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Conserved domains on  [gi|528497678|ref|XP_005156741|]
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fidgetin-like protein 1 isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 367-552 3.67e-129

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: 378.56  E-value: 3.67e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 367 EPKIIELIMSEIMDHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSG 446
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 447 ATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEDRI 526
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 528497678 527 LVVGATNRPQEIDEAARRRLAKRLYI 552
Cdd:cd19525  161 LVVGATNRPQEIDEAARRRLVKRLYI 186
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 610-658 2.01e-09

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


The actual alignment was detected with superfamily member pfam09336:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 53.65  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528497678  610 ISLSDIAtimAEQV--RPILYSDFQEALKTVRPSVSSKDLELYEEWNKTFG 658
Cdd:pfam09336  14 MTWMDIP---SDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 579-615 2.32e-07

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: 47.53  E-value: 2.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528497678  579 EMEKVVQGTEGFSGADMTQLCREAALGPIR----SISLSDI 615
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRrgleAVTQEDL 43
 
Name Accession Description Interval E-value
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 367-552 3.67e-129

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: 378.56  E-value: 3.67e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 367 EPKIIELIMSEIMDHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSG 446
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 447 ATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEDRI 526
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 528497678 527 LVVGATNRPQEIDEAARRRLAKRLYI 552
Cdd:cd19525  161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 383-645 3.22e-83

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 265.33  E-value: 3.22e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 383 PPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSK 460
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 461 WVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTD-GEHDSSRRIKTEFLVQLDGAatSAEDRILVVGATNRPQEID 539
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGF--ESRGDVLIIAATNRPDLLD 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 540 EAARR--RLAKRLYIPLPEAEARRQIVTNLMSHEKSQLGVDeMEKVVQGTEGFSGADMTQLCREAALGPIRsislSDIAT 617
Cdd:COG1222  230 PALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVD-LDKLAKLTEGFSGADLKAIVTEAGMFAIR----EGRDT 304

                        250       260
                 ....*....|....*....|....*...
gi 528497678 618 IMAEqvrpilysDFQEALKTVRPSVSSK 645
Cdd:COG1222  305 VTME--------DLEKAIEKVKKKTETA 324
cell_div_CdvC NF041006
cell division protein CdvC;
330-657 3.19e-70

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 232.70  E-value: 3.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 330 SRGASSKFISPMPRQEEDLKDNTPKDmQPVDERLKNFEPkiiELIMSEimdhGPPVAWDDIAGLEFAKATIKEIVVWPML 409
Cdd:NF041006  53 LRHAYEQMINEYKKRIEVLEELVPAE-PAGPDVEKESDE---ELVVKE----KPKVTFSDIVGLEDVKEALKEAIVYPSK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 410 RPDIFTglRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIAR-----CHQPAVI 484
Cdd:NF041006 125 RPDLFP--LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKARekskeEGKPAII 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 485 FIDEIDSLLSQRTdGEHDSSRRIKTEFLVQLDGAATSAED-RILVVGATNRPQEIDEAARRRLAKRLYIPLPEAEARRQi 563
Cdd:NF041006 203 FIDEIDALLGVYS-SEVGGEVRVRNQFLKEMDGLQDKSENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLE- 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 564 vtnLMSHEKSQLGVDE---MEKVVQGTEGFSGADMTQLCREAALGPIRSISLSDIatimaEQVRPILYSDFQEALKTVRP 640
Cdd:NF041006 281 ---LLKYYTSKIKLENdvdLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGL-----GEPRPITMEDFKEVLKIRKP 352

                        330
                 ....*....|....*..
gi 528497678 641 SVSSKDLELYEEWNKTF 657
Cdd:NF041006 353 SVNQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 350-658 5.58e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 236.34  E-value: 5.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  350 DNTPKDMQPVDERLKNFEPKIIELIMSEImdhgPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLF 427
Cdd:TIGR01243 419 KELKVTMKDFMEALKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLF 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  428 GPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQR-TDGEHDSSRR 506
Cdd:TIGR01243 494 GPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDR 573

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  507 IKTEFLVQLDGAATSAEdrILVVGATNRPQEIDEAARR--RLAKRLYIPLPEAEARRQIvtnLMSHEKS-QLGVD-EMEK 582
Cdd:TIGR01243 574 IVNQLLTEMDGIQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEI---FKIHTRSmPLAEDvDLEE 648

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  583 VVQGTEGFSGADMTQLCREAALGPIRSISLSDIATIMAEQVRPILYS------DFQEALKTVRPSVSSKDLELYEEWNKT 656
Cdd:TIGR01243 649 LAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKDlkvemrHFLEALKKVKPSVSKEDMLRYERLAKE 728


                  ..
gi 528497678  657 FG 658
Cdd:TIGR01243 729 LK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 380-608 9.73e-56

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 194.28  E-value: 9.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 380 DHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSL 457
Cdd:PRK03992 123 IESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV-GiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 458 TSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSR---RIKTEFLVQLDGAATSAEDRIlvVGATNR 534
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGFDPRGNVKI--IAATNR 279

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528497678 535 PQEIDEAARR--RLAKRLYIPLPEAEARRQIV---TNLMSHEKSqlgVDeMEKVVQGTEGFSGADMTQLCREAALGPIR 608
Cdd:PRK03992 280 IDILDPAILRpgRFDRIIEVPLPDEEGRLEILkihTRKMNLADD---VD-LEELAELTEGASGADLKAICTEAGMFAIR 354
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 424-554 4.39e-51

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: 173.16  E-value: 4.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  424 ILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDS 503
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528497678  504 SRRIKTEFLVQLDGaATSAEDRILVVGATNRPQEIDEAARRRLAKRLYIPL 554
Cdd:pfam00004  81 SRRVVNQLLTELDG-FTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 420-556 1.08e-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: 85.89  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678   420 PPKGILLFGPPGTGKTLIGKCIACQSGAT---FFSISASSLTS--------------KWVGEGEKMVRALFAIARCHQPA 482
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528497678   483 VIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLdgaatsaEDRILVVGATNRPQEIDEAA-RRRLAKRLYIPLPE 556
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS-------EKNLTVILTTNDEKDLGPALlRRRFDRRIVLLLIL 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 610-658 2.01e-09

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 53.65  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528497678  610 ISLSDIAtimAEQV--RPILYSDFQEALKTVRPSVSSKDLELYEEWNKTFG 658
Cdd:pfam09336  14 MTWMDIP---SDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 579-615 2.32e-07

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: 47.53  E-value: 2.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528497678  579 EMEKVVQGTEGFSGADMTQLCREAALGPIR----SISLSDI 615
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRrgleAVTQEDL 43
 
Name Accession Description Interval E-value
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 367-552 3.67e-129

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: 378.56  E-value: 3.67e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 367 EPKIIELIMSEIMDHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSG 446
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 447 ATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEDRI 526
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 528497678 527 LVVGATNRPQEIDEAARRRLAKRLYI 552
Cdd:cd19525  161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 390-552 1.25e-100

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: 304.27  E-value: 1.25e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 390 IAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMV 469
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 470 RALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEDRILVVGATNRPQEIDEAARRRLAKR 549
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                 ...
gi 528497678 550 LYI 552
Cdd:cd19509  161 IYI 163
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 389-552 5.77e-84

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: 261.32  E-value: 5.77e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKM 468
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 469 VRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEDRILVVGATNRPQEIDEAARRRLAK 548
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                 ....
gi 528497678 549 RLYI 552
Cdd:cd19524  161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 383-645 3.22e-83

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 265.33  E-value: 3.22e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 383 PPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSK 460
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 461 WVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTD-GEHDSSRRIKTEFLVQLDGAatSAEDRILVVGATNRPQEID 539
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGF--ESRGDVLIIAATNRPDLLD 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 540 EAARR--RLAKRLYIPLPEAEARRQIVTNLMSHEKSQLGVDeMEKVVQGTEGFSGADMTQLCREAALGPIRsislSDIAT 617
Cdd:COG1222  230 PALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVD-LDKLAKLTEGFSGADLKAIVTEAGMFAIR----EGRDT 304

                        250       260
                 ....*....|....*....|....*...
gi 528497678 618 IMAEqvrpilysDFQEALKTVRPSVSSK 645
Cdd:COG1222  305 VTME--------DLEKAIEKVKKKTETA 324
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 389-552 6.07e-73

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: 232.47  E-value: 6.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKM 468
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 469 VRALFAIARCHQPAVIFIDEIDSLLSQRTDgEHDSSRRIKTEFLVQLDGAATSAEDRILVVGATNRPQEIDEAARRRLAK 548
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDD-EASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                 ....
gi 528497678 549 RLYI 552
Cdd:cd19523  160 RLLV 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 387-624 1.43e-71

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: 237.12  E-value: 1.43e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 387 WDDIAGLEFAKATIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEG 465
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 466 EKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGaatsAEDRILVVGATNRPQEIDEAARRR 545
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEE----LRSDVVVIAATNRPDLLDPALLRR 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 546 LAKRLYIPLPEAEARRQIVTNLMSHEKSQLGVDeMEKVVQGTEGFSGADMTQLCREAALGPIR----SISLSDI-ATIMA 620
Cdd:COG0464  312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVD-LEELAEATEGLSGADIRNVVRRAALQALRlgrePVTTEDLlEALER 390


                 ....
gi 528497678 621 EQVR 624
Cdd:COG0464  391 EDIF 394
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 383-552 2.62e-70

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: 225.90  E-value: 2.62e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 383 PPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWV 462
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 463 GEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSaEDRILVVGATNRPQEIDEAA 542
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGND-SQGVLVLGATNIPWQLDSAI 160

                        170
                 ....*....|
gi 528497678 543 RRRLAKRLYI 552
Cdd:cd19521  161 RRRFEKRIYI 170
cell_div_CdvC NF041006
cell division protein CdvC;
330-657 3.19e-70

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 232.70  E-value: 3.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 330 SRGASSKFISPMPRQEEDLKDNTPKDmQPVDERLKNFEPkiiELIMSEimdhGPPVAWDDIAGLEFAKATIKEIVVWPML 409
Cdd:NF041006  53 LRHAYEQMINEYKKRIEVLEELVPAE-PAGPDVEKESDE---ELVVKE----KPKVTFSDIVGLEDVKEALKEAIVYPSK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 410 RPDIFTglRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIAR-----CHQPAVI 484
Cdd:NF041006 125 RPDLFP--LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKARekskeEGKPAII 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 485 FIDEIDSLLSQRTdGEHDSSRRIKTEFLVQLDGAATSAED-RILVVGATNRPQEIDEAARRRLAKRLYIPLPEAEARRQi 563
Cdd:NF041006 203 FIDEIDALLGVYS-SEVGGEVRVRNQFLKEMDGLQDKSENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLE- 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 564 vtnLMSHEKSQLGVDE---MEKVVQGTEGFSGADMTQLCREAALGPIRSISLSDIatimaEQVRPILYSDFQEALKTVRP 640
Cdd:NF041006 281 ---LLKYYTSKIKLENdvdLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGL-----GEPRPITMEDFKEVLKIRKP 352

                        330
                 ....*....|....*..
gi 528497678 641 SVSSKDLELYEEWNKTF 657
Cdd:NF041006 353 SVNQEMLKAYEAWHEKF 369
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 389-552 2.61e-68

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: 220.63  E-value: 2.61e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKM 468
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 469 VRALFAIARCHQPAVIFIDEIDSLLSQR-TDGEHDSSRRIKTEFLVQLDGAATSAEDR-----ILVVGATNRPQEIDEAA 542
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 528497678 543 RRRLAKRLYI 552
Cdd:cd19522  161 RRRLEKRIYI 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 350-658 5.58e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 236.34  E-value: 5.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  350 DNTPKDMQPVDERLKNFEPKIIELIMSEImdhgPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLF 427
Cdd:TIGR01243 419 KELKVTMKDFMEALKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLF 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  428 GPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQR-TDGEHDSSRR 506
Cdd:TIGR01243 494 GPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDR 573

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  507 IKTEFLVQLDGAATSAEdrILVVGATNRPQEIDEAARR--RLAKRLYIPLPEAEARRQIvtnLMSHEKS-QLGVD-EMEK 582
Cdd:TIGR01243 574 IVNQLLTEMDGIQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEI---FKIHTRSmPLAEDvDLEE 648

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  583 VVQGTEGFSGADMTQLCREAALGPIRSISLSDIATIMAEQVRPILYS------DFQEALKTVRPSVSSKDLELYEEWNKT 656
Cdd:TIGR01243 649 LAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKDlkvemrHFLEALKKVKPSVSKEDMLRYERLAKE 728


                  ..
gi 528497678  657 FG 658
Cdd:TIGR01243 729 LK 730
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 389-552 7.46e-66

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: 213.83  E-value: 7.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIF--TGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGE 466
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 467 KMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEDRILVVGATNRPQEIDEAARRRL 546
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 528497678 547 AKRLYI 552
Cdd:cd19520  161 PKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 280-641 8.48e-57

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: 205.14  E-value: 8.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  280 LRGEEGISTNFRSAREQFIVDQQKK---HSHQGQRGSPGNVFTITKKCLGANRSRGasSKFISPMPRQEEDLK--DNTPK 354
Cdd:TIGR01243  69 LRANAGVTIGDTVTVERAEVKEAKKvvlAPTQPIRFGRDFVDYVKEFLLGKPISKG--ETVIVPVLEGALPFVvvSTQPA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  355 DMQPVDErlkNFEPKIIELIMSEIMDHG-PPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGT 432
Cdd:TIGR01243 147 GFVYVTE---ATEVEIREKPVREEIERKvPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGT 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  433 GKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFL 512
Cdd:TIGR01243 224 GKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLL 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  513 VQLDGaaTSAEDRILVVGATNRPQEIDEAARR--RLAKRLYIPLPEAEARRQIvtnLMSHEKSQLGVDE--MEKVVQGTE 588
Cdd:TIGR01243 304 TLMDG--LKGRGRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEI---LKVHTRNMPLAEDvdLDKLAEVTH 378

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  589 GFSGADMTQLCREAALGPIRSISLSDIATIMAEQV-RPIL------YSDFQEALKTVRPS 641
Cdd:TIGR01243 379 GFVGADLAALAKEAAMAALRRFIREGKINFEAEEIpAEVLkelkvtMKDFMEALKMVEPS 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 380-608 9.73e-56

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 194.28  E-value: 9.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 380 DHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSL 457
Cdd:PRK03992 123 IESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV-GiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 458 TSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSR---RIKTEFLVQLDGAATSAEDRIlvVGATNR 534
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGFDPRGNVKI--IAATNR 279

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528497678 535 PQEIDEAARR--RLAKRLYIPLPEAEARRQIV---TNLMSHEKSqlgVDeMEKVVQGTEGFSGADMTQLCREAALGPIR 608
Cdd:PRK03992 280 IDILDPAILRpgRFDRIIEVPLPDEEGRLEILkihTRKMNLADD---VD-LEELAELTEGASGADLKAICTEAGMFAIR 354
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 389-552 1.68e-51

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 175.56  E-value: 1.68e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGE 466
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 467 KMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAatSAEDRILVVGATNRPQEIDEAARR-- 544
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM--SSRGKVVVIAATNRPDAIDPALRRpg 157


                 ....*...
gi 528497678 545 RLAKRLYI 552
Cdd:cd19503  158 RFDREVEI 165
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 328-608 2.16e-51

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: 181.92  E-value: 2.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  328 NRSRGASSKFISPMPRQEEDLKDNTPKDMQPV--DERLKNFEpkiielimseiMDHGPPVAWDDIAGLEFAKATIKEIVV 405
Cdd:TIGR01242  71 NVSAFIDRKSLKPGARVALNQQTLTIVDVLPTskDPLVKGME-----------VEERPNVSYEDIGGLEEQIREIREAVE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  406 WPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVI 484
Cdd:TIGR01242 140 LPLKHPELFEEVGiEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSII 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  485 FIDEIDSLLSQRTDGEHDSSR---RIKTEFLVQLDGaaTSAEDRILVVGATNRPQEIDEAARR--RLAKRLYIPLPEAEA 559
Cdd:TIGR01242 220 FIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAELDG--FDPRGNVKVIAATNRPDILDPALLRpgRFDRIIEVPLPDFEG 297

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 528497678  560 RRQIVTNLMSHEKSQLGVDeMEKVVQGTEGFSGADMTQLCREAALGPIR 608
Cdd:TIGR01242 298 RLEILKIHTRKMKLAEDVD-LEAIAKMTEGASGADLKAICTEAGMFAIR 345
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 396-552 2.37e-51

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: 174.78  E-value: 2.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 396 AKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALF 473
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIR-PPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 474 AIARCHQPAVIFIDEIDSLLSQRTD-GEHDSSRRIKTEFLVQLDGAatSAEDRILVVGATNRPQEIDEAARR--RLAKRL 550
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQsDSSGVTDRVVSQLLTELDGI--ESLKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                 ..
gi 528497678 551 YI 552
Cdd:cd19511  158 YV 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 396-552 2.73e-51

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: 174.78  E-value: 2.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 396 AKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAI 475
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 476 ARCHQPAVIFIDEIDSLLSQRTD-GEHDSSRRIKTEFLVQLDGAATsaEDRILVVGATNRPQEIDEAARR--RLAKRLYI 552
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSsGESGELRRVLNQLLTELDGVNS--RSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 424-554 4.39e-51

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: 173.16  E-value: 4.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  424 ILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDS 503
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528497678  504 SRRIKTEFLVQLDGaATSAEDRILVVGATNRPQEIDEAARRRLAKRLYIPL 554
Cdd:pfam00004  81 SRRVVNQLLTELDG-FTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 379-630 5.69e-47

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: 173.24  E-value: 5.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  379 MDHGPPVAWDDIAGLEFAKATIKEIVVWpmLR-PDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASS 456
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDF--LKnPSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  457 LTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQR---TDGEHDSSRRIKTEFLVQLDGAATSaeDRILVVGATN 533
Cdd:TIGR01241 124 FVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGNDEREQTLNQLLVEMDGFGTN--TGVIVIAATN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  534 RPQEIDEAARR--RLAKRLYIPLPEAEARRQIvtnLMSHEKsQLGVDEM---EKVVQGTEGFSGADMTQLCREAALGPIR 608
Cdd:TIGR01241 202 RPDVLDPALLRpgRFDRQVVVDLPDIKGREEI---LKVHAK-NKKLAPDvdlKAVARRTPGFSGADLANLLNEAALLAAR 277

                         250       260       270
                  ....*....|....*....|....*....|.
gi 528497678  609 S----ISLSDIA-----TIMAEQVRPILYSD 630
Cdd:TIGR01241 278 KnkteITMNDIEeaidrVIAGPEKKSRVISE 308
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 396-552 1.91e-46

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: 161.51  E-value: 1.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 396 AKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALF 473
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIR-PPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 474 AIARCHQPAVIFIDEIDSLLSQR-TDGEHDSSRRIKTEFLVQLDGAATSAEdrILVVGATNRPQEIDEAARR--RLAKRL 550
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLI 157


                 ..
gi 528497678 551 YI 552
Cdd:cd19529  158 YI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
387-636 7.09e-46

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 163.13  E-value: 7.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 387 WDDIAGLEFAKATIKEIVVWPMLRPDiftgLRG----PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWV 462
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRREN----LRKfglwPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 463 GEGEKMVRALFAIARCHqPAVIFIDEIDSLLSQRTD-GEHDSSRRIKTEFLVQLDGAAtsaeDRILVVGATNRPQEIDEA 541
Cdd:COG1223   77 GETARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGLP----SGSVVIAATNHPELLDSA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 542 ARRRLAKRLYIPLPEAEARRQIVTNLMSHEKSQLGVDeMEKVVQGTEGFSGADMTQLCREAALgpiRSIslsdiatimAE 621
Cdd:COG1223  152 LWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFELD-LKKLAKKLEGLSGADIEKVLKTALK---KAI---------LE 218

                        250
                 ....*....|....*
gi 528497678 622 QVRPILYSDFQEALK 636
Cdd:COG1223  219 DREKVTKEDLEEALK 233
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 387-544 9.65e-46

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: 160.20  E-value: 9.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 387 WDDIAGLEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEG 465
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 466 EKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSR---RIKTEFLVQLDGAATSaeDRILVVGATNRPQEIDEAA 542
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPR--GNIKVIMATNRPDILDPAL 159


                 ..
gi 528497678 543 RR 544
Cdd:cd19502  160 LR 161
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 379-608 3.15e-44

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 164.17  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 379 MDHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASS 456
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 457 LTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKT---EFLVQLDGAATSAEdrILVVGATN 533
Cdd:PTZ00361 253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRtmlELLNQLDGFDSRGD--VKVIMATN 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 534 RPQEIDEAARR--RLAKRLYIPLPEAEARR---QIVTNLMSHEKSqlgVDeMEKVVQGTEGFSGADMTQLCREAALGPIR 608
Cdd:PTZ00361 331 RIESLDPALIRpgRIDRKIEFPNPDEKTKRrifEIHTSKMTLAED---VD-LEEFIMAKDELSGADIKAICTEAGLLALR 406
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 379-638 3.69e-44

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 163.01  E-value: 3.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 379 MDHGPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSL 457
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 458 TSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSR---RIKTEFLVQLDGAATSAEdrILVVGATNR 534
Cdd:PTZ00454 216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN--VKVIMATNR 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 535 PQEIDEAARR--RLAKRLYIPLPEAEARR---QIVTNLMSHEKSqlgVDeMEKVVQGTEGFSGADMTQLCREAALGPIRs 609
Cdd:PTZ00454 294 ADTLDPALLRpgRLDRKIEFPLPDRRQKRlifQTITSKMNLSEE---VD-LEDFVSRPEKISAADIAAICQEAGMQAVR- 368

                        250       260
                 ....*....|....*....|....*....
gi 528497678 610 islsdiatimaEQVRPILYSDFQEALKTV 638
Cdd:PTZ00454 369 -----------KNRYVILPKDFEKGYKTV 386
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 389-544 2.83e-43

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: 153.36  E-value: 2.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEK 467
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528497678 468 MVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAedRILVVGATNRPQEIDEAARR 544
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPALRR 155
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 385-552 1.24e-42

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: 151.62  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 385 VAWDDIAGLEFAKATIKEIVVWpMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVG 463
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 464 EGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGE---HDSSRRIKTEFLVQLDGAATSaeDRILVVGATNRPQEIDE 540
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFESN--TGVIVIAATNRPDVLDP 157

                        170
                 ....*....|....
gi 528497678 541 AARR--RLAKRLYI 552
Cdd:cd19501  158 ALLRpgRFDRQVYV 171
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 404-552 3.06e-38

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: 139.16  E-value: 3.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 404 VVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIARCHQPA 482
Cdd:cd19530   12 ILRPIKRPDIYKALGiDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528497678 483 VIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAatSAEDRILVVGATNRPQEIDEAARR--RLAKRLYI 552
Cdd:cd19530   92 VIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGL--EERSNVFVIAATNRPDIIDPAMLRpgRLDKTLYV 161
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
389-608 3.24e-38

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 150.57  E-value: 3.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEK 467
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 468 MVRALFAIARCHQPAVIFIDEIDSLLSQR---TDGEHDSSRRIKTEFLVQLDGaaTSAEDRILVVGATNRPQEIDEAARR 544
Cdd:PRK10733 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRgagLGGGHDEREQTLNQMLVEMDG--FEGNEGIIVIAATNRPDVLDPALLR 309

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528497678 545 --RLAKRLYIPLPEAEARRQIVTNLMSHEKSQLGVDEmEKVVQGTEGFSGADMTQLCREAALGPIR 608
Cdd:PRK10733 310 pgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDA-AIIARGTPGFSGADLANLVNEAALFAAR 374
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
378-604 1.18e-37

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 147.88  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 378 IMDHGPPVAWDDIAGLEFAKATIKEIVvwPMLR-PDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISAS 455
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQEIV--DFLKdPEKFTRLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 456 SLTSKWVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQR---TDGEHDssrriktE-------FLVQLDGAATSaeDR 525
Cdd:COG0465  210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGHD-------EreqtlnqLLVEMDGFEGN--EG 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 526 ILVVGATNRPqEI-DEAARR--RLAKRLYIPLPEAEARRQIvtnLMSHEKS-QLG--VDeMEKVVQGTEGFSGADMTQLC 599
Cdd:COG0465  281 VIVIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAI---LKVHARKkPLApdVD-LEVIARRTPGFSGADLANLV 355


                 ....*
gi 528497678 600 REAAL 604
Cdd:COG0465  356 NEAAL 360
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 397-552 1.86e-37

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: 136.87  E-value: 1.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 397 KATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFA 474
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLkfGMT-PSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 475 IARCHQPAVIFIDEIDSLLSQR---TDGEHDSSRRIKTEFLVQLDGaaTSAEDRILVVGATNRPQEIDEAARR--RLAKR 549
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARggnIGDAGGAADRVINQILTEMDG--MNTKKNVFIIGATNRPDIIDPAILRpgRLDQL 158


                 ...
gi 528497678 550 LYI 552
Cdd:cd19528  159 IYI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 389-544 1.05e-36

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: 135.33  E-value: 1.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIA--CQSGA---TFFSISASSLTSKWV 462
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAaeCSKGGqkvSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 463 GEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLDGAATSAEdrILVVGATNRPQEIDEAA 542
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPAL 158


                 ..
gi 528497678 543 RR 544
Cdd:cd19517  159 RR 160
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 389-544 7.43e-36

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: 132.53  E-value: 7.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKATIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGE 466
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 467 KMVRALFAIARCHQPAVIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLD--GAATSAEDRILVVGATNRPQEIDEAARR 544
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDelNNEKTAGGPVLVIGATNRPDSLDPALRR 159
ftsH CHL00176
cell division protein; Validated
 385-604 2.33e-35

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 141.73  E-value: 2.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 385 VAWDDIAGLEFAKATIKEIVVWpMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVG 463
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 464 EGEKMVRALFAIARCHQPAVIFIDEIDSLLSQR---TDGEHDSSRRIKTEFLVQLDGaaTSAEDRILVVGATNRPQEIDE 540
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagIGGGNDEREQTLNQLLTEMDG--FKGNKGVIVIAATNRVDILDA 336

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528497678 541 AARR--RLAKRLYIPLPEAEARRQIvtnLMSHEKSQLGVDEMEKVV--QGTEGFSGADMTQLCREAAL 604
Cdd:CHL00176 337 ALLRpgRFDRQITVSLPDREGRLDI---LKVHARNKKLSPDVSLELiaRRTPGFSGADLANLLNEAAI 401
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 372-565 7.55e-35

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: 138.69  E-value: 7.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  372 ELIMSEImdhgPPVAWDDIAGLEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIA---CQSG 446
Cdd:TIGR03689 170 DLVLEEV----PDVTYADIGGLGSQIEQIRDAVELPFLHPELYReyGLK-PPKGVLLYGPPGCGKTLIAKAVAnslAARI 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  447 AT-------FFSISASSLTSKWVGEGEKMVRALFAIAR----CHQPAVIFIDEIDSLLsqRTDGEHDSS---RRIKTEFL 512
Cdd:TIGR03689 245 GAegggksyFLNIKGPELLNKYVGETERQIRLIFQRARekasEGRPVIVFFDEMDSLF--RTRGSGVSSdveTTVVPQLL 322

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 528497678  513 VQLDGaaTSAEDRILVVGATNRPQEIDEAARR--RLAKRLYIPLPEAEARRQIVT 565
Cdd:TIGR03689 323 AEIDG--VESLDNVIVIGASNREDMIDPAILRpgRLDVKIRIERPDAEAAADIFA 375
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 397-552 4.25e-34

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: 127.63  E-value: 4.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 397 KATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFAIA 476
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 477 RCHQPAVIFIDEIDSLLSQRTDGEhDSS---RRIKTEFLVQLDGAATSAEDrILVVGATNRPQEIDEAARR--RLAKRLY 551
Cdd:cd19527   82 RDAKPCVIFFDELDSLAPSRGNSG-DSGgvmDRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLY 159


                 .
gi 528497678 552 I 552
Cdd:cd19527  160 L 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 396-551 2.03e-32

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: 122.54  E-value: 2.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 396 AKATIKEIVVWPMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEGEKMVRALFA 474
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRlRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 475 IARCHQPAVIFIDEIDSLLSQRTdgeHDSS---RRIKTEFLVQLDGAatSAEDRILVVGATNRPQEIDEAARR--RLAKR 549
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRG---HDSTgvtDRVVNQLLTQLDGV--EGLDGVYVLAATSRPDLIDPALLRpgRLDKL 155


                 ..
gi 528497678 550 LY 551
Cdd:cd19526  156 VY 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 391-554 1.18e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 103.38  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 391 AGLEFAKATIKEIVvwpmlrpdiftgLRGPPKGILLFGPPGTGKTLIGKCIACQS---GATFFSISASSLTSKWVGEGEK 467
Cdd:cd00009    1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 468 ---MVRALFAIARCHQPAVIFIDEIDSLlsqrtdgehdsSRRIKTEFLVQLDGAATSAE--DRILVVGATNRP--QEIDE 540
Cdd:cd00009   69 ghfLVRLLFELAEKAKPGVLFIDEIDSL-----------SRGAQNALLRVLETLNDLRIdrENVRVIGATNRPllGDLDR 137

                        170
                 ....*....|....
gi 528497678 541 AARRRLAKRLYIPL 554
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 422-544 3.34e-20

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: 88.32  E-value: 3.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 422 KGILLFGPPGTGKTLIGKCIACQSGATFFSI-SASSLTSKWVGEGEKMVRALFAIARCHQPA--------VIFIDEIDSL 492
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528497678 493 LSQR-----TDGEHDSsrrIKTEFLVQLDGaaTSAEDRILVVGATNRPQEIDEAARR 544
Cdd:cd19504  116 CKQRgsmagSTGVHDT---VVNQLLSKIDG--VEQLNNILVIGMTNRKDLIDEALLR 167
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 420-556 1.08e-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: 85.89  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678   420 PPKGILLFGPPGTGKTLIGKCIACQSGAT---FFSISASSLTS--------------KWVGEGEKMVRALFAIARCHQPA 482
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528497678   483 VIFIDEIDSLLSQRTDGEHDSSRRIKTEFLVQLdgaatsaEDRILVVGATNRPQEIDEAA-RRRLAKRLYIPLPE 556
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS-------EKNLTVILTTNDEKDLGPALlRRRFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 389-543 9.03e-16

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: 75.10  E-value: 9.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 389 DIAGLEFAKAtikeivvWPMLRPDIFT------GLrGPPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWV 462
Cdd:cd19507    1 DVGGLDNLKD-------WLKKRKAAFSkqasayGL-PTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 463 GEGEKMVRALFAIARCHQPAVIFIDEIDSLLS-QRTDGEHDSSRRIKTEFLVQLdgaatsAEDR--ILVVGATNR----P 535
Cdd:cd19507   73 GESESRLRQMIQTAEAIAPCVLWIDEIEKGFSnADSKGDSGTSSRVLGTFLTWL------QEKKkpVFVVATANNvqslP 146


                 ....*...
gi 528497678 536 QEIDEAAR 543
Cdd:cd19507  147 PELLRKGR 154
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 422-539 3.51e-14

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: 70.63  E-value: 3.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 422 KGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKWVGEG--EKMVRALFAIARCHQPAVIFIDEIDSLLSQ---R 496
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKkvpK 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 528497678 497 TDGEHDSSR--RIKTEFLVQLdgaatSAEDRILVVGATNRPQEID 539
Cdd:cd19506  107 TEKQLDPKRlkKDLPKILKSL-----KPEDRVLIVGTTSRPFEAD 146
ycf46 CHL00195
Ycf46; Provisional
 388-630 2.48e-12

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 69.66  E-value: 2.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 388 DDIAGLEFAKAtikeivvWPMLRPDIFT------GLrgP-PKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSK 460
Cdd:CHL00195 228 SDIGGLDNLKD-------WLKKRSTSFSkqasnyGL--PtPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 461 WVGEGEKMVRALFAIARCHQPAVIFIDEIDSLLSQrTDGEHDS--SRRIKTEFLVQLdgaatsAEDR--ILVVGATNR-- 534
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSN-SESKGDSgtTNRVLATFITWL------SEKKspVFVVATANNid 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 535 --PQEIdeaARR-RLAKRLYIPLPEAEARRQIVT-NLMSHEKSQLGVDEMEKVVQGTEGFSGADMTQLCREA---ALGPI 607
Cdd:CHL00195 372 llPLEI---LRKgRFDEIFFLDLPSLEEREKIFKiHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAmyiAFYEK 448

                        250       260
                 ....*....|....*....|...
gi 528497678 608 RSISLSDIATIMaEQVRPILYSD 630
Cdd:CHL00195 449 REFTTDDILLAL-KQFIPLAQTE 470
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 418-546 2.15e-10

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 59.46  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 418 RGPPKGILLFGPPGTGKTLIGKCIACQSGATfFSISASSLTSKWVGEGEKMVRALFAIARCHQPAVI-FIDEIDSLLSQR 496
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKR 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528497678 497 -TDGEHDSSRRIKTEFLVQldgaaTSAEDR-ILVVGATNRPQEIDEAARRRL 546
Cdd:cd19512   98 sTEKISEDLRAALNAFLYR-----TGEQSNkFMLVLASNQPEQFDWAINDRI 144
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 421-505 1.68e-09

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 57.77  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 421 PKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTS-KWVG-EGEKMVRALFAiarchqpAVIFIDEIDSLLSQRTD 498
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118


                 ....*..
gi 528497678 499 GEHDSSR 505
Cdd:cd19498  119 SGPDVSR 125
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 610-658 2.01e-09

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 53.65  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528497678  610 ISLSDIAtimAEQV--RPILYSDFQEALKTVRPSVSSKDLELYEEWNKTFG 658
Cdd:pfam09336  14 MTWMDIP---SDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 424-493 2.56e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 59.68  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 424 ILLFGPPGTGKTLIGKCIACQSGATFFSISAssltskwVGEGEKMVRALFAIAR----CHQPAVIFIDEI--------DS 491
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARerraYGRRTILFVDEIhrfnkaqqDA 124


                 ..
gi 528497678 492 LL 493
Cdd:COG2256  125 LL 126
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 424-552 4.33e-09

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: 56.69  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 424 ILLFGPPGTGKTLIGKCIACQ---------SGATFFSISASSLTSKWVGEGEKMVRALF-AIARC--HQPAVIF--IDEI 489
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFqKIQELidDKDALVFvlIDEV 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528497678 490 DSLLSQRTD----GEHDSSRRIKTEFLVQLDGAATSaeDRILVVGATNRPQEIDEAARRRLAKRLYI 552
Cdd:cd19508  135 ESLAAARSAsssgTEPSDAIRVVNAVLTQIDRIKRY--HNNVILLTSNLLEKIDVAFVDRADIKQYI 199
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 417-564 1.77e-08

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: 56.33  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 417 LRGPpkgILLFGPPGTGKTLIGKCIACQSGATFFSIS------ASSLTSKWV---GEGEKMVR--ALFAiarchqpAVIF 485
Cdd:COG0714   30 AGGH---LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILGTYIydqQTGEFEFRpgPLFA-------NVLL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 486 IDEIDsllsqRTDgehdssrrIKT---------EFLVQLDGAATSAEDRILVVgATNRPQEID------EAARRRLAKRL 550
Cdd:COG0714  100 ADEIN-----RAP--------PKTqsalleameERQVTIPGGTYKLPEPFLVI-ATQNPIEQEgtyplpEAQLDRFLLKL 165

                        170
                 ....*....|....
gi 528497678 551 YIPLPEAEARRQIV 564
Cdd:COG0714  166 YIGYPDAEEEREIL 179
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 424-493 2.07e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.02  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 424 ILLFGPPGTGKTLIGKCIACQSGATFFSISASSltskwvgEGEKMVRALFAIARCH----QPAVIFIDEI--------DS 491
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEIhrfnkaqqDA 111


                 ..
gi 528497678 492 LL 493
Cdd:PRK13342 112 LL 113
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 579-615 2.32e-07

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: 47.53  E-value: 2.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 528497678  579 EMEKVVQGTEGFSGADMTQLCREAALGPIR----SISLSDI 615
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRrgleAVTQEDL 43
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 388-492 1.82e-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: 48.71  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 388 DDIAGLEFAKATIKEIVVWPMLRPDIftglRGPpkgILLF-GPPGTGKTLIGKCIACQSGATFFSISASSLTSkwvgEGE 466
Cdd:cd19500   10 ADHYGLEDVKERILEYLAVRKLKGSM----KGP---ILCLvGPPGVGKTSLGKSIARALGRKFVRISLGGVRD----EAE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528497678 467 --------------KMVRALfAIARCHQPaVIFIDEIDSL 492
Cdd:cd19500   79 irghrrtyvgampgRIIQAL-KKAGTNNP-VFLLDEIDKI 116
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 420-541 2.34e-06

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: 48.14  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 420 PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKW--------------VGEGEKMVRALFAIARCHQPAVIF 485
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528497678 486 IDEIDSLLSQRTDGEHDSSRRIKTEFLVQL--DGAATSAEDRILVVGATNRPQEIDEA 541
Cdd:cd19505   91 IPNIHELNVNRSTQNLEEDPKLLLGLLLNYlsRDFEKSSTRNILVIASTHIPQKVDPA 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 418-545 2.52e-06

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: 47.73  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 418 RGPP--KGILLFGPPGTGKTLIgkcIACQSGATFFSISASSLTSkwVGEGEKMVRALfaIARCHQPAVIFIDEIDSLLSQ 495
Cdd:cd19510   18 RGIPyrRGYLLYGPPGTGKSSF---IAALAGELDYDICDLNLSE--VVLTDDRLNHL--LNTAPKQSIILLEDIDAAFES 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528497678 496 RtdgEHDSSRRIKTEF---------LVQLDGAAtSAEDRILVVgATNRPQEIDEAARRR 545
Cdd:cd19510   91 R---EHNKKNPSAYGGlsrvtfsglLNALDGVA-SSEERIVFM-TTNHIERLDPALIRP 144
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 392-553 2.11e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 47.53  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  392 GLEFAK---ATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIA---CQSGA----TFFSISASSLTSKW 461
Cdd:TIGR03922 280 GLERVKrqvAALKSSTAMALARAERGLPVAQTSNHMLFAGPPGTGKTTIARVVAkiyCGLGVlrkpLVREVSRADLIGQY 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  462 VGEGEKMVRALF--AIARchqpaVIFIDEIDSLLsQRTDGEHDSsrrIKTEFLVQLDGAATSAEDRILVVGATNRPQ--- 536
Cdd:TIGR03922 360 IGESEAKTNEIIdsALGG-----VLFLDEAYTLV-ETGYGQKDP---FGLEAIDTLLARMENDRDRLVVIGAGYRKDldk 430

                         170
                  ....*....|....*....
gi 528497678  537 --EIDEAARRRLAKRLYIP 553
Cdd:TIGR03922 431 flEVNEGLRSRFTRVIEFP 449
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 424-551 5.25e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 43.26  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 424 ILLFGPPGTGKTLIGKCIA---CQSGATFFSISASsltskwvgegEKMVRALFAIARCHQPAVIFIDEIDSLLSQRTDge 500
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAeqaLLSDEPVIFISFL----------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQG-- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528497678 501 hDSSRRIKTEFLVQLDGAATSaedRILVVGATNRPQEIDEAARRRLAKRLY 551
Cdd:cd01120   69 -DRSSELLEDLAKLLRAARNT---GITVIATIHSDKFDIDRGGSSNDERLL 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
422-472 6.52e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 45.73  E-value: 6.52e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528497678 422 KGILLFGPPGTGKTLIGKCIACQSGA--TFFSISASSLTSKWVGEGEKMVRAL 472
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEdtPFVAISGSEIYSAELKKTEFLMQAL 117
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 424-490 2.81e-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: 42.97  E-value: 2.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528497678 424 ILLFGPPGTGKTLIGKCIACQSGATFFSISASSLT-SKWVGEG-----EKMVR-ALFAIARChQPAVIFIDEID 490
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvenilLKLLQaADYDVERA-QRGIVYIDEID 125
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
424-490 3.86e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 43.22  E-value: 3.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528497678 424 ILLFGPPGTGKTLIgkciaCQSGATF----FSIS-ASSLT-SKWVGEG-EKMVRAL-----FAIARChQPAVIFIDEID 490
Cdd:PRK05342 111 ILLIGPTGSGKTLL-----AQTLARIldvpFAIAdATTLTeAGYVGEDvENILLKLlqaadYDVEKA-QRGIVYIDEID 183
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
424-492 4.35e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 4.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528497678 424 ILLFGPPGTGKTLIGKCIACQSGATFFSIS----------ASSLTSkwVGEGEkmvralfaiarchqpaVIFIDEIDSL 492
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSgpalekpgdlAAILTN--LEEGD----------------VLFIDEIHRL 114
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 424-546 4.71e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 41.08  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 424 ILLFGPPGTGKTLIGKCIA----CQSG-ATFFSISASSLTSKWVGE----------GEKMvraLFAIARC--HQPAVIFI 486
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAgllkPTSGeILIDGKDIAKLPLEELRRrigyvpqlsgGQRQ---RVALARAllLNPDLLLL 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 487 DEIDSLLSQRtdgehdsSRRIKTEFLVQLdgaatsAEDRILVVGATNRPQEIDEAARRRL 546
Cdd:cd00267  105 DEPTSGLDPA-------SRERLLELLREL------AEEGRTVIIVTHDPELAELAADRVI 151
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
409-546 5.12e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.91  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 409 LRPdIFTGlrGPPKGILLFGPPGTGKTLIGKCIA--------------------CQSGATFFSIsASSLTSKwVGEGE-- 466
Cdd:COG1474   42 LRP-ALRG--ERPSNVLIYGPTGTGKTAVAKYVLeeleeeaeergvdvrvvyvnCRQASTRYRV-LSRILEE-LGSGEdi 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 467 --------KMVRALF-AIARCHQPAVIFIDEIDSLLSQRTDgehdssrriktEFLVQLDGAATSAED-RILVVGATNRPQ 536
Cdd:COG1474  117 pstglstdELFDRLYeALDERDGVLVVVLDEIDYLVDDEGD-----------DLLYQLLRANEELEGaRVGVIGISNDLE 185

                        170
                 ....*....|...
gi 528497678 537 ---EIDEAARRRL 546
Cdd:COG1474  186 fleNLDPRVKSSL 198
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 423-546 1.11e-03

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: 39.58  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  423 GILLFGPPGTGKTLIGKCIACQ-SGATFFSI------SASSLTSKW---VGEGEKMVRALFAIARchQPAVIFIDEIDSL 492
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVqltrdtTEEDLFGRRnidPGGASWVDGPLVRAAR--EGEIAVLDEINRA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  493 LSQRTDGEHD--SSRRIKTEFLVQLDGAatsAEDRILVVGATNRP----QEIDEAARRRL 546
Cdd:pfam07728  79 NPDVLNSLLSllDERRLLLPDGGELVKA---APDGFRLIATMNPLdrglNELSPALRSRF 135
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 422-571 1.17e-03

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 41.53  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  422 KGILLFGPPGTGKTLIGKCIACQSGAT--FFSISASSLTSKWVGEGEKMVRALF-AIA-RCHQPAVIFIDEIDSLLSQRT 497
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEALTQAFRkAIGvRIKEEKEVYEGEVVELEIEEA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  498 DGEHDSSRRIKTEFLV------------------QLDGAATSAEDRILVVGATNRPQEIDEA-ARRR---LAKRLYIPLP 555
Cdd:pfam06068 131 ENPLSGGKTIKGGKITlkttkmektlklgpkiyeQLQKEKVSAGDVIYIDKNTGRVKKLGRSfARATdfdLEATEFVPCP 210

                         170
                  ....*....|....*...
gi 528497678  556 EAEA--RRQIVTNLMSHE 571
Cdd:pfam06068 211 KGEVhkRKEVVQTVTLHD 228
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 418-489 1.71e-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: 39.41  E-value: 1.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528497678  418 RG-PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISASSLTSKwvgegekmvRALFAIARCHQPA-VIFIDEI 489
Cdd:pfam05496  29 RGeALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP---------GDLAAILTNLEPGdVLFIDEI 93
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 409-442 2.62e-03

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 41.16  E-value: 2.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 528497678 409 LRPDiftgLRGPpkgILLF-GPPGTGKTLIGKCIA 442
Cdd:COG0466  346 LKKK----LKGP---ILCLvGPPGVGKTSLGKSIA 373
PRK04195 PRK04195
replication factor C large subunit; Provisional
 384-492 3.27e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 40.29  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678 384 PVAWDDIAGLEFAKATIKEivvWpmlrpdIFTGLRG-PPKGILLFGPPGTGKTLIGKCIACQSGATFFSISAS-----SL 457
Cdd:PRK04195  10 PKTLSDVVGNEKAKEQLRE---W------IESWLKGkPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDV 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528497678 458 TSKWVGEGEKMvRALFAIARchqpAVIFIDEIDSL 492
Cdd:PRK04195  81 IERVAGEAATS-GSLFGARR----KLILLDEVDGI 110
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 424-492 4.40e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.59  E-value: 4.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528497678  424 ILLFGPPGTGKTLIGKCIACQSGATFFSISASSLtskwvgegEKMVRALFAIARCHQPAVIFIDEIDSL 492
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL--------EKPGDLAAILTNLEEGDVLFIDEIHRL 93
AAA_22 pfam13401
AAA domain;
424-492 5.11e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528497678  424 ILLFGPPGTGKTLIGKCIA---CQSGATFFSISASSLTS-----KWVGEG----------EKMVRALF--AIARCHQPAV 483
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVDLPSGTSpkdllRALLRAlglplsgrlsKEELLAALqqLLLALAVAVV 87


                  ....*....
gi 528497678  484 IFIDEIDSL 492
Cdd:pfam13401  88 LIIDEAQHL 96
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 361-435 8.91e-03

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 38.47  E-value: 8.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528497678  361 ERLK--NFEPKIIELIMSEIMDHGppvawDDIAGLEFAKATIKEIVVWPMLRPDIFTGlrgpPKGILLFGPPGTGKT 435
Cdd:TIGR03499 141 ERLLeaGVSEELARELLEKLPEDA-----DAEDAWRWLREALEGMLPVKPEEDPILEQ----GGVIALVGPTGVGKT 208
 
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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