 518229806 193 VLLVGPPGTGKTLLAKAVAGEAGVPF 218
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF 136
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
193-264 1.46e-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: 41.13  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518229806  193 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVemfvgvgaaRVRDLFEQARG-QAPAIIFIDELDALGRA 264
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAILTNlEEGDVLFIDEIHRLSPA 96
AAA_22 pfam13401
AAA domain;
184-309 1.48e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  184 RLGARIpkgVLLVGPPGTGKTLLAKAVA---GEAGVPFFSI------SGSEFVEMFV------GVGAARVRDLFEQ---- 244
Cdd:pfam13401   2 RFGAGI---LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAAlqql 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518229806  245 -ARGQAPAIIFIDELDALgrargvggpigghdeREQTLNQLLTEMDGFDSSVGLIILAATNRPEIL 309
Cdd:pfam13401  79 lLALAVAVVLIIDEAQHL---------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
Sigma54_activat pfam00158
Sigma-54 interaction domain;
187-340 2.80e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 38.92  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  187 ARIPKGVLLVGPPGTGKTLLAKAV---AGEAGVPFFSI-----------SgsefvEMFvGV------GAARVRD-LFEQA 245
Cdd:pfam00158  19 APTDAPVLITGESGTGKELFARAIhqlSPRADGPFVAVncaaipeelleS-----ELF-GHekgaftGADSDRKgLFELA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  246 RGqapAIIFIDE---LDALGRAR-------GVGGPIGGHDEReqtlnqlltemdgfdsSVGLIILAATNRPeiLDQAlLR 315
Cdd:pfam00158  93 DG---GTLFLDEigeLPLELQAKllrvlqeGEFERVGGTKPI----------------KVDVRIIAATNRD--LEEA-VA 150
                         170       180
                  ....*....|....*....|....*
gi 518229806  316 AGRFdrqvlvdRPDKKGRLDILKVH 340
Cdd:pfam00158 151 EGRF-------REDLYYRLNVIPIE 168
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
194-259 2.84e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 39.08  E-value: 2.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518229806 194 LLVGPPGTGKTLLAKAVAGE---AGVPFFSISGSEFVEMFVG----------VGAARVRDLFEQARGQAPAIIFIDELD 259
Cdd:cd19499   45 LFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
182-288 3.21e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.64  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806  182 YGRLGARIPKGVLLVGPPGTGKTLLAKAV---AGEAGVPFFSISGSEFVEMFVGVGAARVRDLFEQARGQAPAIIFIDEL 258
Cdd:pfam13191  16 LDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEALTREGLLRQLLDELESSLLEAWR 95
                          90       100       110
                  ....*....|....*....|....*....|
gi 518229806  259 DALGRARGVGGPIGGHDEREqtLNQLLTEM 288
Cdd:pfam13191  96 AALLEALAPVPELPGDLAER--LLDLLLRL 123
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
193-212 3.69e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 40.02  E-value: 3.69e-03
                         10        20
                 ....*....|....*....|
gi 518229806 193 VLLVGPPGTGKTLLAKAVAG 212
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
154-211 4.00e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.14  E-value: 4.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518229806 154 VTFADVAGVDEAKAELVEIVDFL--KNPQDYGRLGA--RIPKGVLLVGPPGTGKTLLAKAVA 211
Cdd:COG1401  181 LSAAEELYSEDLESEDDYLKDLLreKFEETLEAFLAalKTKKNVILAGPPGTGKTYLARRLA 242
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
193-212 4.98e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.67  E-value: 4.98e-03
                          10        20
                  ....*....|....*....|
gi 518229806  193 VLLVGPPGTGKTLLAKAVAG 212
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
185-300 7.16e-03

RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 38.45  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518229806 185 LGARIPKGVL--LVGPPGTGKTLLAKAVAGEAGVPfFSISGSEFVEMFVGVG----AARVRDLFEQARGQAPAIIFIDEL 258
Cdd:cd19493    4 LAGGLPLGAIteITGASGSGKTQFALTLASSAAMP-ARKGGLDGGVLYIDTEskfsAERLAEIAEARFPEAFSGFMEENE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 518229806 259 DALGRARGVggpiggHDEREQTLNQLLTEMDG-----FDSSVGLIIL 300
Cdd:cd19493   83 RAEEMLKRV------AVVRVTTLAQLLERLPNleehiLSSGVRLVVI 123
 
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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