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Conserved domains on  [gi|566559877|ref|NP_001274422|]
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fidgetin-like protein 1 isoform 1 [Homo sapiens]

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; ...
 380-565 4.11e-137

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: 399.36  E-value: 4.11e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 380 EPKMIELIMNEIMDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 459
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 460 ATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRI 539
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 566559877 540 LVVGATNRPQEIDEAARRRLVKRLYI 565
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 ...
 631-671 4.22e-08

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: 50.19  E-value: 4.22e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 566559877  631 ITPDQV--RPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 671
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 590-621 9.18e-06

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: 42.91  E-value: 9.18e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 566559877  590 EEEIEQIVQQSDAFSGADMTQLCREASLGPIR 621
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
 
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; ...
 380-565 4.11e-137

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: 399.36  E-value: 4.11e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 380 EPKMIELIMNEIMDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 459
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 460 ATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRI 539
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 566559877 540 LVVGATNRPQEIDEAARRRLVKRLYI 565
Cdd:cd19525  161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 396-654 2.50e-77

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 250.31  E-value: 2.50e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 396 PPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 473
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 474 WVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD-GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEID 552
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGF--ESRGDVLIIAATNRPDLLD 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 553 EAARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRslqtADIAT 630
Cdd:COG1222  230 PALLRpgRFDRVIEVPLPDEEAREEI-LKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIR----EGRDT 304

                        250       260
                 ....*....|....*....|....
gi 566559877 631 ITPDqvrpiayiDFENAFRTVRPS 654
Cdd:COG1222  305 VTME--------DLEKAIEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 374-671 1.38e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 224.40  E-value: 1.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  374 ERLKNLEPKMIELIMNEImdhgPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIG 451
Cdd:TIGR01243 430 EALKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  452 KCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES-SRRIKTEFLVQLDG 530
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  531 ATTSSEdrILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADM 608
Cdd:TIGR01243 585 IQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEI-FKIHTRSMPLAEDVDLEELAEMTEGYTGADI 661

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566559877  609 TQLCREASLGPIRSLQT--------ADIATITPDQVrpIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 671
Cdd:TIGR01243 662 EAVCREAAMAALRESIGspakekleVGEEEFLKDLK--VEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
cell_div_CdvC NF041006
cell division protein CdvC;
363-670 8.86e-63

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 213.06  E-value: 8.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 363 AGPTEPAHPVDErlKNLEPkmiELIMNEimdhGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTglRGPPKGILLFGP 442
Cdd:NF041006  74 LVPAEPAGPDVE--KESDE---ELVVKE----KPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP--LGWPRGILLYGP 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 443 PGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVAR-----CQQPAVIFIDEIDSLLsqrgdGEHESS 517
Cdd:NF041006 143 PGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKARekskeEGKPAIIFIDEIDALL-----GVYSSE 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 518 R----RIKTEFLVQLDGATTSSED-RILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVINLMSKEQccLSEE- 591
Cdd:NF041006 218 VggevRVRNQFLKEMDGLQDKSENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIK--LENDv 295

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 592 EIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTADIAtitpdQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTF 670
Cdd:NF041006 296 DLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLG-----EPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 437-567 6.20e-53

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: 178.17  E-value: 6.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  437 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES 516
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 566559877  517 SRRIKTEFLVQLDGAtTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPL 567
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 393-652 8.47e-51

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 181.18  E-value: 8.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 393 DHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 470
Cdd:PRK03992 123 IESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV-GiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 471 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGATTSSEDRIlvVGATN 546
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGNVKI--IAATN 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 547 RPQEIDEAARR-----RLVKrlyIPLPEASARKQIV-INL--MSkeqccLSEE-EIEQIVQQSDAFSGADMTQLCREASL 617
Cdd:PRK03992 279 RIDILDPAILRpgrfdRIIE---VPLPDEEGRLEILkIHTrkMN-----LADDvDLEELAELTEGASGADLKAICTEAGM 350

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 566559877 618 GPIRSLQTAdiatITPDqvrpiayiDFENAFRTVR 652
Cdd:PRK03992 351 FAIRDDRTE----VTME--------DFLKAIEKVM 373
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 433-569 1.54e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877   433 PPKGILLFGPPGTGKTLIGKCIASQSGAT---FFSISASSLTS--------------KWVGEGEKMVRALFAVARCQQPA 495
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566559877   496 VIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQldgattsSEDRILVVGATNRPQEIDEAA-RRRLVKRLYIPLPE 569
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALlRRRFDRRIVLLLIL 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 631-671 4.22e-08

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: 50.19  E-value: 4.22e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 566559877  631 ITPDQV--RPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 671
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 590-621 9.18e-06

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: 42.91  E-value: 9.18e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 566559877  590 EEEIEQIVQQSDAFSGADMTQLCREASLGPIR 621
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
 
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; ...
 380-565 4.11e-137

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: 399.36  E-value: 4.11e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 380 EPKMIELIMNEIMDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 459
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 460 ATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRI 539
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 566559877 540 LVVGATNRPQEIDEAARRRLVKRLYI 565
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 ...
 403-565 5.94e-105

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: 315.83  E-value: 5.94e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 403 IAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMV 482
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 483 RALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKR 562
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                 ...
gi 566559877 563 LYI 565
Cdd:cd19509  161 IYI 163
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 402-565 1.86e-86

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: 267.87  E-value: 1.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 481
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 482 VRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVK 561
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                 ....
gi 566559877 562 RLYI 565
Cdd:cd19524  161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 396-654 2.50e-77

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 250.31  E-value: 2.50e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 396 PPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 473
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 474 WVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD-GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEID 552
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGF--ESRGDVLIIAATNRPDLLD 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 553 EAARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRslqtADIAT 630
Cdd:COG1222  230 PALLRpgRFDRVIEVPLPDEEAREEI-LKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIR----EGRDT 304

                        250       260
                 ....*....|....*....|....
gi 566559877 631 ITPDqvrpiayiDFENAFRTVRPS 654
Cdd:COG1222  305 VTME--------DLEKAIEKVKKK 320
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 402-565 1.45e-74

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: 237.09  E-value: 1.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 481
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 482 VRALFAVARCQQPAVIFIDEIDSLLSQRgDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVK 561
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                 ....
gi 566559877 562 RLYI 565
Cdd:cd19523  160 RLLV 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 396-565 6.86e-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: 224.74  E-value: 6.86e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 396 PPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 475
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 476 GEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSeDRILVVGATNRPQEIDEAA 555
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDS-QGVLVLGATNIPWQLDSAI 160

                        170
                 ....*....|
gi 566559877 556 RRRLVKRLYI 565
Cdd:cd19521  161 RRRFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 402-565 3.88e-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: 220.24  E-value: 3.88e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 481
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 482 VRALFAVARCQQPAVIFIDEIDSLLSQRG-DGEHESSRRIKTEFLVQLDGATTSSEDR-----ILVVGATNRPQEIDEAA 555
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGtSEEHEASRRVKSELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 566559877 556 RRRLVKRLYI 565
Cdd:cd19522  161 RRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 400-652 7.61e-68

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: 227.49  E-value: 7.61e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 400 WEDIAGVEFAKATIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEG 478
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 479 EKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGattsSEDRILVVGATNRPQEIDEAARRR 558
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEE----LRSDVVVIAATNRPDLLDPALLRR 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 559 LVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTadiaTITPDqvrp 638
Cdd:COG0464  312 FDEIIFFPLPDAEERLEI-FRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE----PVTTE---- 382

                        250
                 ....*....|....
gi 566559877 639 iayiDFENAFRTVR 652
Cdd:COG0464  383 ----DLLEALERED 392
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 402-565 3.47e-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: 214.98  E-value: 3.47e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIF--TGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE 479
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 480 KMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRL 559
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 566559877 560 VKRLYI 565
Cdd:cd19520  161 PKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 374-671 1.38e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 224.40  E-value: 1.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  374 ERLKNLEPKMIELIMNEImdhgPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIG 451
Cdd:TIGR01243 430 EALKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  452 KCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES-SRRIKTEFLVQLDG 530
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  531 ATTSSEdrILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADM 608
Cdd:TIGR01243 585 IQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEI-FKIHTRSMPLAEDVDLEELAEMTEGYTGADI 661

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566559877  609 TQLCREASLGPIRSLQT--------ADIATITPDQVrpIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 671
Cdd:TIGR01243 662 EAVCREAAMAALRESIGspakekleVGEEEFLKDLK--VEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
cell_div_CdvC NF041006
cell division protein CdvC;
363-670 8.86e-63

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 213.06  E-value: 8.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 363 AGPTEPAHPVDErlKNLEPkmiELIMNEimdhGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTglRGPPKGILLFGP 442
Cdd:NF041006  74 LVPAEPAGPDVE--KESDE---ELVVKE----KPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP--LGWPRGILLYGP 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 443 PGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVAR-----CQQPAVIFIDEIDSLLsqrgdGEHESS 517
Cdd:NF041006 143 PGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKARekskeEGKPAIIFIDEIDALL-----GVYSSE 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 518 R----RIKTEFLVQLDGATTSSED-RILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVINLMSKEQccLSEE- 591
Cdd:NF041006 218 VggevRVRNQFLKEMDGLQDKSENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIK--LENDv 295

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 592 EIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTADIAtitpdQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTF 670
Cdd:NF041006 296 DLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLG-----EPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 366-654 5.34e-54

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: 197.44  E-value: 5.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  366 TEPAHPVdERLKNLEPKMIELIMNEIMDHG-PPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPP 443
Cdd:TIGR01243 143 TQPAGFV-YVTEATEVEIREKPVREEIERKvPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPP 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  444 GTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTE 523
Cdd:TIGR01243 222 GTGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQ 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  524 FLVQLDGatTSSEDRILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSD 601
Cdd:TIGR01243 302 LLTLMDG--LKGRGRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEI-LKVHTRNMPLAEDVDLDKLAEVTH 378

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566559877  602 AFSGADMTQLCREASLGPIR--------SLQTADIATITPDQVRpIAYIDFENAFRTVRPS 654
Cdd:TIGR01243 379 GFVGADLAALAKEAAMAALRrfiregkiNFEAEEIPAEVLKELK-VTMKDFMEALKMVEPS 438
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 409-565 2.36e-53

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: 180.56  E-value: 2.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 409 AKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAV 488
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 489 ARCQQPAVIFIDEIDSLLSQRGD-GEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAARR--RLVKRLYI 565
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSsGESGELRRVLNQLLTELDGVN--SRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 409-565 4.07e-53

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: 179.79  E-value: 4.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 409 AKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALF 486
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIR-PPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 487 AVARCQQPAVIFIDEIDSLLSQRGD-GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKRL 563
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQsDSSGVTDRVVSQLLTELDGI--ESLKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                 ..
gi 566559877 564 YI 565
Cdd:cd19511  158 YV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 437-567 6.20e-53

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: 178.17  E-value: 6.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  437 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES 516
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 566559877  517 SRRIKTEFLVQLDGAtTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPL 567
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 402-557 2.54e-52

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: 177.87  E-value: 2.54e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE 479
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566559877 480 KMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR 557
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM--SSRGKVVVIAATNRPDAIDPALRR 155
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 393-652 8.47e-51

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 181.18  E-value: 8.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 393 DHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 470
Cdd:PRK03992 123 IESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV-GiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 471 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGATTSSEDRIlvVGATN 546
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGNVKI--IAATN 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 547 RPQEIDEAARR-----RLVKrlyIPLPEASARKQIV-INL--MSkeqccLSEE-EIEQIVQQSDAFSGADMTQLCREASL 617
Cdd:PRK03992 279 RIDILDPAILRpgrfdRIIE---VPLPDEEGRLEILkIHTrkMN-----LADDvDLEELAELTEGASGADLKAICTEAGM 350

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 566559877 618 GPIRSLQTAdiatITPDqvrpiayiDFENAFRTVR 652
Cdd:PRK03992 351 FAIRDDRTE----VTME--------DFLKAIEKVM 373
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 396-625 2.49e-49

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: 176.53  E-value: 2.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  396 PPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 474
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGiEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  475 VGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGatTSSEDRILVVGATNRPQE 550
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAELDG--FDPRGNVKVIAATNRPDI 273

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 566559877  551 IDEAARR--RLVKRLYIPLPEASARKQIVINLMSKEQccLSEE-EIEQIVQQSDAFSGADMTQLCREASLGPIRSLQT 625
Cdd:TIGR01242 274 LDPALLRpgRFDRIIEVPLPDFEGRLEILKIHTRKMK--LAEDvDLEAIAKMTEGASGADLKAICTEAGMFAIREERD 349
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 409-565 3.16e-48

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: 166.52  E-value: 3.16e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 409 AKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALF 486
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIR-PPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 487 AVARCQQPAVIFIDEIDSLLSQRG-DGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAARR--RLVKRL 563
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGtTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLI 157


                 ..
gi 566559877 564 YI 565
Cdd:cd19529  158 YI 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 392-651 7.90e-46

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 167.63  E-value: 7.90e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 392 MDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 470
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 471 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSR---RIKTEFLVQLDGATTSSEdrILVVGATNR 547
Cdd:PTZ00454 216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN--VKVIMATNR 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 548 PQEIDEAARR--RLVKRLYIPLPEASARKQIVINLMSKEQccLSEE-EIEQIVQQSDAFSGADMTQLCREASLGPIRSlq 624
Cdd:PTZ00454 294 ADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMN--LSEEvDLEDFVSRPEKISAADIAAICQEAGMQAVRK-- 369

                        250       260
                 ....*....|....*....|....*..
gi 566559877 625 taDIATITPDqvrpiayiDFENAFRTV 651
Cdd:PTZ00454 370 --NRYVILPK--------DFEKGYKTV 386
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 400-557 6.85e-45

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: 157.88  E-value: 6.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 400 WEDIAGVEFAKATIKEIVVWPMLRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 477
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEEL-GiePPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 478 GEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSR---RIKTEFLVQLDGATTSseDRILVVGATNRPQEIDEA 554
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPR--GNIKVIMATNRPDILDPA 158


                 ...
gi 566559877 555 ARR 557
Cdd:cd19502  159 LLR 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 402-557 9.95e-45

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: 157.21  E-value: 9.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK 480
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566559877 481 MVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSedRILVVGATNRPQEIDEAARR 557
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPALRR 155
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
400-615 7.12e-44

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 157.74  E-value: 7.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 400 WEDIAGVEFAKATIKEIVVWPMLRPDiftgLRG----PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 475
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRREN----LRKfglwPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 476 GEGEKMVRALFAVARcQQPAVIFIDEIDSLLSQRGD----GEhesSRRIKTEFLVQLDGATtsseDRILVVGATNRPQEI 551
Cdd:COG1223   77 GETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDqndvGE---VKRVVNALLQELDGLP----SGSVVIAATNHPELL 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566559877 552 DEAARRRLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREA 615
Cdd:COG1223  149 DSALWRRFDEVIEFPLPDKEERKEI-LELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 392-626 1.81e-43

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: 163.61  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  392 MDHGPPVNWEDIAGVEFAKATIKEIVVWpmLR-PDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 469
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDF--LKnPSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  470 LTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDG---EHESSRRIKTEFLVQLDGATTSseDRILVVGATN 546
Cdd:TIGR01241 124 FVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGNDEREQTLNQLLVEMDGFGTN--TGVIVIAATN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  547 RPQEIDEAARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQ 624
Cdd:TIGR01241 202 RPDVLDPALLRpgRFDRQVVVDLPDIKGREEI-LKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNK 280


                  ..
gi 566559877  625 TA 626
Cdd:TIGR01241 281 TE 282
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 398-565 7.17e-43

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: 152.39  E-value: 7.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 398 VNWEDIAGVEFAKATIKEIVVWpMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 476
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 477 EGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGE---HESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 553
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFESNTG--VIVIAATNRPDVLDP 157

                        170
                 ....*....|....
gi 566559877 554 AARR--RLVKRLYI 565
Cdd:cd19501  158 ALLRpgRFDRQVYV 171
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 392-621 7.68e-43

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 160.32  E-value: 7.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 392 MDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 469
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 470 LTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGATTSSEdrILVVGAT 545
Cdd:PTZ00361 253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatsgGEKEIQRTM-LELLNQLDGFDSRGD--VKVIMAT 329

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 546 NRPQEIDEAARR--RLVKRLYIPLPEASARKQIVINLMSKEQccLSEE-EIEQIVQQSDAFSGADMTQLCREASLGPIR 621
Cdd:PTZ00361 330 NRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMT--LAEDvDLEEFIMAKDELSGADIKAICTEAGLLALR 406
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 417-565 1.72e-40

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: 145.32  E-value: 1.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 417 VVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPA 495
Cdd:cd19530   12 ILRPIKRPDIYKALGiDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566559877 496 VIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAARR--RLVKRLYI 565
Cdd:cd19530   92 VIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSN--VFVIAATNRPDIIDPAMLRpgRLDKTLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 410-565 2.99e-38

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: 139.18  E-value: 2.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 410 KATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFA 487
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLkfGMT-PSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 488 VARCQQPAVIFIDEIDSLLSQRG---DGEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAARR--RLVKR 562
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMN--TKKNVFIIGATNRPDIIDPAILRpgRLDQL 158


                 ...
gi 566559877 563 LYI 565
Cdd:cd19528  159 IYI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 402-557 1.66e-37

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: 137.54  E-value: 1.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE 479
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 480 KMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSED--RILVVGATNRPQEIDEAARR 557
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAggPVLVIGATNRPDSLDPALRR 159
ftsH CHL00176
cell division protein; Validated
 398-636 7.82e-37

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 146.35  E-value: 7.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 398 VNWEDIAGVEFAKATIKEIVVWpMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 476
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 477 EGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRG---DGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 553
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGagiGGGNDEREQTLNQLLTEMDGFKGNKG--VIVIAATNRVDILDA 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 554 AARR--RLVKRLYIPLPEASARKQIvINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRslqtADIATI 631
Cdd:CHL00176 337 ALLRpgRFDRQITVSLPDREGRLDI-LKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTAR----RKKATI 411


                 ....*
gi 566559877 632 TPDQV 636
Cdd:CHL00176 412 TMKEI 416
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 410-565 3.18e-36

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: 133.41  E-value: 3.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 410 KATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVA 489
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 490 RCQQPAVIFIDEIDSLLSQRGDGEHESS--RRIKTEFLVQLDGATTSSEDrILVVGATNRPQEIDEAARR--RLVKRLYI 565
Cdd:cd19527   82 RDAKPCVIFFDELDSLAPSRGNSGDSGGvmDRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLYL 160
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
402-647 4.51e-36

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 144.41  E-value: 4.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK 480
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 481 MVRALFAVARCQQPAVIFIDEIDSLLSQRG---DGEHESSRRIKTEFLVQLDGatTSSEDRILVVGATNRPQEIDEAARR 557
Cdd:PRK10733 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglGGGHDEREQTLNQMLVEMDG--FEGNEGIIVIAATNRPDVLDPALLR 309

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 558 --RLVKRLYIPLPEASARKQIVINLMSKEQCClSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQtadiatitpdq 635
Cdd:PRK10733 310 pgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNEAALFAARGNK----------- 377

                        250
                 ....*....|..
gi 566559877 636 vRPIAYIDFENA 647
Cdd:PRK10733 378 -RVVSMVEFEKA 388
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 402-557 2.94e-35

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: 131.09  E-value: 2.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 402 DIAGVEFAKATIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGA-----TFFSISASSLTSKWV 475
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 476 GEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAA 555
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPAL 158


                 ..
gi 566559877 556 RR 557
Cdd:cd19517  159 RR 160
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
391-617 4.98e-34

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 137.48  E-value: 4.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 391 IMDHGPPVNWEDIAGVEFAKATIKEIVvwPMLR-PDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISAS 468
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQEIV--DFLKdPEKFTRLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 469 SLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDG------EHESsrrikT--EFLVQLDGATTSSedRIL 540
Cdd:COG0465  210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdEREQ-----TlnQLLVEMDGFEGNE--GVI 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 541 VVGATNRPqEI-DEAARR--RLVKRLYIPLPEASARKQIvinL---MSKEQccLSEE-EIEQIVQQSDAFSGADMTQLCR 613
Cdd:COG0465  283 VIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAI---LkvhARKKP--LAPDvDLEVIARRTPGFSGADLANLVN 356


                 ....
gi 566559877 614 EASL 617
Cdd:COG0465  357 EAAL 360
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 409-564 5.63e-34

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: 127.16  E-value: 5.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 409 AKATIKEIVVWPMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFA 487
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRlRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 488 VARCQQPAVIFIDEIDSLLSQRGdgeHESS---RRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKR 562
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRG---HDSTgvtDRVVNQLLTQLDGV--EGLDGVYVLAATSRPDLIDPALLRpgRLDKL 155


                 ..
gi 566559877 563 LY 564
Cdd:cd19526  156 VY 157
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 385-577 2.75e-33

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: 134.45  E-value: 2.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  385 ELIMNEImdhgPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIAS---QSG 459
Cdd:TIGR03689 170 DLVLEEV----PDVTYADIGGLGSQIEQIRDAVELPFLHPELYReyGLK-PPKGVLLYGPPGCGKTLIAKAVANslaARI 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  460 AT-------FFSISASSLTSKWVGEGEKMVRALFAVARCQ----QPAVIFIDEIDSLLSQRGDG---EHESSrrIKTEFL 525
Cdd:TIGR03689 245 GAegggksyFLNIKGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGSGvssDVETT--VVPQLL 322

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 566559877  526 VQLDGatTSSEDRILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIV 577
Cdd:TIGR03689 323 AEIDG--VESLDNVIVIGASNREDMIDPAILRpgRLDVKIRIERPDAEAAADIF 374
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 431-567 5.20e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 101.45  E-value: 5.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 431 RGPPKGILLFGPPGTGKTLIGKCIA---SQSGATFFSISASSLTSKWVGEGEK---MVRALFAVARCQQPAVIFIDEIDS 504
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566559877 505 LlsqrgdgehesSRRIKTEFLVQLDGATTSSE--DRILVVGATNRP--QEIDEAARRRLVKRLYIPL 567
Cdd:cd00009   96 L-----------SRGAQNALLRVLETLNDLRIdrENVRVIGATNRPllGDLDRALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 435-557 1.61e-21

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: 92.17  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 435 KGILLFGPPGTGKTLIGKCIASQSGATFFSI-SASSLTSKWVGEGEKMVRALFAVARCQQPA--------VIFIDEIDSL 505
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 566559877 506 LSQRGDGEHESS--RRIKTEFLVQLDGatTSSEDRILVVGATNRPQEIDEAARR 557
Cdd:cd19504  116 CKQRGSMAGSTGvhDTVVNQLLSKIDG--VEQLNNILVIGMTNRKDLIDEALLR 167
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 433-569 1.54e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877   433 PPKGILLFGPPGTGKTLIGKCIASQSGAT---FFSISASSLTS--------------KWVGEGEKMVRALFAVARCQQPA 495
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566559877   496 VIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQldgattsSEDRILVVGATNRPQEIDEAA-RRRLVKRLYIPLPE 569
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALlRRRFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 433-556 5.98e-17

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: 78.56  E-value: 5.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 433 PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLS-QRGD 511
Cdd:cd19507   30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSnADSK 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 566559877 512 GEHESSRRIKTEFLVQLDGATTSsedrILVVGATNR----PQEIDEAAR 556
Cdd:cd19507  110 GDSGTSSRVLGTFLTWLQEKKKP----VFVVATANNvqslPPELLRKGR 154
ycf46 CHL00195
Ycf46; Provisional
 401-647 2.19e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.21  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 401 EDIAGVEFAKAtikeivvWPMLRPDIFT------GLrgP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 473
Cdd:CHL00195 228 SDIGGLDNLKD-------WLKKRSTSFSkqasnyGL--PtPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 474 WVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQ---RGDGehESSRRIKTEFLVQLDGATTSsedrILVVGATNR--- 547
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNsesKGDS--GTTNRVLATFITWLSEKKSP----VFVVATANNidl 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 548 -PQEIdeaARR-RLVKRLYIPLPEASARKQIV-INLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREA---SLGPIR 621
Cdd:CHL00195 373 lPLEI---LRKgRFDEIFFLDLPSLEEREKIFkIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAmyiAFYEKR 449

                        250       260
                 ....*....|....*....|....*.
gi 566559877 622 SLQTADIATITpDQVRPIAYIDFENA 647
Cdd:CHL00195 450 EFTTDDILLAL-KQFIPLAQTEKEQI 474
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 435-552 9.06e-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: 69.48  E-value: 9.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 435 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEG--EKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDG 512
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 566559877 513 EHESS--RRIKTEFLVQLDgaTTSSEDRILVVGATNRPQEID 552
Cdd:cd19506  107 TEKQLdpKRLKKDLPKILK--SLKPEDRVLIVGTTSRPFEAD 146
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 431-559 1.98e-11

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: 62.54  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 431 RGPPKGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVI-FIDEIDSLLSQR 509
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKR 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 566559877 510 G-DGEHESSRRIKTEFLVQldgaTTSSEDRILVVGATNRPQEIDEAARRRL 559
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 ...
 434-544 1.33e-10

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 60.86  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 434 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVG-EGEKMVRALFAvarcqqpAVIFIDEIDSLLSQRGD 511
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 566559877 512 GEHESSRR-IKTEFLVQLDGATTSSE------DRILVVGA 544
Cdd:cd19498  119 SGPDVSREgVQRDLLPIVEGSTVSTKygpvktDHILFIAA 158
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 437-506 1.72e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQSGATFFSISAssltskwVGEGEKMVRALFAVAR----CQQPAVIFIDEI--------DS 504
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARerraYGRRTILFVDEIhrfnkaqqDA 124


                 ..
gi 566559877 505 LL 506
Cdd:COG2256  125 LL 126
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 437-600 2.11e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSltskwvgEGEKMVRALFAVARCQ----QPAVIFIDEI--------DS 504
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEIhrfnkaqqDA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 505 LLSQRGDGehessrriktefLVQLDGATTS-----------SEDRILVVgatnRP---QEIDEAARRRL--VKRLYIPLP 568
Cdd:PRK13342 112 LLPHVEDG------------TITLIGATTEnpsfevnpallSRAQVFEL----KPlseEDIEQLLKRALedKERGLVELD 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 566559877 569 EaSARKQIV----------INLMskEQCCLSEEEI-----EQIVQQS 600
Cdd:PRK13342 176 D-EALDALArlangdarraLNLL--ELAALGVDSItlellEEALQKR 219
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 437-565 1.24e-08

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: 55.53  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQ---------SGATFFSISASSLTSKWVGEGEKMVRALFavARCQQ-----PAVIF--ID 500
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMF--QKIQEliddkDALVFvlID 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 501 EIDSLLSQR----GDGEHESSRRIKTEFLVQLDgaTTSSEDRILVVGATNRPQEIDEAARRRLVKRLYI 565
Cdd:cd19508  133 EVESLAAARsassSGTEPSDAIRVVNAVLTQID--RIKRYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 631-671 4.22e-08

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: 50.19  E-value: 4.22e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 566559877  631 ITPDQV--RPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 671
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 433-554 1.24e-07

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: 51.61  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 433 PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW--------------VGEGEKMVRALFAVARCQQPAVIF 498
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 566559877 499 IDEIDSLLSQRGDGEHESSRRIKTEFLVQL--DGATTSSEDRILVVGATNRPQEIDEA 554
Cdd:cd19505   91 IPNIHELNVNRSTQNLEEDPKLLLGLLLNYlsRDFEKSSTRNILVIASTHIPQKVDPA 148
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 430-511 1.96e-07

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: 51.41  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 430 LRGPPKG-ILLF-GPPGTGKTLIGKCIASQSGATFFSISASSLTSkwvgEGE--------------KMVRALfAVARCQQ 493
Cdd:cd19500   31 LKGSMKGpILCLvGPPGVGKTSLGKSIARALGRKFVRISLGGVRD----EAEirghrrtyvgampgRIIQAL-KKAGTNN 105

                         90
                 ....*....|....*....
gi 566559877 494 PaVIFIDEIDSL-LSQRGD 511
Cdd:cd19500  106 P-VFLLDEIDKIgSSFRGD 123
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 430-577 5.10e-07

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: 51.71  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 430 LRGPpkgILLFGPPGTGKTLIGKCIASQSGATFFSIS------ASSLTSKWV---GEGEKMVR--ALFAVarcqqpaVIF 498
Cdd:COG0714   30 AGGH---LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILGTYIydqQTGEFEFRpgPLFAN-------VLL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 499 IDEIDsllsqRGDgehessrrIKT---------EFLVQLDGATTSSEDRILVVgATNRPQEID------EAARRRLVKRL 563
Cdd:COG0714  100 ADEIN-----RAP--------PKTqsalleameERQVTIPGGTYKLPEPFLVI-ATQNPIEQEgtyplpEAQLDRFLLKL 165

                        170
                 ....*....|....
gi 566559877 564 YIPLPEASARKQIV 577
Cdd:COG0714  166 YIGYPDAEEEREIL 179
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 431-558 9.73e-07

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: 48.89  E-value: 9.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 431 RGPP--KGILLFGPPGTGKTLIgkcIASQSGATFFSISASSLTSkwVGEGEKMVRALFAVArcQQPAVIFIDEIDSLLSQ 508
Cdd:cd19510   18 RGIPyrRGYLLYGPPGTGKSSF---IAALAGELDYDICDLNLSE--VVLTDDRLNHLLNTA--PKQSIILLEDIDAAFES 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 509 RgdgEHESSRRIKTEF---------LVQLDGaTTSSEDRILVVgATNRPQEIDEAARRR 558
Cdd:cd19510   91 R---EHNKKNPSAYGGlsrvtfsglLNALDG-VASSEERIVFM-TTNHIERLDPALIRP 144
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 590-621 9.18e-06

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: 42.91  E-value: 9.18e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 566559877  590 EEEIEQIVQQSDAFSGADMTQLCREASLGPIR 621
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 437-503 1.10e-05

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 47.21  E-value: 1.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-----EKMVR-ALFAVARCQQpAVIFIDEID 503
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvenilLKLLQaADYDVERAQR-GIVYIDEID 125
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
435-485 2.23e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.27  E-value: 2.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 566559877 435 KGILLFGPPGTGKTLIGKCIASQSGA--TFFSISASSLTSKWVGEGEKMVRAL 485
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEdtPFVAISGSEIYSAELKKTEFLMQAL 117
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 403-566 2.46e-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: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  403 IAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQ-SGATFFS------ISASSLTSKWV 475
Cdd:TIGR03922 281 LERVKRQVAALKSSTAMALARAERGLPVAQTSNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQYI 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  476 GEGEKMVRALFAVArcqQPAVIFIDEIDSLLsQRGDGEHESsrrIKTEFLVQLDGATTSSEDRILVVGATNRPQ-----E 550
Cdd:TIGR03922 361 GESEAKTNEIIDSA---LGGVLFLDEAYTLV-ETGYGQKDP---FGLEAIDTLLARMENDRDRLVVIGAGYRKDldkflE 433

                         170
                  ....*....|....*.
gi 566559877  551 IDEAARRRLVKRLYIP 566
Cdd:TIGR03922 434 VNEGLRSRFTRVIEFP 449
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
437-503 4.39e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 46.31  E-value: 4.39e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-EKMVRAL-----FAVARCQQpAVIFIDEID 503
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEDvENILLKLlqaadYDVEKAQR-GIVYIDEID 183
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 436-559 1.44e-04

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: 42.28  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  436 GILLFGPPGTGKTLIGKCIASQ-SGATFFSI------SASSLTSKW-VGEGEKMVRALFAVARCQQPAVIFIDEID---- 503
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVqltrdtTEEDLFGRRnIDPGGASWVDGPLVRAAREGEIAVLDEINranp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566559877  504 -------SLLSQrgdgehessRRIKTEFLVQLDGAttsSEDRILVVGATNRP----QEIDEAARRRL 559
Cdd:pfam07728  81 dvlnsllSLLDE---------RRLLLPDGGELVKA---APDGFRLIATMNPLdrglNELSPALRSRF 135
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
437-505 2.24e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.97  E-value: 2.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQSGATFFSIS----------ASSLTSkwVGEGEkmvralfavarcqqpaVIFIDEIDSL 505
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSgpalekpgdlAAILTN--LEEGD----------------VLFIDEIHRL 114
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 437-564 2.75e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.95  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQ---SGATFFSISASsltskwvgegEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGE 513
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQallSDEPVIFISFL----------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 566559877 514 hesSRRIKTEFLVQLDGATTSSedrILVVGATNRPQEIDEAARRRLVKRLY 564
Cdd:cd01120   71 ---SSELLEDLAKLLRAARNTG---ITVIATIHSDKFDIDRGGSSNDERLL 115
PRK04195 PRK04195
replication factor C large subunit; Provisional
 397-522 3.95e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 43.37  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 397 PVNWEDIAGVEFAKATIKEivvWpmlrpdIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISAS-----SL 470
Cdd:PRK04195  10 PKTLSDVVGNEKAKEQLRE---W------IESWLKGkPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 566559877 471 TSKWVGEGEKMvRALFAVARcqqpAVIFIDEIDSlLSQRGD--GEHESSRRIKT 522
Cdd:PRK04195  81 IERVAGEAATS-GSLFGARR----KLILLDEVDG-IHGNEDrgGARAILELIKK 128
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 437-503 6.23e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 42.73  E-value: 6.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 437 ILLFGPPGTGKTLIGKCIasqsgATF----FSIS-ASSLT-SKWVGEG-EKMVRAL-----FAVARCQQpAVIFIDEID 503
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTL-----ARIldvpFAIAdATTLTeAGYVGEDvENILLKLlqaadYDVEKAER-GIIYIDEID 184
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 437-560 6.40e-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: 40.69  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 437 ILLFGPPGTGKTLIGKCIA----SQSG-ATFFSISASSLTSKWVGE----------GEKMvRALFAVARCQQPAVIFIDE 501
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAgllkPTSGeILIDGKDIAKLPLEELRRrigyvpqlsgGQRQ-RVALARALLLNPDLLLLDE 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 566559877 502 IDSLLSQRgdgehesSRRIKTEFLVQLdgattsSEDRILVVGATNRPQEIDEAARRRLV 560
Cdd:cd00267  107 PTSGLDPA-------SRERLLELLREL------AEEGRTVIIVTHDPELAELAADRVIV 152
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 437-642 8.21e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.90  E-value: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  437 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLtskwvgegEKMVRALFAVARCQQPAVIFIDEIdsllsqrgdgeHES 516
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL--------EKPGDLAAILTNLEEGDVLFIDEI-----------HRL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  517 SRRIKtEFL------VQLD-------GATTSSED--RILVVGATNRPQEIDEAARRR--LVKRL--Yiplpeasarkqiv 577
Cdd:TIGR00635  94 SPAVE-ELLypamedFRLDivigkgpSARSVRLDlpPFTLVGATTRAGMLTSPLRDRfgIILRLefY------------- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 566559877  578 inlmskeqcclSEEEIEQIVQQSDAFSGADMTQlcREASLGPIRSLQTADIATITPDQVRPIAYI 642
Cdd:TIGR00635 160 -----------TVEELAEIVSRSAGLLNVEIEP--EAALEIARRSRGTPRIANRLLRRVRDFAQV 211
PRK13341 PRK13341
AAA family ATPase;
438-533 1.47e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.96  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877 438 LLFGPPGTGKTLIGKCIASQSGATFFSISAssltskwVGEGEKMVRALFAVARCQ-----QPAVIFIDEI--------DS 504
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERlerhgKRTILFIDEVhrfnkaqqDA 128

                         90       100       110
                 ....*....|....*....|....*....|.
gi 566559877 505 LLS--QRGDgehessrrikteflVQLDGATT 533
Cdd:PRK13341 129 LLPwvENGT--------------ITLIGATT 145
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 434-503 2.17e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 39.49  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  434 PKGILLF-GPPGTGKTLIGKCIASQSG---ATFFSISASSLT-----SKWVGEGEKMVRA-----LFAVARCQQPAVIFI 499
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMeehsvSRLIGAPPGYVGYeeggqLTEAVRRKPYSIVLI 81


                  ....
gi 566559877  500 DEID 503
Cdd:pfam07724  82 DEIE 85
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 431-502 2.46e-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: 39.02  E-value: 2.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 566559877  431 RG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKwvgegekmvRALFAVARCQQPA-VIFIDEI 502
Cdd:pfam05496  29 RGeALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP---------GDLAAILTNLEPGdVLFIDEI 93
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 422-455 2.69e-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: 2.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 566559877 422 LRPDiftgLRGPpkgILLF-GPPGTGKTLIGKCIA 455
Cdd:COG0466  346 LKKK----LKGP---ILCLvGPPGVGKTSLGKSIA 373
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 435-485 3.21e-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: 40.37  E-value: 3.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 566559877  435 KGILLFGPPGTGKTLIGKCIASQSGAT--FFSISASSLTSKWVGEGEKMVRAL 485
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEALTQAF 103
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 437-502 4.35e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.68  E-value: 4.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 566559877 437 ILLFGPPGTGKTLIGKCIASQSGATFFSIS----------ASSLTSkwVGEGEkmvralfavarcqqpaVIFIDEI 502
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSgpaiekpgdlAAILTN--LEEGD----------------VLFIDEI 114
AAA_22 pfam13401
AAA domain;
437-505 7.30e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566559877  437 ILLFGPPGTGKTLIGKCIASQ---SGATFFSISASSLTS-----KWVGEG----------EKMVRALF--AVARCQQPAV 496
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpeVRDSVVFVDLPSGTSpkdllRALLRAlglplsgrlsKEELLAALqqLLLALAVAVV 87


                  ....*....
gi 566559877  497 IFIDEIDSL 505
Cdd:pfam13401  88 LIIDEAQHL 96
 
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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