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Conserved domains on  [gi|1624728525|ref|XP_028869807|]
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26S proteasome regulatory subunit 4 -like protein B [Babesia sp. Xinjiang]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 315-753 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 861.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 315 MGNTQGDLNqNQENKNGNNDGTPREKPPPPVFGKNKKKQQRNFAPIRIPTVTPSTKCRLRLLKLERIKDYLLLEEEYVAN 394
Cdd:PTZ00361    1 MGNAQGQGN-NQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 395 KIRLNPTKNKNQDDLVRLEDLRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVNILSFVDKTLLEPGCSVLLHNKTNSVVG 474
Cdd:PTZ00361   80 QEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 475 ILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVAN 554
Cdd:PTZ00361  160 ILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVAN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 555 ETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDP 634
Cdd:PTZ00361  240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 635 QADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTE 714
Cdd:PTZ00361  320 RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTE 399

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1624728525 715 AGLLALRERRMQITQADLRKAREKALQLKKGNIPESLYC 753
Cdd:PTZ00361  400 AGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
UBCc_UEV super family cl49610
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 247-307 2.28e-13

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin, and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways.


The actual alignment was detected with superfamily member cd23794:

Pssm-ID: 483950  Cd Length: 138  Bit Score: 67.59  E-value: 2.28e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624728525 247 ELSCLDLPDNVELRPFDLNDLSRLELTVRAPEGIWRDIPVRFECVIPEGYPHERLRVRCLS 307
Cdd:cd23794     9 DLEELDLPGQCKVEFPDPNDLLKFEVTITPDEGYYKGGTFVFEIDIPDNYPFEPPKVKCLT 69
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 315-753 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 861.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 315 MGNTQGDLNqNQENKNGNNDGTPREKPPPPVFGKNKKKQQRNFAPIRIPTVTPSTKCRLRLLKLERIKDYLLLEEEYVAN 394
Cdd:PTZ00361    1 MGNAQGQGN-NQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 395 KIRLNPTKNKNQDDLVRLEDLRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVNILSFVDKTLLEPGCSVLLHNKTNSVVG 474
Cdd:PTZ00361   80 QEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 475 ILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVAN 554
Cdd:PTZ00361  160 ILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVAN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 555 ETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDP 634
Cdd:PTZ00361  240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 635 QADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTE 714
Cdd:PTZ00361  320 RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTE 399

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1624728525 715 AGLLALRERRMQITQADLRKAREKALQLKKGNIPESLYC 753
Cdd:PTZ00361  400 AGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 369-740 3.59e-154

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: 452.72  E-value: 3.59e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 369 TKCRLRLLKLEriKDYLLLEEEyvanKIRLNPTKNKNQDDLVRLedlRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVNI 448
Cdd:TIGR01242   2 SELDVRIRKLE--DEKRSLEKE----KIRLERELERLRSEIERL---RSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 449 LSFVDKTLLEPGCSVLLHNKTNSVVGILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVG 528
Cdd:TIGR01242  73 SAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 529 IRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRY 608
Cdd:TIGR01242 153 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 609 DATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMA 688
Cdd:TIGR01242 233 DSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLA 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1624728525 689 QDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKAREKAL 740
Cdd:TIGR01242 313 EDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 487-738 9.78e-130

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 388.21  E-value: 9.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 487 MKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGS 566
Cdd:COG1222    67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 567 ELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGekEIQRTMLELLNQLDGFDPQADVKVIMATNR 646
Cdd:COG1222   147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 647 IESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQ 726
Cdd:COG1222   225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                         250
                  ....*....|..
gi 1624728525 727 ITQADLRKAREK 738
Cdd:COG1222   305 VTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 496-665 8.89e-112

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: 335.85  E-value: 8.89e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 496 SYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                         170
                  ....*....|
gi 1624728525 656 RPGRIDRKIQ 665
Cdd:cd19502   161 RPGRFDRKIE 170
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 535-667 1.43e-50

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: 172.78  E-value: 1.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYdatSGG 614
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1624728525 615 EKEIQRTMLELLNQLDGF-DPQADVKVIMATNRIESLDPALIrpGRIDRKIQLP 667
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 531-670 1.15e-19

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: 86.27  E-value: 1.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525  531 PPKGVILYGPPGTGKTLLAKAVANE---TCATFLRVVGSEL--------------IQKYLGEGPKLVREMFRVAEENAPS 593
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525  594 IIFIDEIDAIGTKRYdatsggekEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPgRIDRKIQLPNPD 670
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 247-307 2.28e-13

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, E2 M and related proteins; The E2F/E2M subfamily includes mammalian ubiquitin-conjugating enzymes E2 F (UBE2F/NCE2, EC 2.3.2.32) and E2 M (UBE2M/UBC12, EC 2.3.2.34), yeast NEDD8-conjugating enzyme UBC12 (EC 2.3.2.24), plant RUB1-conjugating enzyme 1-2 (RCE1/UBC12 and RCE2/UBC12L, EC 2.3.2.-), and similar proteins. UBE2F (also called EDD8-conjugating enzyme UBE2F, NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, or RING-type E3 NEDD8 transferase UBE2F) and UBE2M (also called NEDD8-conjugating enzyme UBC12, or NEDD8 carrier protein) accept the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. The RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. UBE2M is involved in cell proliferation. Saccharomyces cerevisiae UBC12 and Arabidopsis thaliana RCE1/RCE2 accept the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and the ECR1-AXR1 E1 complex, respectively.


Pssm-ID: 467414  Cd Length: 138  Bit Score: 67.59  E-value: 2.28e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624728525 247 ELSCLDLPDNVELRPFDLNDLSRLELTVRAPEGIWRDIPVRFECVIPEGYPHERLRVRCLS 307
Cdd:cd23794     9 DLEELDLPGQCKVEFPDPNDLLKFEVTITPDEGYYKGGTFVFEIDIPDNYPFEPPKVKCLT 69
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 535-612 8.67e-04

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: 41.69  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETC-----ATFLRVvgSELIQKYL---GEGpKLVREMFRVAeenAPSIIFIDEI-----D 601
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAACrqgyrVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDELgylpfS 166

                          90
                  ....*....|....*....
gi 1624728525 602 AIGT--------KRYDATS 612
Cdd:NF038214  167 REGAnllfeliaDRYERGS 185
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 315-753 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 861.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 315 MGNTQGDLNqNQENKNGNNDGTPREKPPPPVFGKNKKKQQRNFAPIRIPTVTPSTKCRLRLLKLERIKDYLLLEEEYVAN 394
Cdd:PTZ00361    1 MGNAQGQGN-NQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 395 KIRLNPTKNKNQDDLVRLEDLRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVNILSFVDKTLLEPGCSVLLHNKTNSVVG 474
Cdd:PTZ00361   80 QEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 475 ILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVAN 554
Cdd:PTZ00361  160 ILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVAN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 555 ETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDP 634
Cdd:PTZ00361  240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 635 QADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTE 714
Cdd:PTZ00361  320 RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTE 399

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1624728525 715 AGLLALRERRMQITQADLRKAREKALQLKKGNIPESLYC 753
Cdd:PTZ00361  400 AGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 377-750 1.39e-174

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 505.52  E-value: 1.39e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 377 KLERIKDYLLLEEEYV----ANKIRLNPTKNKNQDDLVRL----EDLRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVNI 448
Cdd:PRK03992    2 RLEALEERNSELEEQIrqleLKLRDLEAENEKLERELERLkselEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 449 LSFVDKTLLEPGCSVLLHNKTNSVVGILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVG 528
Cdd:PRK03992   82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 529 IRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRY 608
Cdd:PRK03992  162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 609 DATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMA 688
Cdd:PRK03992  242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624728525 689 QDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKAREKALQLKKGNIPES 750
Cdd:PRK03992  322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSMEE 383
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 373-735 1.14e-157

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 462.70  E-value: 1.14e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 373 LRLLKLERIKDYLLLEEEYVAnkirlnpTKNKN-QDDLVR----LEDLRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVN 447
Cdd:PTZ00454   22 EKLKELEKELEFLDIQEEYIK-------EEQKNlKRELIRakeeVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 448 ILSFVDKTLLEPGCSVLLHNKTNSVVGILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEV 527
Cdd:PTZ00454   95 ILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 528 GIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKR 607
Cdd:PTZ00454  175 GIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKR 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 608 YDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTM 687
Cdd:PTZ00454  255 FDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNL 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1624728525 688 AQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKA 735
Cdd:PTZ00454  335 SEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKG 382
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 369-740 3.59e-154

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: 452.72  E-value: 3.59e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 369 TKCRLRLLKLEriKDYLLLEEEyvanKIRLNPTKNKNQDDLVRLedlRGSPMSVGTMEEMIDDNHAIVTSSMGPEYYVNI 448
Cdd:TIGR01242   2 SELDVRIRKLE--DEKRSLEKE----KIRLERELERLRSEIERL---RSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 449 LSFVDKTLLEPGCSVLLHNKTNSVVGILLDDVDPLVSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVG 528
Cdd:TIGR01242  73 SAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 529 IRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRY 608
Cdd:TIGR01242 153 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 609 DATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMA 688
Cdd:TIGR01242 233 DSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLA 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1624728525 689 QDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKAREKAL 740
Cdd:TIGR01242 313 EDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 487-738 9.78e-130

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 388.21  E-value: 9.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 487 MKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGS 566
Cdd:COG1222    67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 567 ELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGekEIQRTMLELLNQLDGFDPQADVKVIMATNR 646
Cdd:COG1222   147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 647 IESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQ 726
Cdd:COG1222   225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                         250
                  ....*....|..
gi 1624728525 727 ITQADLRKAREK 738
Cdd:COG1222   305 VTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 496-665 8.89e-112

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: 335.85  E-value: 8.89e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 496 SYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                         170
                  ....*....|
gi 1624728525 656 RPGRIDRKIQ 665
Cdd:cd19502   161 RPGRFDRKIE 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 477-751 2.60e-81

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: 274.86  E-value: 2.60e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 477 LDDVDPlvSLMK---VErAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVA 553
Cdd:TIGR01243 432 LKMVEP--SAIRevlVE-VPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVA 508

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 554 NETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGFD 633
Cdd:TIGR01243 509 TESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQ 586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 634 PQADVKVIMATNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICT 713
Cdd:TIGR01243 587 ELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCR 666

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1624728525 714 EAGLLALRERRMQITQADLRKARE---KALQLKKGNIPESL 751
Cdd:TIGR01243 667 EAAMAALRESIGSPAKEKLEVGEEeflKDLKVEMRHFLEAL 707
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 496-740 9.89e-81

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: 266.46  E-value: 9.89e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 496 SYSDIGGLEEQIQEIKEAVELpLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:TIGR01241  53 TFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:TIGR01241 132 GASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 656 RPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKA 735
Cdd:TIGR01241 212 RPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEA 291


                  ....*
gi 1624728525 736 REKAL 740
Cdd:TIGR01241 292 IDRVI 296
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 474-738 3.80e-80

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: 261.77  E-value: 3.80e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 474 GILLDDVDPLVSLMKVERAPLesYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVA 553
Cdd:COG0464   135 LVTYEDIGGLEEELLELREAI--LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALA 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 554 NETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRydaTSGGEKEIQRTMLELLNQLDGFd 633
Cdd:COG0464   213 GELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL- 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 634 pQADVKVIMATNRIESLDPALIRpgRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICT 713
Cdd:COG0464   289 -RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVR 365

                         250       260
                  ....*....|....*....|....*
gi 1624728525 714 EAGLLALRERRMQITQADLRKAREK 738
Cdd:COG0464   366 RAALQALRLGREPVTTEDLLEALER 390
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 484-721 1.08e-76

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: 262.15  E-value: 1.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 484 VSLMKVERAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRV 563
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 564 VGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATsgGEKEiQRTMLELLNQLDGFDPQADVKVIMA 643
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624728525 644 TNRIESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALR 721
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
498-738 2.44e-75

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 254.58  E-value: 2.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 498 SDIGGLEEQIQEIKEAVELpLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGP 577
Cdd:COG0465   142 DDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 578 KLVREMFRVAEENAPSIIFIDEIDAIGTKRyDATSGG---EKEiqRTmlelLNQL----DGFDPQADVKVIMATNRIESL 650
Cdd:COG0465   221 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQR-GAGLGGghdERE--QT----LNQLlvemDGFEGNEGVIVIAATNRPDVL 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 651 DPALIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEE-------FvntkddlSGADIKAICTEAGLLALRER 723
Cdd:COG0465   294 DPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEViarrtpgF-------SGADLANLVNEAALLAARRN 366

                         250
                  ....*....|....*
gi 1624728525 724 RMQITQADLRKAREK 738
Cdd:COG0465   367 KKAVTMEDFEEAIDR 381
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 499-666 1.02e-68

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: 222.94  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPK 578
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 579 LVREMFRVAEENAPSIIFIDEIDAIGTKRydATSGGEKEiQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPG 658
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKR--EEDQREVE-RRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                  ....*...
gi 1624728525 659 RIDRKIQL 666
Cdd:cd19503   158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 496-665 1.72e-67

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: 220.18  E-value: 1.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 496 SYSDIGGLEEQIQEIKEAVELpLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                         170
                  ....*....|
gi 1624728525 656 RPGRIDRKIQ 665
Cdd:cd19501   161 RPGRFDRQVY 170
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 499-667 2.47e-66

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: 216.92  E-value: 2.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPK 578
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 579 LVREMFRVAEENAPSIIFIDEIDAIGTKRYDATsgGEKEiQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPG 658
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                  ....*....
gi 1624728525 659 RIDRKIQLP 667
Cdd:cd19519   158 RFDREIDIG 166
ftsH CHL00176
cell division protein; Validated
 496-738 2.45e-64

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 226.08  E-value: 2.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 496 SYSDIGGLEEQIQEIKEAVELpLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:CHL00176  181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:CHL00176  260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 656 RPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKA 735
Cdd:CHL00176  340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419


                  ...
gi 1624728525 736 REK 738
Cdd:CHL00176  420 IDR 422
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 424-731 3.53e-64

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 222.66  E-value: 3.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 424 TMEEMIDDNHAIVTSSMGPEYYVNILSFVDKTLLEPGCSVLLHNKTN-SVVGILLDDVDPLVslmkVERAPLESYSDIGG 502
Cdd:TIGR03689 111 TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGyAFEAIPRTEVEDLV----LEEVPDVTYADIGG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 503 LEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCAT----------FLRVVGSELIQKY 572
Cdd:TIGR03689 187 LGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARigaegggksyFLNIKGPELLNKY 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 573 LGEGPKLVREMF----RVAEENAPSIIFIDEIDAIGTKRydaTSGGEKEIQRTML-ELLNQLDGFDPQADVKVIMATNRI 647
Cdd:TIGR03689 267 VGETERQIRLIFqrarEKASEGRPVIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNRE 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 648 ESLDPALIRPGRIDRKIQLPNPDTKTKRKIFEIHtskmtMAQDVDLEEFVNTKDDLSGADIKAICTEA--GLLALRERR- 724
Cdd:TIGR03689 344 DMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPEDLAAHDGDREATAAALIQRVvdALYARSEANr 418


                  ....*...
gi 1624728525 725 -MQITQAD 731
Cdd:TIGR03689 419 yVEVTYAN 426
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 508-664 1.32e-61

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 203.67  E-value: 1.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 508 QEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVA 587
Cdd:cd19511     3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525 588 EENAPSIIFIDEIDAIGTKRYDATSGGEKEiqRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKI 664
Cdd:cd19511    83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 508-666 6.86e-61

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: 201.96  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 508 QEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVA 587
Cdd:cd19529     3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624728525 588 EENAPSIIFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKIQL 666
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRR--GTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
496-740 2.30e-58

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 209.89  E-value: 2.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 496 SYSDIGGLEEQIQEIKEAVELpLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:PRK10733  150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 656 RPGRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKA 735
Cdd:PRK10733  309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388


                  ....*
gi 1624728525 736 REKAL 740
Cdd:PRK10733  389 KDKIM 393
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 506-664 7.71e-58

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: 193.65  E-value: 7.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 506 QIQEIKEAVELPLTHPELyEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFR 585
Cdd:cd19481     1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624728525 586 VAEENAPSIIFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKI 664
Cdd:cd19481    80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 535-667 1.43e-50

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: 172.78  E-value: 1.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYdatSGG 614
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1624728525 615 EKEIQRTMLELLNQLDGF-DPQADVKVIMATNRIESLDPALIrpGRIDRKIQLP 667
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 508-664 2.20e-49

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: 170.77  E-value: 2.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 508 QEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVA 587
Cdd:cd19528     3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525 588 EENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKI 664
Cdd:cd19528    83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
498-749 1.38e-48

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 171.61  E-value: 1.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 498 SDIGGLEEQIQEIKEAVElPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGP 577
Cdd:COG1223     2 DDVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 578 KLVREMFRVAEEnAPSIIFIDEIDAIGTKRYDATSGGekEIQRTMLELLNQLDGFDpqADVKVIMATNRIESLDPALIRp 657
Cdd:COG1223    81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 658 gRIDRKIQLPNPDTKTKRKIFEIHTSKMTMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRKARE 737
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                         250
                  ....*....|..
gi 1624728525 738 KALQLKKGNIPE 749
Cdd:COG1223   234 QRKERKKEPKKE 245
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 500-664 2.46e-48

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: 167.91  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 500 IGGLEEQIQEIKEAVELPLTHPELYEevGIR-PPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPK 578
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP--GLRgPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 579 LVREMFRVAEENAPSIIFIDEIDAIGTKRydatSGGEKEIQRTM-LELLNQLDGF--DPQADVKVIMATNRIESLDPALI 655
Cdd:cd19509    79 IVRALFALARELQPSIIFIDEIDSLLSER----GSGEHEASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFL 154


                  ....*....
gi 1624728525 656 RpgRIDRKI 664
Cdd:cd19509   155 R--RFEKRI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 499-666 5.57e-47

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: 164.50  E-value: 5.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPK 578
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 579 LVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKeiqRTMLELLNQLDGF----DPQADVKVIMATNRIESLDPAL 654
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157

                         170
                  ....*....|..
gi 1624728525 655 IRPGRIDRKIQL 666
Cdd:cd19518   158 RRAGRFDREICL 169
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 499-663 6.39e-45

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: 158.83  E-value: 6.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANEtCAT-------FLRvVGSELIQK 571
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAE-CSKggqkvsfFMR-KGADCLSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 572 YLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELlnqLDGFDPQADVKVIMATNRIESLD 651
Cdd:cd19517    79 WVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALD 155

                         170
                  ....*....|..
gi 1624728525 652 PALIRPGRIDRK 663
Cdd:cd19517   156 PALRRPGRFDRE 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 503-662 2.27e-44

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 156.88  E-value: 2.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 503 LEEQIQEIKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVRE 582
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 583 MFRVAEENAPSIIFIDEIDAIGTKRYDATSGGekeIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDR 662
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 499-656 2.00e-43

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: 154.50  E-value: 2.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEEVGI-RPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGP 577
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 578 KLVREMFRVAEENAPSIIFIDEIDAIGTKRydatSGGEKEIQRTM-LELLNQLDGF--DPQADVKVIMATNRIESLDPAL 654
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAI 156


                  ..
gi 1624728525 655 IR 656
Cdd:cd19520   157 LR 158
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 509-666 1.24e-41

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 149.20  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 509 EIKEAVELPLTHPELYEEvGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAE 588
Cdd:cd19527     4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 589 ENAPSIIFIDEIDAIGTKR-YDATSGGekEIQRTMLELLNQLDGF-DPQADVKVIMATNRIESLDPALIRPGRIDRKIQL 666
Cdd:cd19527    83 DAKPCVIFFDELDSLAPSRgNSGDSGG--VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 499-664 1.57e-40

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: 146.28  E-value: 1.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEevGIRPP-KGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGP 577
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 578 KLVREMFRVAEENAPSIIFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGF-------DPQADVKVIMATNRIESL 650
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156

                         170
                  ....*....|....
gi 1624728525 651 DPALIRpgRIDRKI 664
Cdd:cd19522   157 DEALRR--RLEKRI 168
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 493-664 2.29e-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: 146.16  E-value: 2.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 493 PLESYSDIGGLEEQIQEIKEAVELPLTHPELYeeVGIRPP-KGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQK 571
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF--TGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 572 YLGEGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRtmlELLNQLDGFDPQAD-VKVIMATNRIESL 650
Cdd:cd19521    80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVGNDSQgVLVLGATNIPWQL 156

                         170
                  ....*....|....
gi 1624728525 651 DPALIRpgRIDRKI 664
Cdd:cd19521   157 DSAIRR--RFEKRI 168
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 510-664 1.52e-39

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: 143.34  E-value: 1.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 510 IKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPKLVREMFRVAEE 589
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624728525 590 NAPSIIFIDEIDAIGTKRYDATSGgekEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKI 664
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 499-656 5.11e-39

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: 141.91  E-value: 5.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYeeVGIR-PPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGP 577
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 578 KLVREMFRVAEENAPSIIFIDEIDAIGTKRydatSGGEKEIQRTM-LELLNQLDGFDPQAD--VKVIMATNRIESLDPAL 654
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSER----SEGEHEASRRLkTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAV 154


                  ..
gi 1624728525 655 IR 656
Cdd:cd19524   155 LR 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 497-656 1.93e-38

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: 141.28  E-value: 1.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 497 YSDIGGLEEQIQEIKEAVELPLTHPELYeeVGIR-PPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:cd19525    21 WADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDatsgGEKEIQRTM-LELLNQLDGFD--PQADVKVIMATNRIESLDP 652
Cdd:cd19525    99 GEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE----GEHESSRRIkTEFLVQLDGATtsSEDRILVVGATNRPQEIDE 174


                  ....
gi 1624728525 653 ALIR 656
Cdd:cd19525   175 AARR 178
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 499-656 8.42e-30

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: 115.75  E-value: 8.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLEEQIQEIKEAVELPLTHPELYEEVgIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEGPK 578
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 579 LVREMFRVAEENAPSIIFIDEIDAIGTKRYDatsgGEKEIQRTMLELLNQLDGF--DPQADVKVIMATNRIESLDPALIR 656
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 500-666 7.01e-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: 113.74  E-value: 7.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 500 IGGLEEQIQEI-KEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVV-GSELIQKYLGEGP 577
Cdd:cd19504     2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 578 KLVREMFRVAEENAPS--------IIFIDEIDAIGTKRydATSGGEKEIQRTML-ELLNQLDGFDPQADVKVIMATNRIE 648
Cdd:cd19504    82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTNRKD 159

                         170
                  ....*....|....*...
gi 1624728525 649 SLDPALIRPGRIDRKIQL 666
Cdd:cd19504   160 LIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 501-667 3.27e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 110.70  E-value: 3.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 501 GGLEEQIQEIKEAVELPlthpelyeevgirPPKGVILYGPPGTGKTLLAKAVANETC---ATFLRVVGSELIQKYLGE-- 575
Cdd:cd00009     1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELFrpgAPFLYLNASDLLEGLVVAel 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 -GPKLVREMFRVAEENAPSIIFIDEIDAIGtkrydatsggeKEIQRTMLELLNQL-DGFDPQADVKVIMATNRIESLDPA 653
Cdd:cd00009    68 fGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                         170
                  ....*....|....
gi 1624728525 654 LIRPGRIDRKIQLP 667
Cdd:cd00009   137 RALYDRLDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
 495-747 1.59e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 110.88  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 495 ESYSDIGGLEEQIQEIKEAVElplTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLG 574
Cdd:CHL00195  225 EKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVG 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 575 EGPKLVREMFRVAEENAPSIIFIDEIDAIGTKRYDAT-SGGEKEIQRTMLELLNQldgfdPQADVKVIMATNRIESLDPA 653
Cdd:CHL00195  302 ESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLPLE 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 654 LIRPGRIDRKIQLPNPDTKTKRKIFEIHTSKM--TMAQDVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRmQITQAD 731
Cdd:CHL00195  377 ILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR-EFTTDD 455

                         250
                  ....*....|....*....
gi 1624728525 732 LRKAREKAL---QLKKGNI 747
Cdd:CHL00195  456 ILLALKQFIplaQTEKEQI 474
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 499-662 1.34e-24

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: 100.52  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 499 DIGGLE---EQIQEIKEAVELPlthpelYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGE 575
Cdd:cd19507     1 DVGGLDnlkDWLKKRKAAFSKQ------ASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 576 GPKLVREMFRVAEENAPSIIFIDEID-AIGTKRYDATSGGEKEIQRTMLELLNQldgfdPQADVKVIMATNRIESLDPAL 654
Cdd:cd19507    75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPEL 149


                  ....*...
gi 1624728525 655 IRPGRIDR 662
Cdd:cd19507   150 LRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 510-664 1.70e-22

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: 94.34  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 510 IKEAVELPLTHPELYEEVGIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVvgsELIQKYLGEgpKLVREMFRVAEE 589
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDL---NLSEVVLTD--DRLNHLLNTAPK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 590 NapSIIFIDEID-AIGTKRYDAT----SGGEKEIqrTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPGRIDRKI 664
Cdd:cd19510    76 Q--SIILLEDIDaAFESREHNKKnpsaYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 531-670 1.15e-19

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: 86.27  E-value: 1.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525  531 PPKGVILYGPPGTGKTLLAKAVANE---TCATFLRVVGSEL--------------IQKYLGEGPKLVREMFRVAEENAPS 593
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525  594 IIFIDEIDAIGTKRYdatsggekEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALIRPgRIDRKIQLPNPD 670
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 247-307 2.28e-13

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, E2 M and related proteins; The E2F/E2M subfamily includes mammalian ubiquitin-conjugating enzymes E2 F (UBE2F/NCE2, EC 2.3.2.32) and E2 M (UBE2M/UBC12, EC 2.3.2.34), yeast NEDD8-conjugating enzyme UBC12 (EC 2.3.2.24), plant RUB1-conjugating enzyme 1-2 (RCE1/UBC12 and RCE2/UBC12L, EC 2.3.2.-), and similar proteins. UBE2F (also called EDD8-conjugating enzyme UBE2F, NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, or RING-type E3 NEDD8 transferase UBE2F) and UBE2M (also called NEDD8-conjugating enzyme UBC12, or NEDD8 carrier protein) accept the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. The RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. UBE2M is involved in cell proliferation. Saccharomyces cerevisiae UBC12 and Arabidopsis thaliana RCE1/RCE2 accept the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and the ECR1-AXR1 E1 complex, respectively.


Pssm-ID: 467414  Cd Length: 138  Bit Score: 67.59  E-value: 2.28e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624728525 247 ELSCLDLPDNVELRPFDLNDLSRLELTVRAPEGIWRDIPVRFECVIPEGYPHERLRVRCLS 307
Cdd:cd23794     9 DLEELDLPGQCKVEFPDPNDLLKFEVTITPDEGYYKGGTFVFEIDIPDNYPFEPPKVKCLT 69
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 535-655 2.85e-13

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: 69.01  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETC---------ATFLRVVGSELIQKYLGEGPKLVREMFR-----VAEENAPSIIFIDEI 600
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1624728525 601 DAIGTKRYDATSGGE-KEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPALI 655
Cdd:cd19508   135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 422-476 8.79e-13

Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 63.29  E-value: 8.79e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1624728525 422 VGTMEEMIDDNHAIVTSSMGPEYYVNILSFVDKTLLEPGCSVLLHNKTNSVVGIL 476
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 690-734 4.14e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 58.32  E-value: 4.14e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1624728525 690 DVDLEEFVNTKDDLSGADIKAICTEAGLLALRERRMQITQADLRK 734
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 500-739 1.87e-09

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 60.34  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 500 IGGLEEQIQEIKEAvelplthpeLYEEVGIRPPKGVILYGPPGTGKTLLAKAVAN---ETCATFLRVVG----------- 565
Cdd:TIGR02928  17 IVHRDEQIEELAKA---------LRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKeleEAAEDRDVRVVtvyvncqildt 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 566 -----SELIQKYLGEGP----------KLVREMFRVAEENAPSIIFI-DEIDAIgtkrydATSGGEKEIQRTMLELLNQL 629
Cdd:TIGR02928  88 lyqvlVELANQLRGSGEevpttglstsEVFRRLYKELNERGDSLIIVlDEIDYL------VGDDDDLLYQLSRARSNGDL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 630 DGfdpqADVKVIMATNRI---ESLDPAlIRPGRIDRKIQLPNPDTKTKRKIFEiHTSKMTMAQDVDLEEFVNTKDDLSGA 706
Cdd:TIGR02928 162 DN----AKVGVIGISNDLkfrENLDPR-VKSSLCEEEIIFPPYDAEELRDILE-NRAEKAFYDGVLDDGVIPLCAALAAQ 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1624728525 707 DI----KAICT--EAGLLALRERRMQITQADLRKAREKA 739
Cdd:TIGR02928 236 EHgdarKAIDLlrVAGEIAEREGAERVTEDHVEKAQEKI 274
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 503-665 3.51e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 56.00  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 503 LEEQIQEIKEAVELPLTHPELYeevgirppKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQkyLG-EGPKLVR 581
Cdd:cd19512     1 LEARVRDIAIATRNTKKNKGLY--------RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 582 EMFRVAEE-NAPSIIFIDEIDAIGTKRydaTSGGEKEIQRTMLELLNQLDGfDPQADVKVIMATNRIESLDPALirPGRI 660
Cdd:cd19512    71 KVFDWANTsRRGLLLFVDEADAFLRKR---STEKISEDLRAALNAFLYRTG-EQSNKFMLVLASNQPEQFDWAI--NDRI 144


                  ....*
gi 1624728525 661 DRKIQ 665
Cdd:cd19512   145 DEMVE 149
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 535-600 8.30e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.53  E-value: 8.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRV--VGSeliqkylgeGPKLVREMFRVAEENA----PSIIFIDEI 600
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 528-666 2.24e-08

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: 53.92  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 528 GIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQ---KYLGEGPKLVREM-----------FRVAEENAPS 593
Cdd:cd19505     8 GLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpDFGNDDWIDGMLIlkeslhrlnlqFELAKAMSPC 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525 594 IIFIDEIDAIGTKRydaTSGGEKEIQRTMLELLNQLDGFDPQADVK----VIMATNRIESLDPALIRPGRIDRKIQL 666
Cdd:cd19505    88 IIWIPNIHELNVNR---STQNLEEDPKLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
504-739 3.58e-08

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 56.39  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 504 EEQIQEIKEAVElPLTHPElyeevgirPPKGVILYGPPGTGKTLLAKAVANE--------------------TCATFLRV 563
Cdd:COG1474    32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergvdvrvvyvncrQASTRYRV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 564 VgSELIQKyLGEGPKL---------VREMF--RVAEENAPSIIFIDEIDAIGTKRYDatsggekeiqrtmlELLNQL--- 629
Cdd:COG1474   103 L-SRILEE-LGSGEDIpstglstdeLFDRLyeALDERDGVLVVVLDEIDYLVDDEGD--------------DLLYQLlra 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 630 DGFDPQADVKVIMATNRI---ESLDPALIRPGRiDRKIQLPNPDTKTKRKIFEiHTSKMTMAQDVDLEEFVNTKDDLSGA 706
Cdd:COG1474   167 NEELEGARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFPPYDADELRDILE-DRAELAFYDGVLSDEVIPLIAALAAQ 244

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1624728525 707 DI----KAICT--EAGLLALRERRMQITQADLRKAREKA 739
Cdd:COG1474   245 EHgdarKAIDLlrVAGEIAEREGSDRVTEEHVREAREKI 283
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 535-600 6.52e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 55.48  E-value: 6.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRV--VGSeliqkylgeGPKLVREMFRVAEENAPS----IIFIDEI 600
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALsaVTS---------GVKDLREVIEEARQRRSAgrrtILFIDEI 101
PRK04195 PRK04195
replication factor C large subunit; Provisional
 530-657 1.96e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 54.16  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 530 RPPKGVILYGPPGTGKTLLAKAVANEtcatflrvVGSELIqkylgegpklvrEM-----------FRVAEENAPS----- 593
Cdd:PRK04195   37 KPKKALLLYGPPGVGKTSLAHALAND--------YGWEVI------------ELnasdqrtadviERVAGEAATSgslfg 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624728525 594 ----IIFIDEIDAIgTKRYDAtsGGEKEIqrtmLELLNqldgfdpQADVKVIMATNRIESLDPALIRP 657
Cdd:PRK04195   97 arrkLILLDEVDGI-HGNEDR--GGARAI----LELIK-------KAKQPIILTANDPYDPSLRELRN 150
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 534-656 3.29e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.98  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 534 GVILYGPPGTGKTLLAKAVANETC-ATFLRVVGS------ELIQKYL--GEGPKLV-REMFRVAEEnaPSIIFIDEIDAI 603
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVdGPLVRAARE--GEIAVLDEINRA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624728525 604 gtkrydatsggEKEIQRTMLELLN-----QLDGF----DPQADVKVIMATNRI----ESLDPALIR 656
Cdd:pfam07728  79 -----------NPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLdrglNELSPALRS 133
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 491-695 4.36e-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: 53.31  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 491 RAPLESYSDIGGLEEQIQEIKEAVELPLTHPELYEEVGIRPpKGVILYGPPGTGKTLLAKAVANETCA-TFLR------V 563
Cdd:TIGR03922 272 EAELAEQIGLERVKRQVAALKSSTAMALARAERGLPVAQTS-NHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreV 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 564 VGSELIQKYLGEGPKLVREMFrvaEENAPSIIFIDEIDAIGTKRYDATSG-GEKEIQRTMLELLNQLDgfdpqaDVKVIM 642
Cdd:TIGR03922 351 SRADLIGQYIGESEAKTNEII---DSALGGVLFLDEAYTLVETGYGQKDPfGLEAIDTLLARMENDRD------RLVVIG 421

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525 643 ATNRiESLDPAL-IRPG---RIDRKIQLPnpdTKTKRKIFEIhTSKMTMAQDVDLEE 695
Cdd:TIGR03922 422 AGYR-KDLDKFLeVNEGlrsRFTRVIEFP---SYSPDELVEI-ARRMATERDSVLDD 473
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 521-626 2.14e-06

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: 48.92  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 521 PELYEEVgirPPKGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQ-KYLGegpklvREMFRVAEENAPSIIFIDE 599
Cdd:cd19498    38 EELRDEV---TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDE 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1624728525 600 IDAI----GTKRYDATSGGekeIQRTMLELL 626
Cdd:cd19498   109 IDKIakrgGSSGPDVSREG---VQRDLLPIV 136
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 532-645 3.18e-06

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 47.96  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 532 PKGVILY-GPPGTGKTLLAKAVANE---TCATFLRVVGSELIQKYL--------------GEGPKLVREMFRvaeeNAPS 593
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrligappgyvgyEEGGQLTEAVRR----KPYS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1624728525 594 IIFIDEIDAIGtkrydatsggeKEIQRTMLELLN--QL-DGFDPQADVK---VIMATN 645
Cdd:pfam07724  78 IVLIDEIEKAH-----------PGVQNDLLQILEggTLtDKQGRTVDFKntlFIMTGN 124
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 533-635 3.98e-06

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: 47.94  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 533 KGVIL--YGPPGTGKTLLAKAVANETCATFLRV-VG-----SELI---QKYLGEGP-KLVREMFRVAEENApsIIFIDEI 600
Cdd:cd19500    36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPgRIIQALKKAGTNNP--VFLLDEI 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1624728525 601 DAIGTK-RYDATSGgekeiqrtMLELLnqldgfDPQ 635
Cdd:cd19500   114 DKIGSSfRGDPASA--------LLEVL------DPE 135
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 483-598 9.43e-06

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


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 47.91  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 483 LVSLMKVERAPLEsysDIGGLEEQIQEIKEAVELPLTHpelyeevgiRPPKGVILYGPPGTGKTLLAKAVANETCATFLR 562
Cdd:pfam05673  16 LEPVPHPDPVRLD---DLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLR 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1624728525 563 VVgsELIQKYLGEGPKLVREmfrVAEENAPSIIFID 598
Cdd:pfam05673  84 LI--EVDKEDLGDLPDLVDL---LRDRPYRFILFCD 114
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 529-600 1.36e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 48.23  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 529 IRPPKGVILYGPPGTGKTLLAKAVANETCAT----FLRVV------GSELIQKY---LGEG-----PKLVREMFRVAEEN 590
Cdd:COG1401   218 LKTKKNVILAGPPGTGKTYLARRLAEALGGEdngrIEFVQfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKN 297

                          90
                  ....*....|..
gi 1624728525 591 --APSIIFIDEI 600
Cdd:COG1401   298 pdKPYVLIIDEI 309
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
529-564 2.35e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 46.31  E-value: 2.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1624728525 529 IRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVV 564
Cdd:COG1484    96 IERGENLILLGPPGTGKTHLAIALGHEACRAGYRVR 131
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
535-600 3.50e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.66  E-value: 3.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATfLRVVGSELIQKylgegPKLVREMFRVAEENapSIIFIDEI 600
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-----PGDLAAILTNLEEG--DVLFIDEI 111
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 500-664 4.58e-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: 44.86  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 500 IGGLEEQIQEIKEAVELP---LTHPElyeevgiRPPKGVILYGPPGTGKTLLAKAVANETCAT---FLRVVGSELIQK-- 571
Cdd:cd19499    13 VVGQDEAVKAVSDAIRRAragLSDPN-------RPIGSFLFLGPTGVGKTELAKALAELLFGDednLIRIDMSEYMEKhs 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 572 ----------YLG--EGPKLVREMFRvaeeNAPSIIFIDEIDAigtkrydatsgGEKEIQRTMLELLNQ---LDGFDPQA 636
Cdd:cd19499    86 vsrligappgYVGytEGGQLTEAVRR----KPYSVVLLDEIEK-----------AHPDVQNLLLQVLDDgrlTDSHGRTV 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1624728525 637 DVK---VIMATNRiesLDPALIrpGRIDRKI 664
Cdd:cd19499   151 DFKntiIIMTSNH---FRPEFL--NRIDEIV 176
PRK13341 PRK13341
AAA family ATPase;
536-600 5.17e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.59  E-value: 5.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 536 ILYGPPGTGKTLLAKAVANETCATFLrVVGSELiqkylgEGPKLVREMFRVAEE-----NAPSIIFIDEI 600
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKErlerhGKRTILFIDEV 118
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 535-651 1.15e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 42.49  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLgegpklvREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGG 614
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1624728525 615 EKEIQRTMLELLNQLDgfdpqadvKVIMATNRIESLD 651
Cdd:cd01120    74 LLEDLAKLLRAARNTG--------ITVIATIHSDKFD 102
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 533-599 1.41e-04

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 42.90  E-value: 1.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624728525 533 KGVILYGPPGTGKTLLAKAVANETCATFLRVVGSELIQKYLGEG--PKLVREMFRVAEENAPSIIFIDE 599
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 535-601 2.02e-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: 44.00  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRV-----------VGSELIQK-----YLGEGPklvreMFRvaeenapSIIFID 598
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQqtgefEFRPGP-----LFA-------NVLLAD 101


                  ...
gi 1624728525 599 EID 601
Cdd:COG0714   102 EIN 104
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 535-737 2.12e-04

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 43.79  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANE-------------TCATFLRVVGSELiqkYLGEGPKLVREMFRVAEE---NAPSIIFID 598
Cdd:COG2842    53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILErlaGTGRLLIID 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 599 EIDAIGTKrydatsggekeiqrtMLELLNQLdgFDpQADVKVIMATNriESLdPALIRP-----GRIDRKIQLPNPDTKT 673
Cdd:COG2842   130 EADHLKPK---------------ALEELRDI--HD-ETGVGVVLIGM--ERL-PAKLKRyeqlySRIGFWVEFKPLSLED 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624728525 674 KRKIFEIhtskmtmAQDVDLEEFVNTKDDLSGADIKAICT---EAGLLALRERRMQITQADLRKARE 737
Cdd:COG2842   189 VRALAEA-------WGELTDPDLLELLHRITRGNLRRLDRtlrLAARAAKRNGLTKITLDHVRAAAL 248
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 508-604 2.74e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 43.83  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 508 QEIKEAVELPLTHPELYEEVgirpPKGVILYGPPGTGKTLLAKAVANETcATFLRVVGSELIQKylgegPKLVREMFRVA 587
Cdd:TIGR00635  10 EKVKEQLQLFIEAAKMRQEA----LDHLLLYGPPGLGKTTLAHIIANEM-GVNLKITSGPALEK-----PGDLAAILTNL 79

                          90
                  ....*....|....*..
gi 1624728525 588 EENapSIIFIDEIDAIG 604
Cdd:TIGR00635  80 EEG--DVLFIDEIHRLS 94
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 535-606 4.69e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 42.59  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKavaneTCATFLRVV-----GSELIQK-YLGEG-----PKLVRE-MFRVaEENAPSIIFIDEIDA 602
Cdd:cd19497    53 ILLIGPTGSGKTLLAQ-----TLAKILDVPfaiadATTLTEAgYVGEDvenilLKLLQAaDYDV-ERAQRGIVYIDEIDK 126


                  ....
gi 1624728525 603 IGTK 606
Cdd:cd19497   127 IARK 130
cdc6 PRK00411
ORC1-type DNA replication protein;
504-742 5.09e-04

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 43.30  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 504 EEQIQEIKEAVElPLTHpelyeevGIRPPKgVILYGPPGTGKTLLAKAVANE-------------TC---ATFLRVVgSE 567
Cdd:PRK00411   36 EEQIEELAFALR-PALR-------GSRPLN-VLIYGPPGTGKTTTVKKVFEEleeiavkvvyvyiNCqidRTRYAIF-SE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 568 LIQKYLGEGPKLV----REMF-----RVAEENAPSIIFIDEIDAIgtkrydatsgGEKEIQRTMLELLNQLDGFdPQADV 638
Cdd:PRK00411  106 IARQLFGHPPPSSglsfDELFdkiaeYLDERDRVLIVALDDINYL----------FEKEGNDVLYSLLRAHEEY-PGARI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 639 KVIMATNRIESLDpalirpgRIDRKIQ---LPN-----PDTKTkrKIFEIHTSKMTMA------QDVDLEEFVNTKDDLS 704
Cdd:PRK00411  175 GVIGISSDLTFLY-------ILDPRVKsvfRPEeiyfpPYTAD--EIFDILKDRVEEGfypgvvDDEVLDLIADLTAREH 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1624728525 705 GADIKAICT--EAGLLALRERRMQITQADLRKAREKALQL 742
Cdd:PRK00411  246 GDARVAIDLlrRAGLIAEREGSRKVTEEDVRKAYEKSEIV 285
44 PHA02544
clamp loader, small subunit; Provisional
 536-654 6.36e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.67  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 536 ILYGP-PGTGKTLLAKAVANETCATFLRVVGSELiqkylgeGPKLVR-EMFRVAE----ENAPSIIFIDEIDAIGTkryd 609
Cdd:PHA02544   46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDC-------RIDFVRnRLTRFAStvslTGGGKVIIIDEFDRLGL---- 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1624728525 610 atsggeKEIQRTMLELLNQLdgfdpQADVKVIMATNRIESLDPAL 654
Cdd:PHA02544  115 ------ADAQRHLRSFMEAY-----SKNCSFIITANNKNGIIEPL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 535-612 8.67e-04

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: 41.69  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETC-----ATFLRVvgSELIQKYL---GEGpKLVREMFRVAeenAPSIIFIDEI-----D 601
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAACrqgyrVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDELgylpfS 166

                          90
                  ....*....|....*....
gi 1624728525 602 AIGT--------KRYDATS 612
Cdd:NF038214  167 REGAnllfeliaDRYERGS 185
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 535-555 1.23e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.18  E-value: 1.23e-03
                          10        20
                  ....*....|....*....|.
gi 1624728525 535 VILYGPPGTGKTLLAKAVANE 555
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANE 56
PRK08116 PRK08116
hypothetical protein; Validated
 534-607 1.59e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.16  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 534 GVILYGPPGTGKTLLAKAVANETCATFLRVVG---SEL---IQKYLGEGPKLVREMFRVAEENAPSIIfideIDAIGTKR 607
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANELIEKGVPVIFvnfPQLlnrIKSTYKSSGKEDENEIIRSLVNADLLI----LDDLGAER 191
AAA_22 pfam13401
AAA domain;
529-643 2.11e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 529 IRPPKGVI-LYGPPGTGKTLLAKAVANETC-----------------ATFLRVVGSELIQKYLGEGPKL-VREMFR--VA 587
Cdd:pfam13401   1 IRFGAGILvLTGESGTGKTTLLRRLLEQLPevrdsvvfvdlpsgtspKDLLRALLRALGLPLSGRLSKEeLLAALQqlLL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1624728525 588 EENAPSIIFIDEIDAigtkrydatsggekeIQRTMLELLNQLDGFdPQADVKVIMA 643
Cdd:pfam13401  81 ALAVAVVLIIDEAQH---------------LSLEALEELRDLLNL-SSKLLQLILV 120
ycf2 CHL00206
Ycf2; Provisional
 528-641 2.77e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 41.43  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525  528 GIRPPKGVILYGPPGTGKTLLAKAVANETCATFLRVvgseLIQKYLgegpklvremfrvaeENAPSIIFIDEIDAIGTKR 607
Cdd:CHL00206  1626 ALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITV----FLNKFL---------------DNKPKGFLIDDIDIDDSDD 1686

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1624728525  608 YDATSGGEKEIQRTMLELLNQLDG-FDPQADVKVI 641
Cdd:CHL00206  1687 IDDSDDIDRDLDTELLTMMNALTMdMMPKIDRFYI 1721
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 535-566 3.78e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.58  E-value: 3.78e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLRVVGS 566
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDS 32
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 502-653 4.04e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.64  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624728525 502 GLEEQIQEIKEAvelplthpelYEEVGIRPPKGVILYGPPGTGKTLLAKAV---ANETCATFLRVVGSELIQkYLGEGPK 578
Cdd:pfam13191   4 GREEELEQLLDA----------LDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLP-YSPLLEA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624728525 579 LVREMFRVAEENAPSIIFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDPQADVKVIMATNRIESLDPA 653
Cdd:pfam13191  73 LTREGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEA 147
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
535-591 4.74e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.36  E-value: 4.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624728525 535 VILYGPPGTGKTLLAKAVANETCATFLR--VVGSEL-------IQKYLGEGPKLVREMFRVAEENA 591
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLfgaglapLERSPEATARTYARLLALARELL 67
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
533-555 5.24e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.95  E-value: 5.24e-03
                          10        20
                  ....*....|....*....|...
gi 1624728525 533 KGVILYGPPGTGKTLLAKAVANE 555
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARE 87
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 501-551 6.33e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 40.09  E-value: 6.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1624728525 501 GGLEEQIQEIKEAVelplthpeLYeevgirPPKG--VILYGPPGTGKTLLAKA 551
Cdd:COG1221   111 GSLKNAIEQAKAAI--------LY------PPKGlhTLILGPTGVGKSFFAEL 149
Prot_ATP_OB_N pfam17758
Proteasomal ATPase OB N-terminal domain; This is N-terminal oligonucleotide binding (OB) ...
 421-476 6.57e-03

Proteasomal ATPase OB N-terminal domain; This is N-terminal oligonucleotide binding (OB) domain of proteasomal ATPase


Pssm-ID: 436018  Cd Length: 62  Bit Score: 35.60  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1624728525 421 SVGTMEEMIDDNHAIVTSSMGPEYYVNILSFVDKTLLEPGCSVLLhNKTNSVVGIL 476
Cdd:pfam17758   1 TYGTFLRVDDDDGTADVSVGGRRMRVAVSPTVDASELRPGQQVRL-NEALVVVGAL 55
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 529-600 9.70e-03

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


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 38.58  E-value: 9.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624728525 529 IRPPKGVILYGPPGTGKTLLAKAVANETCAT-----FLRVVG-SELIQKYLGEGpKLVREMFRVAeenAPSIIFIDEI 600
Cdd:pfam01695  89 IDRAQNVVLLGPPGVGKTHLAIALGVEACRAgysvrFTSAADlVNQLKRAHGDG-KLTRKLQQLL---KPDVLILDEW 162
 
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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