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Conserved domains on  [gi|519017463|ref|WP_020173338|]
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ATP-dependent zinc metalloprotease FtsH [Methyloferula stellata]

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];
14-599 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1095.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  14 VFLLVVALVMLFQNPGQRVasTDITFSQLLNEVDQGRVREVTISGNEINGHYTD--NRAFATYAPNDPTLVQTLYKKNVA 91
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSV--KEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDgtKTRFTTYRVNDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  92 ISAKPPSDgNSWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGKAMGFGKSKAKLLTEAHGRVTFEDVAGVDEAKEDLQEI 171
Cdd:COG0465   79 VTAKPPEE-SSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 172 VEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCI 251
Cdd:COG0465  158 VDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 252 IFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIVVPNPDIVGR 331
Cdd:COG0465  238 IFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 332 ERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAERRTLVMTEKE 411
Cdd:COG0465  318 EAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 412 KELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFGweKVTS 491
Cdd:COG0465  398 KKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTT 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 492 GAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEATRIITEK 571
Cdd:COG0465  476 GASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTEN 555
                        570       580
                 ....*....|....*....|....*...
gi 519017463 572 RADLEVLAKGLLEYETLSGDEIIGLLQG 599
Cdd:COG0465  556 RDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-599 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1095.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  14 VFLLVVALVMLFQNPGQRVasTDITFSQLLNEVDQGRVREVTISGNEINGHYTD--NRAFATYAPNDPTLVQTLYKKNVA 91
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSV--KEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDgtKTRFTTYRVNDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  92 ISAKPPSDgNSWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGKAMGFGKSKAKLLTEAHGRVTFEDVAGVDEAKEDLQEI 171
Cdd:COG0465   79 VTAKPPEE-SSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 172 VEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCI 251
Cdd:COG0465  158 VDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 252 IFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIVVPNPDIVGR 331
Cdd:COG0465  238 IFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 332 ERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAERRTLVMTEKE 411
Cdd:COG0465  318 EAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 412 KELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFGweKVTS 491
Cdd:COG0465  398 KKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTT 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 492 GAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEATRIITEK 571
Cdd:COG0465  476 GASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTEN 555
                        570       580
                 ....*....|....*....|....*...
gi 519017463 572 RADLEVLAKGLLEYETLSGDEIIGLLQG 599
Cdd:COG0465  556 RDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
102-597 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: 852.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  102 SWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGKAMGFGKSKAKLLTEAHGRVTFEDVAGVDEAKEDLQEIVEFLRDPQKF 181
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  182 QRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVG 261
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  262 RHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIVVPNPDIVGRERILKVHVRK 341
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  342 VPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAERRTLVMTEKEKELTAYHEGG 421
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  422 HAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFGweKVTSGAQSDIEQAT 501
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  502 KLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEATRIITEKRADLEVLAKG 581
Cdd:TIGR01241 399 NIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*.
gi 519017463  582 LLEYETLSGDEIIGLL 597
Cdd:TIGR01241 479 LLEKETITREEIKELL 494
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
6-633 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 776.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463   6 RNFALWVIVfllVVALVMLFQNPGQRVA-STDITFSQLLNEVDQGRVREVTISGNEINGHYTDNRAFATYAP-NDPTLVQ 83
Cdd:PRK10733   3 KNLILWLVI---AVVLMSVFQSFGPSESnGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPvNDPKLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  84 TLYKKNVAISAKPPSDgNSWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGK-AMGFGKSKAKLLTEAHGRVTFEDVAGVD 162
Cdd:PRK10733  80 NLLTKNVKVVGEPPEE-PSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKgAMSFGKSKARMLTEDQIKTTFADVAGCD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 163 EAKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFE 242
Cdd:PRK10733 159 EAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 243 QAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIV 322
Cdd:PRK10733 239 QAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 323 VPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAER 402
Cdd:PRK10733 319 VGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAER 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 403 RTLVMTEKEKELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEI 482
Cdd:PRK10733 399 RSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEI 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 483 VFGWEKVTSGAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHA 562
Cdd:PRK10733 479 IYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYN 558
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519017463 563 EATRIITEKRADLEVLAKGLLEYETLSGDEIIGLLqGRRPVREVAEEPAPVRA--------PTSPVPTTGTSRPRPGPE 633
Cdd:PRK10733 559 RARQLLTDNMDILHAMKDALMKYETIDAPQIDDLM-ARRDVRPPAGWEEPGASnnsddngtPKAPRPVDEPRTPNPGNT 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
153-323 1.76e-128

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: 375.42  E-value: 1.76e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGV 232
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 233 GASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALL 312
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 519017463 313 RPGRFDRQIVV 323
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
406-596 1.03e-85

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 266.00  E-value: 1.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  406 VMTEKEKELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFG 485
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  486 weKVTSGAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEAT 565
Cdd:pfam01434  82 --EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 519017463  566 RIITEKRADLEVLAKGLLEYETLSGDEIIGL 596
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
189-327 3.53e-22

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: 93.21  E-value: 3.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463   189 PRGVLLVGPPGTGKTLLARAIAGEANVP---FFTISGSDFVE--------------MFVGVGASRVRDMFEQAKKNAPCI 251
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519017463   252 IFIDEIDAVGRHRGaglgggndEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPgRFDRQIVVPNPD 327
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
192-227 8.08e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.22  E-value: 8.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEA-----NVPFFTIsgSDFVE 227
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-599 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1095.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  14 VFLLVVALVMLFQNPGQRVasTDITFSQLLNEVDQGRVREVTISGNEINGHYTD--NRAFATYAPNDPTLVQTLYKKNVA 91
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSV--KEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDgtKTRFTTYRVNDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  92 ISAKPPSDgNSWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGKAMGFGKSKAKLLTEAHGRVTFEDVAGVDEAKEDLQEI 171
Cdd:COG0465   79 VTAKPPEE-SSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 172 VEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCI 251
Cdd:COG0465  158 VDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 252 IFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIVVPNPDIVGR 331
Cdd:COG0465  238 IFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 332 ERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAERRTLVMTEKE 411
Cdd:COG0465  318 EAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 412 KELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFGweKVTS 491
Cdd:COG0465  398 KKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTT 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 492 GAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEATRIITEK 571
Cdd:COG0465  476 GASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTEN 555
                        570       580
                 ....*....|....*....|....*...
gi 519017463 572 RADLEVLAKGLLEYETLSGDEIIGLLQG 599
Cdd:COG0465  556 RDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
102-597 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: 852.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  102 SWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGKAMGFGKSKAKLLTEAHGRVTFEDVAGVDEAKEDLQEIVEFLRDPQKF 181
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  182 QRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVG 261
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  262 RHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIVVPNPDIVGRERILKVHVRK 341
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  342 VPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAERRTLVMTEKEKELTAYHEGG 421
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  422 HAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFGweKVTSGAQSDIEQAT 501
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  502 KLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEATRIITEKRADLEVLAKG 581
Cdd:TIGR01241 399 NIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKA 478
                         490
                  ....*....|....*.
gi 519017463  582 LLEYETLSGDEIIGLL 597
Cdd:TIGR01241 479 LLEKETITREEIKELL 494
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
6-633 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 776.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463   6 RNFALWVIVfllVVALVMLFQNPGQRVA-STDITFSQLLNEVDQGRVREVTISGNEINGHYTDNRAFATYAP-NDPTLVQ 83
Cdd:PRK10733   3 KNLILWLVI---AVVLMSVFQSFGPSESnGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPvNDPKLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  84 TLYKKNVAISAKPPSDgNSWLVTLLVNGLPLIAFLGVWIFLSRQMQGAGGK-AMGFGKSKAKLLTEAHGRVTFEDVAGVD 162
Cdd:PRK10733  80 NLLTKNVKVVGEPPEE-PSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKgAMSFGKSKARMLTEDQIKTTFADVAGCD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 163 EAKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFE 242
Cdd:PRK10733 159 EAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 243 QAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIV 322
Cdd:PRK10733 239 QAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 323 VPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAER 402
Cdd:PRK10733 319 VGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAER 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 403 RTLVMTEKEKELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEI 482
Cdd:PRK10733 399 RSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEI 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 483 VFGWEKVTSGAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHA 562
Cdd:PRK10733 479 IYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYN 558
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519017463 563 EATRIITEKRADLEVLAKGLLEYETLSGDEIIGLLqGRRPVREVAEEPAPVRA--------PTSPVPTTGTSRPRPGPE 633
Cdd:PRK10733 559 RARQLLTDNMDILHAMKDALMKYETIDAPQIDDLM-ARRDVRPPAGWEEPGASnnsddngtPKAPRPVDEPRTPNPGNT 636
ftsH CHL00176
cell division protein; Validated
77-593 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 638.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  77 NDPTLVQTLYKKNVAISAKPPSDGNSWLVTLLVNGLPLIAFLGVWIFLSR---QMQGAGGKAMGFGKSKAKLLTEAHGRV 153
Cdd:CHL00176 101 GASELIQKLKEANIDFDAHPPVLKSNIVTILSNLLLPLILIGVLWFFFQRssnFKGGPGQNLMNFGKSKARFQMEADTGI 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 154 TFEDVAGVDEAKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVG 233
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVG 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 234 ASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLR 313
Cdd:CHL00176 261 AARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLR 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 314 PGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAK 393
Cdd:CHL00176 341 PGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAI 420
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 394 DKIMMGAERRTLVMTeKEKELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVL 473
Cdd:CHL00176 421 DRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGA 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 474 MAGRVSEEIVFGWEKVTSGAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEV 553
Cdd:CHL00176 500 LGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRFMQRNSEYSEEIADKIDMEV 579
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 519017463 554 RRLVEAGHAEATRIITEKRADLEVLAKGLLEYETLSGDEI 593
Cdd:CHL00176 580 RSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEF 619
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
153-323 1.76e-128

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: 375.42  E-value: 1.76e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGV 232
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 233 GASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALL 312
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 519017463 313 RPGRFDRQIVV 323
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
153-404 9.03e-118

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 353.93  E-value: 9.03e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVE-FLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVG 231
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 232 VGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGndEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPAL 311
Cdd:COG1222  155 EGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPAL 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 312 LRPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFED 391
Cdd:COG1222  233 LRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEK 312
                        250
                 ....*....|...
gi 519017463 392 AKDKIMMGAERRT 404
Cdd:COG1222  313 AIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
153-409 8.91e-105

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 322.94  E-value: 8.91e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVG 231
Cdd:PRK03992 128 VTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIG 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 232 VGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPAL 311
Cdd:PRK03992 208 EGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAI 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 312 LRPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFED 391
Cdd:PRK03992 288 LRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLK 367
                        250
                 ....*....|....*...
gi 519017463 392 AKDKIMMGAERRTLVMTE 409
Cdd:PRK03992 368 AIEKVMGKEEKDSMEEPG 385
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
153-397 3.52e-90

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 284.38  E-value: 3.52e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  153 VTFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVG 231
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  232 VGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPAL 311
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  312 LRPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFED 391
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358

                  ....*.
gi 519017463  392 AKDKIM 397
Cdd:TIGR01242 359 AVEKVL 364
Peptidase_M41 pfam01434
Peptidase family M41;
406-596 1.03e-85

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 266.00  E-value: 1.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  406 VMTEKEKELTAYHEGGHAIVALNVIATDPVHKATIIPRGRAMGMVMQLPERDKLSMSYEQMTSRLAVLMAGRVSEEIVFG 485
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  486 weKVTSGAQSDIEQATKLARAMVTRWGFSEELGTVMYGENQEEVFLGYSMGRQQNISEATSQKIDAEVRRLVEAGHAEAT 565
Cdd:pfam01434  82 --EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 519017463  566 RIITEKRADLEVLAKGLLEYETLSGDEIIGL 596
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
144-402 4.07e-82

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: 264.47  E-value: 4.07e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 144 KLLTEAHGRVTFEDVAGVDEAKEDLQEIVE-FLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISG 222
Cdd:COG0464  145 EEELLELREAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 223 SDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGaGLGGGNDEREqtLNQLLVEMDGFEanEGIILIAATN 302
Cdd:COG0464  225 SDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELR--SDVVVIAATN 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 303 RPDVLDPALLRpgRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKR 382
Cdd:COG0464  300 RPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377
                        250       260
                 ....*....|....*....|
gi 519017463 383 IVTMVEFEDAKDKIMMGAER 402
Cdd:COG0464  378 PVTTEDLLEALEREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
153-397 3.14e-74

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: 252.52  E-value: 3.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  153 VTFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVG 231
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  232 VGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEReqTLNQLLVEMDGFEANEGIILIAATNRPDVLDPAL 311
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPAL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  312 LRPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFED 391
Cdd:TIGR01243 608 LRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEV 687

                  ....*.
gi 519017463  392 AKDKIM 397
Cdd:TIGR01243 688 GEEEFL 693
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
152-379 4.60e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 235.96  E-value: 4.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  152 RVTFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFV 230
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  231 GVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGggnDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPA 310
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519017463  311 LLRPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARR 379
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
154-321 4.72e-68

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 219.52  E-value: 4.72e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 154 TFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGV 232
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 233 GASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALL 312
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*....
gi 519017463 313 RPGRFDRQI 321
Cdd:cd19502  161 RPGRFDRKI 169
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
155-396 5.03e-66

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 216.67  E-value: 5.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 155 FEDVAGVDEAKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGA 234
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 235 SRVRDMFEQAkKNAPCIIFIDEIDAVGRHRGAGLGGGndEREQTLNQLLVEMDGFeaNEGIILIAATNRPDVLDPALLRp 314
Cdd:COG1223   81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 315 gRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDAKD 394
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 ..
gi 519017463 395 KI 396
Cdd:COG1223  234 QR 235
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
164-321 2.97e-65

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: 211.37  E-value: 2.97e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 164 AKEDLQEIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQ 243
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519017463 244 AKKNAPCIIFIDEIDAVGRHRGAglGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQI 321
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
154-397 1.56e-64

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 219.26  E-value: 1.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 154 TFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGV 232
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 233 GASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALL 312
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 313 RPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFEDA 392
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                 ....*
gi 519017463 393 KDKIM 397
Cdd:PTZ00361 421 KEKVL 425
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
153-392 4.35e-63

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 214.24  E-value: 4.35e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVG 231
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 232 VGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPAL 311
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 312 LRPGRFDRQIVVPNPDIVGRERILKVHVRKVPLAPDVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFED 391
Cdd:PTZ00454 302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEK 381

                 .
gi 519017463 392 A 392
Cdd:PTZ00454 382 G 382
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
164-323 9.58e-63

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: 204.82  E-value: 9.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 164 AKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFE 242
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 243 QAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEReqTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIV 322
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 519017463 323 V 323
Cdd:cd19511  159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
157-323 2.18e-58

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 193.66  E-value: 2.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGAS 235
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 236 RVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGlGGGNDEReqTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPG 315
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*...
gi 519017463 316 RFDRQIVV 323
Cdd:cd19503  158 RFDREVEI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
192-324 1.21e-56

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: 187.80  E-value: 1.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  192 VLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGaglGGG 271
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 519017463  272 NDEREQTLNQLLVEMDGFEANEG-IILIAATNRPDVLDPALLrpGRFDRQIVVP 324
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
164-323 4.00e-56

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: 187.32  E-value: 4.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 164 AKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFE 242
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 243 QAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEReqTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIV 322
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 519017463 323 V 323
Cdd:cd19529  159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
165-323 1.99e-55

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: 185.79  E-value: 1.99e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 165 KEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQ 243
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 244 AKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQIVV 323
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 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 ...
157-324 3.47e-53

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: 179.94  E-value: 3.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGAS 235
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 236 RVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGggnDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPG 315
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHG---EVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 519017463 316 RFDRQIVVP 324
Cdd:cd19519  158 RFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
161-323 1.35e-48

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 167.28  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 161 VDEAKEDLQ-EIVEFLRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRD 239
Cdd:cd19530    1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 240 MFEQAKKNAPCIIFIDEIDAVGRHRGaglGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDR 319
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                 ....
gi 519017463 320 QIVV 323
Cdd:cd19530  158 TLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
157-321 1.37e-48

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 167.58  E-value: 1.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEFL-RDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGAS 235
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 236 RVRDMFEQAKKNAPCIIFIDEIDAVGRHRGaglGGGNDEREQTLNQLLVEMDGFEANE----GIILIAATNRPDVLDPAL 311
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 519017463 312 LRPGRFDRQI 321
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
164-321 1.21e-44

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 156.43  E-value: 1.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 164 AKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFE 242
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519017463 243 QAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDereQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQI 321
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
158-323 2.86e-44

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: 155.59  E-value: 2.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 158 VAGVDEAKEDLQEIV--EFLRdPQKFqRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGAS 235
Cdd:cd19509    1 IAGLDDAKEALKEAVilPSLR-PDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 236 RVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAglggGNDEREQTL-NQLLVEMDGFEA--NEGIILIAATNRPDVLDPALL 312
Cdd:cd19509   79 IVRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNkpEDRVLVLGATNRPWELDEAFL 154
                        170
                 ....*....|.
gi 519017463 313 RpgRFDRQIVV 323
Cdd:cd19509  155 R--RFEKRIYI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
165-323 1.58e-40

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: 145.35  E-value: 1.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 165 KEDLQEIVEF-LRDPQKFQrLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQ 243
Cdd:cd19527    2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 244 AKKNAPCIIFIDEIDAVGRHRGA-GLGGGNDEReqTLNQLLVEMDGFE-ANEGIILIAATNRPDVLDPALLRPGRFDRQI 321
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 519017463 322 VV 323
Cdd:cd19527  159 YL 160
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
153-323 3.30e-40

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: 144.62  E-value: 3.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVEFlrdPQKFQRL--GGRIP-RGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMF 229
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 230 VGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAglgGGNDEREQTLNQLLVEMDGF-EANEGIILIAATNRPDVLD 308
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 519017463 309 PALLRpgRFDRQIVV 323
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
157-320 2.54e-38

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: 139.57  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEF-LRDPQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEAN-----VPFFTISGSDFVEMFV 230
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 231 GVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAglgggndEREQT----LNQLLVEMDGFEANEGIILIAATNRPDV 306
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....
gi 519017463 307 LDPALLRPGRFDRQ 320
Cdd:cd19517  154 LDPALRRPGRFDRE 167
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
157-323 2.46e-32

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 122.65  E-value: 2.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEFLRD-PQKFQRLGgRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGAS 235
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLrPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 236 RVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAglgGGNDEREQTLNQLLVEMDGFEAN--EGIILIAATNRPDVLDPALLR 313
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 519017463 314 pgRFDRQIVV 323
Cdd:cd19524  157 --RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
157-323 5.00e-32

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 122.02  E-value: 5.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEF-LRDPQKFQrlGGRIP-RGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGA 234
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 235 SRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAglGGGNDEREQTLNQLLVEMDGF---EANEG----IILIAATNRPDVL 307
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVggaSENDDpskmVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 519017463 308 DPALLRpgRFDRQIVV 323
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
153-323 6.44e-32

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 122.02  E-value: 6.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIV--EFLRdPQKFQRLGGRiPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFV 230
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVvwPMLR-PDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 231 GVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAglgGGNDEREQTLNQLLVEMDGF--EANEGIILIAATNRPDVLD 308
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEID 173
                        170
                 ....*....|....*
gi 519017463 309 PALLRpgRFDRQIVV 323
Cdd:cd19525  174 EAARR--RLVKRLYI 186
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
159-324 1.30e-30

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: 117.25  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 159 AGVDEAKEDLQEIVEflrdpqkfqrlgGRIPRGVLLVGPPGTGKTLLARAIAGEA---NVPFFTISGSDFVEMFVG---V 232
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 233 GASRVRDMFEQAKKNAPCIIFIDEIDAVGRhrgaglgggnDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALL 312
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|..
gi 519017463 313 RPGRFDRQIVVP 324
Cdd:cd00009  139 LYDRLDIRIVIP 150
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
157-317 1.60e-30

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: 117.53  E-value: 1.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEF-LRDPQKFQrlGGRI---PRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGV 232
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 233 GASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGlgggndEREQTL---NQLLVEMDGF--EANEGIILIAATNRPDVL 307
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLstDGNCRVIVMGATNRPQDL 152
                        170
                 ....*....|..
gi 519017463 308 DPALLR--PGRF 317
Cdd:cd19520  153 DEAILRrmPKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
178-321 3.58e-29

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 114.12  E-value: 3.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 178 PQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTI-SGSDFVEMFVGVGASRVRDMF-----EQAKKNAPC- 250
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFadaeeEQRRLGANSg 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519017463 251 --IIFIDEIDAVGRHRGAGlGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQI 321
Cdd:cd19504  104 lhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
153-372 2.28e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 110.11  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 153 VTFEDVAGVDEAKEDLQEIVEFLRdpQKFQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTIsgsDFVEMF--- 229
Cdd:CHL00195 225 EKISDIGGLDNLKDWLKKRSTSFS--KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFggi 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 230 VGVGASRVRDMFEQAKKNAPCIIFIDEID-AVGRHRGAGLGGgndereqTLNQLLVEMDGF--EANEGIILIAATNRPDV 306
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLATFITWlsEKKSPVFVVATANNIDL 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519017463 307 LDPALLRPGRFDRQIVVPNPDIVGRERILKVHVRKV-PLA-PDVDLRTVARGTPGFSGADLMNLVNEA 372
Cdd:CHL00195 373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEA 440
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
165-323 3.84e-23

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: 95.88  E-value: 3.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 165 KEDLQEiveFLRDPQKFQRLGgrIP--RGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDfvemfVGVGASRVRDMFE 242
Cdd:cd19510    2 IDDLKD---FIKNEDWYNDRG--IPyrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 243 QAKKNApcIIFIDEIDAV---GRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDR 319
Cdd:cd19510   72 TAPKQS--IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149

                 ....
gi 519017463 320 QIVV 323
Cdd:cd19510  150 KIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
189-327 3.53e-22

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: 93.21  E-value: 3.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463   189 PRGVLLVGPPGTGKTLLARAIAGEANVP---FFTISGSDFVE--------------MFVGVGASRVRDMFEQAKKNAPCI 251
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519017463   252 IFIDEIDAVGRHRGaglgggndEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPgRFDRQIVVPNPD 327
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
157-319 5.14e-22

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 93.20  E-value: 5.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIVEFLRDPQkfQRLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASR 236
Cdd:cd19507    1 DVGGLDNLKDWLKKRKAAFSKQA--SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 237 VRDMFEQAKKNAPCIIFIDEID-AVGRHRGAGLGGGNderEQTLNQLLVEMDgfEANEGIILIAATNRPDVLDPALLRPG 315
Cdd:cd19507   79 LRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTS---SRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153

                 ....
gi 519017463 316 RFDR 319
Cdd:cd19507  154 RFDE 157
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
157-323 1.49e-20

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: 88.79  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 157 DVAGVDEAKEDLQEIV--EFLRdPQKFQRLGgRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGA 234
Cdd:cd19523    1 DIAGLGALKAAIKEEVlwPLLR-PDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 235 SRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNdeREQTlnQLLVEMDGF--EANEGIILIAATNRPDVLDPALL 312
Cdd:cd19523   79 KILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLR 154
                        170
                 ....*....|.
gi 519017463 313 RpgRFDRQIVV 323
Cdd:cd19523  155 R--YFSKRLLV 163
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
183-321 2.32e-15

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 73.95  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 183 RLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFV--------------EMFVGVGASRVRDMFEQAKKNA 248
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 519017463 249 PCIIFIDEIDAVGRHRGAGLGGGNDereQTLNQLLVEM--DGFEANE--GIILIAATNRPDVLDPALLRPGRFDRQI 321
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCI 159
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
347-391 7.51e-14

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: 66.02  E-value: 7.51e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 519017463  347 DVDLRTVARGTPGFSGADLMNLVNEAALMAARRGKRIVTMVEFED 391
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK04195 PRK04195
replication factor C large subunit; Provisional
154-314 2.47e-13

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 72.65  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 154 TFEDVAGVDEAKEDLQE-IVEFLRdpqkfqrlgGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDF-----VE 227
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREwIESWLK---------GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 228 MFVGvGASRVRDMFEQAKKnapcIIFIDEIDavGRHRGAGLGGgnderEQTLNQLLVemdgfEANEGIILIAatNrpDVL 307
Cdd:PRK04195  83 RVAG-EAATSGSLFGARRK----LILLDEVD--GIHGNEDRGG-----ARAILELIK-----KAKQPIILTA--N--DPY 141

                 ....*....
gi 519017463 308 DPAL--LRP 314
Cdd:PRK04195 142 DPSLreLRN 150
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
192-392 4.26e-13

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 71.63  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPFFTISGsdfvemfVGVGASRVRDMFEQAKKNA----PCIIFIDEIdavgrHRgag 267
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI-----HR--- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 268 lgggndereqtLN---Q--LL--VEmDGFeanegIILIAAT--NrPD-VLDPALLrpgrfDR-QIVVPNP----DIVGR- 331
Cdd:COG2256  117 -----------FNkaqQdaLLphVE-DGT-----ITLIGATteN-PSfEVNSALL-----SRcRVFVLKPlseeDLEQLl 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519017463 332 ERILKVHVR-----KVPLAPDVdLRTVARgtpgFSGAD---LMNLVNEAALMAARRGKRIVTMVEFEDA 392
Cdd:COG2256  174 ERALADDERglggyKLELDDEA-LEALAR----LADGDarrALNALELAVLSAPPDGVIEITLELVEEA 237
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
190-311 4.62e-13

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: 67.17  E-value: 4.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 190 RGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGvGASRVRDMFEQAKK-NAPCIIFIDEIDAVGRHRgAGL 268
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-STE 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 519017463 269 GGGNDEReQTLNQLLVEMDgfEANEGIILIAATNRPDVLDPAL 311
Cdd:cd19512  101 KISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 140
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
192-301 2.44e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 69.34  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFvemfvgvGASRVRDMFEQAKKNA----PCIIFIDEIdavgrHRgag 267
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDEI-----HR--- 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 519017463 268 lgggndereqtLN---Q--LL--VEmDGFeanegIILIAAT 301
Cdd:PRK13342 104 -----------FNkaqQdaLLphVE-DGT-----ITLIGAT 127
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
191-317 7.97e-11

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: 60.00  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  191 GVLLVGPPGTGKTLLARAIAgEA--NVPFFTISGSDF--VEMFVG------VGASRVRDMFEQAKKNApCIIFIDEIDAV 260
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDttEEDLFGrrnidpGGASWVDGPLVRAAREG-EIAVLDEINRA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519017463  261 GRHRGAGLGGGNDEREqtlnqlLVEMDGFE----ANEGIILIAATNRPD----VLDPALLRpgRF 317
Cdd:pfam07728  79 NPDVLNSLLSLLDERR------LLLPDGGElvkaAPDGFRLIATMNPLDrglnELSPALRS--RF 135
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
10-97 4.03e-10

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: 57.23  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463   10 LWVIVFLLVVALVMLFQNPGQRvASTDITFSQLLNEVDQGRVREVTISGNEINGH------YTDNRAFATYAPNDPT--- 80
Cdd:pfam06480   3 LWLLILLVLLLLFLLFLLSSSS-STKEISYSEFLEYLEAGKVKKVVVQDDEILPTgvvegtLKDGSKFTTYFIPSLPnvd 81
                          90       100
                  ....*....|....*....|..
gi 519017463   81 -----LVQTLYKKNVAISAKPP 97
Cdd:pfam06480  82 sllekLEDALEEKGVKVSVKPP 103
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
188-317 5.71e-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: 58.93  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 188 IPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEM-FVGVGA-SRVRDMFEQakknapcIIFIDEIDAVGRHRG 265
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIAKRGG 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519017463 266 AglGGGNDEREQTLNQLLVEMDGFEAN--------EGIILIAA----TNRPDVLDPALlrPGRF 317
Cdd:cd19498  118 S--SGPDVSREGVQRDLLPIVEGSTVStkygpvktDHILFIAAgafhVAKPSDLIPEL--QGRF 177
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
156-265 6.85e-10

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: 58.72  E-value: 6.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 156 EDVAGVDEAKEdlqEIVEFLRDPQKFQRLGGRIprgVLLVGPPGTGKTLLARAIAGEANVPFFTIS-G--SDFVEM---- 228
Cdd:cd19500   10 ADHYGLEDVKE---RILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghr 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 519017463 229 --FVGVGASRVRDMFEQAKKNAPcIIFIDEIDAVGR-HRG 265
Cdd:cd19500   84 rtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGSsFRG 122
ycf2 CHL00206
Ycf2; Provisional
183-384 1.14e-09

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 61.85  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  183 RLGGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFT--------------------ISGSDFVE--------------- 227
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfliddidIDDSDDIDdsddidrdldtellt 1703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  228 --------MFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGG--------NDEREQTLNqllvemdgfea 291
Cdd:CHL00206 1704 mmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNVNESNYLSLGllvnslsrDCERCSTRN----------- 1772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  292 negIILIAATNRPDVLDPALLRPGRFDRQIVVPNPDIVGRER---ILkVHVRKVPLAPDV-DLRTVARGTPGFSGADLMN 367
Cdd:CHL00206 1773 ---ILVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKhffTL-SYTRGFHLEKKMfHTNGFGSITMGSNARDLVA 1848
                         250
                  ....*....|....*..
gi 519017463  368 LVNEAALMAARRGKRIV 384
Cdd:CHL00206 1849 LTNEALSISITQKKSII 1865
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
168-435 5.13e-09

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 58.71  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 168 LQEIVEFLRDPqkfqrLGGRIPRGVLLVGPPGTGKTLLARAI-------AGEANVPFFTI-------------------- 220
Cdd:COG1474   35 IEELASALRPA-----LRGERPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqastryrvlsrilee 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 221 --SGSDFVEmfVGVGASRVRDMFEQA--KKNAPCIIFIDEIDAVGRhrgaglgggnDEREQTLNQLLVEMDGFEANE-GI 295
Cdd:COG1474  110 lgSGEDIPS--TGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVD----------DEGDDLLYQLLRANEELEGARvGV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 296 ILIaaTNRPDV---LDPAL---LRPG--RFDR----QIVvpnpDIVgRERILKVHVRKVpLAPDVdLRTVARGTPGFSGa 363
Cdd:COG1474  178 IGI--SNDLEFlenLDPRVkssLGEEeiVFPPydadELR----DIL-EDRAELAFYDGV-LSDEV-IPLIAALAAQEHG- 247
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519017463 364 DL---MNLVNEAALMAARRGKRIVTMVEFEDAKDKIMMGAeRRTLVMTEKEKELTAYheggHAIVALNVIATDPV 435
Cdd:COG1474  248 DArkaIDLLRVAGEIAEREGSDRVTEEHVREAREKIERDR-LLEVLRGLPTHEKLVL----LAIAELLKDGEDPV 317
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
160-225 1.24e-08

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 57.67  E-value: 1.24e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519017463 160 GVDEAKEDLQEIVEFLRDpqkfQRLGGRiprGVLLVGPPGTGKTLLARAIAGE--ANVPFFTISGSDF 225
Cdd:COG1224   42 GQVEAREAAGIVVKMIKE----GKMAGK---GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
192-308 2.52e-07

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 49.81  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGeanvpffTISGSDFVEMFVGvGASRVRDMFEQAKKN-APCIIFIDEIDAVGRHRgaglgg 270
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAE-------QALLSDEPVIFIS-FLDTILEAIEDLIEEkKLDIIIIDSLSSLARAS------ 66
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 519017463 271 GNDEREQTLNQLLVEMDGFEaNEGIILIAATNRPDVLD 308
Cdd:cd01120   67 QGDRSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
160-225 3.76e-07

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: 52.70  E-value: 3.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519017463  160 GVDEAKEDLQEIVEFLRDpqkfQRLGGRiprGVLLVGPPGTGKTLLARAIAGE--ANVPFFTISGSDF 225
Cdd:pfam06068  28 GQEKAREAAGVIVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
142-321 6.88e-07

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: 52.15  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  142 KAKLLTEahGRVTFEDVAGVDEAKEDlqeiVEFLRDPQKFQRLggRIPRGV---------LLVGPPGTGKTLLARAIA-- 210
Cdd:TIGR03922 264 KAKLLAE--AEAELAEQIGLERVKRQ----VAALKSSTAMALA--RAERGLpvaqtsnhmLFAGPPGTGKTTIARVVAki 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  211 ----GEANVP-FFTISGSDFVEMFVGVGASRVRDMFEQAKKNapcIIFIDEIDA-VGRHRGAglggGNDEREQTLNQLLV 284
Cdd:TIGR03922 336 ycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTlVETGYGQ----KDPFGLEAIDTLLA 408
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 519017463  285 EMDGfeANEGIILIAATNRPDvLDPAL-----LRpGRFDRQI 321
Cdd:TIGR03922 409 RMEN--DRDRLVVIGAGYRKD-LDKFLevnegLR-SRFTRVI 446
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
192-264 1.40e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.51  E-value: 1.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPFFTISG------SDFVEMFVGVGAsrvRDmfeqakknapcIIFIDEIdavgrHR 264
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI-----HR 113
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
192-262 2.10e-06

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 50.43  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPfFTIS-----------GSDfVEMFVgvgasrVR-------DMfEQAKKNapcIIF 253
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKllqaadyDV-EKAERG---IIY 179

                 ....*....
gi 519017463 254 IDEIDAVGR 262
Cdd:COG1219  180 IDEIDKIAR 188
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
190-311 2.30e-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: 48.60  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 190 RGVLLVGPPGTGKTLLARAIAGEANVPF-FTISGSDFVEM--------FVGVGASRVRDMFEQAK-----KNAPCIIFID 255
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQeliddKDALVFVLID 132
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 519017463 256 EIDAVGRHRGAgLGGGNDERE--QTLNQLLVEMDGFEANEGIILIAATNRPDVLDPAL 311
Cdd:cd19508  133 EVESLAAARSA-SSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
192-262 4.57e-06

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 49.39  E-value: 4.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPfFTIS-----------GSDfVEMFVG---------VgasrvrdmfEQAKKNapcI 251
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENILLkllqaadydV---------EKAQRG---I 176
                         90
                 ....*....|.
gi 519017463 252 IFIDEIDAVGR 262
Cdd:PRK05342 177 VYIDEIDKIAR 187
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
187-257 5.65e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.38  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 187 RIPRGVLLVGPPGTGKT----LLARAIAGEANVPFFTI------SGSDFVEMFVGVGAS---RVRD-MF----EQAKKN- 247
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVqfhpswSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNp 298
                         90
                 ....*....|.
gi 519017463 248 -APCIIFIDEI 257
Cdd:COG1401  299 dKPYVLIIDEI 309
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
192-262 7.31e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 47.98  E-value: 7.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPfFTIS-----------GSDfVEMFVgvgasrVR-------DMfEQAKKNapcIIF 253
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VENIL------LKllqaadyDV-ERAQRG---IVY 120

                 ....*....
gi 519017463 254 IDEIDAVGR 262
Cdd:cd19497  121 IDEIDKIAR 129
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
154-264 1.51e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 45.57  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  154 TFEDVAGVDEAKEDLQEIVEFLRdpqkfQRlgGRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISG------SDFVE 227
Cdd:pfam05496   5 TLDEYIGQEKVKENLKIFIEAAK-----QR--GEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGpaierpGDLAA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 519017463  228 MFVGVGAsrvRDmfeqakknapcIIFIDEIdavgrHR 264
Cdd:pfam05496  78 ILTNLEP---GD-----------VLFIDEI-----HR 95
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
192-258 1.64e-05

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: 45.65  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  192 VLLVGPPGTGKTLLARAIAGEANV---PFFTISGSDFVE-----MFVG-----VGASRVRDMFEQAKKNAPCIIFIDEID 258
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
168-259 3.18e-05

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 46.12  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 168 LQEIVEFLRDpqkfQRLGGRIPRGVLLVGPPGTGKTLLARAIAGE---------------ANVPFFTISGSDFVEMFVGV 232
Cdd:COG0470    1 QEEAWEQLLA----AAESGRLPHALLLHGPPGIGKTTLALALARDllcenpeggkacgqcHSRLMAAGNHPDLLELNPEE 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 519017463 233 -----GASRVRDMFEQAKKNAPC----IIFIDEIDA 259
Cdd:COG0470   77 ksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADA 112
44 PHA02544
clamp loader, small subunit; Provisional
186-261 4.05e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 46.14  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 186 GRIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISGS----DFVEMFVGVGASRVrDMFEQAKknapcIIFIDEIDAVG 261
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-SLTGGGK-----VIIIDEFDRLG 113
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
188-323 5.00e-05

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 43.77  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 188 IPRG--VLLVGPPGTGKTLLARAIAGEANVP--FFTISGSDFVEMFVGVGASRVRDMFE----QAKK--------NAPCI 251
Cdd:cd00267   22 LKAGeiVALVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIGYVPQlsggQRQRvalarallLNPDL 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519017463 252 IFIDEI----DAVGRHRgaglgggndereqtLNQLLVEMdgfeANEGIILIAATNRPDVLDPAllrpgrFDRQIVV 323
Cdd:cd00267  102 LLLDEPtsglDPASRER--------------LLELLREL----AEEGRTVIIVTHDPELAELA------ADRVIVL 153
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
155-258 5.43e-05

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: 44.09  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 155 FEDVAGVDEAKEDLQEIVEF----LRDPQKfqrlggriPRGVLL-VGPPGTGKTLLARAIA-----GEANvpFFTISGSD 224
Cdd:cd19499   10 HERVVGQDEAVKAVSDAIRRaragLSDPNR--------PIGSFLfLGPTGVGKTELAKALAellfgDEDN--LIRIDMSE 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 519017463 225 FVEMFVG----------VGASRVRDMFEQAKKNAPCIIFIDEID 258
Cdd:cd19499   80 YMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
154-262 6.30e-05

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: 45.37  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  154 TFEDVAGVDEAKEDLQEIVEFLRDPQKfqrlggrIPRGVLLVGPPGTGKTLLARAIAGEANVPFFTISG------SDFVE 227
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQE-------ALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAA 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 519017463  228 MFVGVGAsrvRDmfeqakknapcIIFIDEIDAVGR 262
Cdd:TIGR00635  75 ILTNLEE---GD-----------VLFIDEIHRLSP 95
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
154-210 7.61e-05

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 45.18  E-value: 7.61e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519017463 154 TFEDVAGVDEAKEDLQEIVEflrdpqkfqrlGGRIPRGVLLVGPPGTGKTLLARAIA 210
Cdd:COG2812    8 TFDDVVGQEHVVRTLKNALA-----------SGRLAHAYLFTGPRGVGKTTLARILA 53
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
143-246 8.06e-05

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 45.37  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 143 AKLLTEAHGRVTFEDVAGVDEAKEDLQEIVEflrdpqkfqrlGGRIPRgVLLVGPPGTGKTLLARAIAGEAnvpFFTISG 222
Cdd:PRK12402   2 APLWTEKYRPALLEDILGQDEVVERLSRAVD-----------SPNLPH-LLVQGPPGSGKTAAVRALAREL---YGDPWE 66
                         90       100
                 ....*....|....*....|....
gi 519017463 223 SDFVEMfvgvgasRVRDMFEQAKK 246
Cdd:PRK12402  67 NNFTEF-------NVADFFDQGKK 83
rfc PRK00440
replication factor C small subunit; Reviewed
154-259 9.01e-05

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 44.86  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 154 TFEDVAGVDEAKEDLQEIVEflrdpqkfqrlGGRIPRgVLLVGPPGTGKTLLARAIAGEanvpfftISGSDFVEMFVGVG 233
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTTAALALARE-------LYGEDWRENFLELN 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 519017463 234 AS--R----VRDMFEQAKKNAPC------IIFIDEIDA 259
Cdd:PRK00440  76 ASdeRgidvIRNKIKEFARTAPVggapfkIIFLDEADN 113
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
192-220 1.39e-04

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 44.39  E-value: 1.39e-04
                         10        20
                 ....*....|....*....|....*....
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPFFTI 220
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
AAA_22 pfam13401
AAA domain;
192-307 1.57e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  192 VLLVGPPGTGKTLLARAIA---GEANVPFFTI------SGSDFVEMFV---------GVGASRVRDMFEQA--KKNAPCI 251
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 519017463  252 IFIDEIDAVgrhrgaglgggndeREQTLNQLLVEMDGFEANEGIILIAATNRPDVL 307
Cdd:pfam13401  88 LIIDEAQHL--------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
169-313 2.09e-04

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 44.41  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 169 QEIVEFLRDPQKFQRLGGRIPRgVLLVGPPGTGKTLLARAIA---------GEANVPFF----TISGS----DFVEMFVG 231
Cdd:COG5635  161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrDLAEEasleDLLAEALE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 232 VGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHrgaglgggnDEREQTLNQLLVEMDGFEANEGIIliaaTNRPDVLDPAL 311
Cdd:COG5635  240 KRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII----TSRPEGYDSSE 306

                 ..
gi 519017463 312 LR 313
Cdd:COG5635  307 LE 308
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
190-257 2.27e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 43.23  E-value: 2.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519017463 190 RGVLLVGPPGTGKTLLARAIAGEA-----NVPFFTIsgSDFV-EMFVGVGASRVRDMFEQAKKnAPCIIfIDEI 257
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLVnELKEARADGRLERLLKRLAK-VDLLI-LDEL 169
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
192-222 2.99e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 43.53  E-value: 2.99e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEANVPFFTISG 222
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
184-213 4.04e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 42.21  E-value: 4.04e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 519017463 184 LGGRIPRG--VLLVGPPGTGKTLLARAIAGEA 213
Cdd:COG0467   13 LGGGLPRGssTLLSGPPGTGKTTLALQFLAEG 44
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
166-211 4.54e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.11  E-value: 4.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519017463 166 EDLQEIVEFLRDPQKFQRLGGRIP-------------RG-----------------VLLVGPPGTGKTLLARAIAG 211
Cdd:COG0606  158 SSLLEVVAFLRGEQPLPPAEPDAPpaeppyepdladvKGqeqakraleiaaagghnLLMIGPPGSGKTMLARRLPG 233
PRK13341 PRK13341
AAA family ATPase;
193-264 1.00e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 42.35  E-value: 1.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 519017463 193 LLVGPPGTGKTLLARAIAGEANVPFFTISGsdfvemfVGVGASRVRDMFEQAKK-----NAPCIIFIDEIdavgrHR 264
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDEV-----HR 120
Sigma54_activat pfam00158
Sigma-54 interaction domain;
192-257 1.47e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.69  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463  192 VLLVGPPGTGKTLLARAI---AGEANVPFFTISGSDFV------EMFvGV------GASRVRD-MFEQAKKNapcIIFID 255
Cdd:pfam00158  25 VLITGESGTGKELFARAIhqlSPRADGPFVAVNCAAIPeellesELF-GHekgaftGADSDRKgLFELADGG---TLFLD 100

                  ..
gi 519017463  256 EI 257
Cdd:pfam00158 101 EI 102
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
187-211 2.03e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 41.33  E-value: 2.03e-03
                         10        20
                 ....*....|....*....|....*..
gi 519017463 187 RIPRG--VLLVGPPGTGKTLLARAIAG 211
Cdd:COG4178  385 SLKPGerLLITGPSGSGKSTLLRAIAG 411
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
192-266 2.59e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 39.61  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKT-LLARAIAG---------EANV-PFFTISGSDFVEMFVGV-GASRVRDMFEQA-KKNAPCIIFIdeID 258
Cdd:cd04105    3 VLLLGPSDSGKTaLFTKLTTGkvrstvtsiEPNVaSFYSNSSKGKKLTLVDVpGHEKLRDKLLEYlKASLKAIVFV--VD 80

                 ....*...
gi 519017463 259 AVGRHRGA 266
Cdd:cd04105   81 SATFQKNI 88
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
184-220 2.78e-03

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 39.55  E-value: 2.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 519017463 184 LGGRIPRG--VLLVGPPGTGKTL-----LARAIAGEANVPFFTI 220
Cdd:cd01124   12 LGGGIPKGsvTLLTGGPGTGKTLfglqfLYAGAKNGEPGLFFTF 55
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
192-211 3.11e-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: 39.44  E-value: 3.11e-03
                          10        20
                  ....*....|....*....|
gi 519017463  192 VLLVGPPGTGKTLLARAIAG 211
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
193-265 4.25e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 40.39  E-value: 4.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 193 LLVGPPGTGKTLLARAIAgEAnvpfftiSGSDFVEMFVGvGasrVRDMFE---------------------QAKKNAPCI 251
Cdd:COG0466  356 CLVGPPGVGKTSLGKSIA-RA-------LGRKFVRISLG-G---VRDEAEirghrrtyigampgriiqglkKAGTKNPVF 423
                         90
                 ....*....|....*
gi 519017463 252 IfIDEIDAVGR-HRG 265
Cdd:COG0466  424 L-LDEIDKMGSdFRG 437
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
187-211 4.88e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 38.29  E-value: 4.88e-03
                         10        20
                 ....*....|....*....|....*..
gi 519017463 187 RIPRG--VLLVGPPGTGKTLLARAIAG 211
Cdd:cd03223   23 EIKPGdrLLITGPSGTGKSSLFRALAG 49
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
192-383 6.08e-03

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.02  E-value: 6.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEA-----NVPFFTISGSDFVEMFvgVGASRVRDMFEQAKKNAPC-IIFIDEIdavgrHRG 265
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEAlennpGARVVYLTAEEFTNDF--INAIRNNTIEEFKEKYRSVdVLLIDDI-----QFL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519017463 266 AGlgggnDEREQ-----TLNQLLvemdgfeANEGIILIAATNRP---DVLDPALLRpgRFDRQIVVP--NPDIVGRERIL 335
Cdd:COG0593  110 AG-----KEATQeeffhTFNALR-------EAGKQIVLTSDRPPkelPGLEERLRS--RLEWGLVVDiqPPDLETRIAIL 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 519017463 336 --KVHVRKVPLAPDVdLRTVARGTPGfSGADLMNLVNEAALMAARRGKRI 383
Cdd:COG0593  176 rkKAADRGLELPDEV-LEYLARRIER-NVRELEGALNRLDAYALLTGRPI 223
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
192-227 8.08e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.22  E-value: 8.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 519017463 192 VLLVGPPGTGKTLLARAIAGEA-----NVPFFTIsgSDFVE 227
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
 
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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