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Conserved domains on  [gi|19112067|ref|NP_595275|]
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AAA family ATPase [Schizosaccharomyces pombe]

Protein Classification

ATP-binding protein( domain architecture ID 11421745)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain

EC:  3.6.1.-
Gene Ontology:  GO:0016887|GO:0005524
PubMed:  11473577

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 381-552 2.01e-85

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: 264.98  E-value: 2.01e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLV 460
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 461 RALFEVAKRQTCSVIFVDEIDSILSARNDSgnEHESSRRLKTEFLIQWSSLTNAAPDkqtghspRVLVLAATNLPWCIDE 540
Cdd:cd19509  81 RALFALARELQPSIIFIDEIDSLLSERGSG--EHEASRRVKTEFLVQMDGVLNKPED-------RVLVLGATNRPWELDE 151

                       170
                ....*....|..
gi 19112067 541 AARRRFVKRTYI 552
Cdd:cd19509 152 AFLRRFEKRIYI 163
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 623-657 3.13e-10

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: 55.97  E-value: 3.13e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19112067   623 PPISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFG 657
Cdd:pfam09336  27 PPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 577-614 1.85e-08

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: 50.61  E-value: 1.85e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 19112067   577 EEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDAL 614
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 221-359 5.07e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.28  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   221 NSTTFPTAMKSQSTTKPTLSNS-VSSPSiQVSNNQNANNSTPL------SFHAPIPPLHVPavplTSASHSSSDGKSRKH 293
Cdd:pfam05109 450 SSTHVPTNLTAPASTGPTVSTAdVTSPT-PAGTTSGASPVTPSpsprdnGTESKAPDMTSP----TSAVTTPTPNATSPT 524

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112067   294 PSPYKPYLNSSHDTLGsSTRPSSADTAGSP-ATSPPATADSKTIVSKTISASTTQQTEPLQQTTPSS 359
Cdd:pfam05109 525 PAVTTPTPNATSPTLG-KTSPTSAVTTPTPnATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNA 590
 
Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 381-552 2.01e-85

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: 264.98  E-value: 2.01e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLV 460
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 461 RALFEVAKRQTCSVIFVDEIDSILSARNDSgnEHESSRRLKTEFLIQWSSLTNAAPDkqtghspRVLVLAATNLPWCIDE 540
Cdd:cd19509  81 RALFALARELQPSIIFIDEIDSLLSERGSG--EHEASRRVKTEFLVQMDGVLNKPED-------RVLVLGATNRPWELDE 151

                       170
                ....*....|..
gi 19112067 541 AARRRFVKRTYI 552
Cdd:cd19509 152 AFLRRFEKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 337-646 1.56e-80

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 258.01  E-value: 1.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 337 VSKTISASTTQQTEPLQQTTPSSDFEYAIMNEIISNHEP-VYWSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLrEPVQ 413
Cdd:COG1222  35 PVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPdVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGI-EPPK 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 414 GMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNE 493
Cdd:COG1222 114 GVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTS 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 494 HEsSRRLKTEFLIQ---WSSLTNaapdkqtghsprVLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLSHLL 568
Cdd:COG1222 194 GE-VQRTVNQLLAEldgFESRGD------------VLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHL 260

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112067 569 HNqVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDAllttsaemippISLNHFKASLRTIRPSVSQEGI 646
Cdd:COG1222 261 RD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLEKAIEKVKKKTETATN 326
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 360-657 6.97e-58

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: 208.22  E-value: 6.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   360 DFEYAIMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAK 437
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESG 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   438 ATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSR---RLKTEfliqwssLTNA 514
Cdd:TIGR01243 513 ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRivnQLLTE-------MDGI 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   515 APDKQtghsprVLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLShlLHNQVHCLTEE-DLEELVNLTEGYS 591
Cdd:TIGR01243 586 QELSN------VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLAEDvDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112067   592 GSDITALAKDAAMGPLRNLGDALLTTSAEMIPP-------ISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFG 657
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEeflkdlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 347-612 9.44e-57

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 196.98  E-value: 9.44e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  347 QQTEPLQQTTPSSDFEYAIMNEIIsnHEP-VYWSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLrEPVQGMLLFGPPGT 423
Cdd:PRK03992 100 QQSLAIVEVLPSEKDPRVQAMEVI--ESPnVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGT 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  424 GKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGN--EHESSRRLk 501
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTsgDREVQRTL- 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  502 TEFLiqwssltnAAPDkqtGHSPR--VLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLshllhnQVHC--- 574
Cdd:PRK03992 256 MQLL--------AEMD---GFDPRgnVKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEIL------KIHTrkm 318

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 19112067  575 -LTEE-DLEELVNLTEGYSGSDITALAKDAAMGPLRNLGD 612
Cdd:PRK03992 319 nLADDvDLEELAELTEGASGADLKAICTEAGMFAIRDDRT 358
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 415-554 6.01e-50

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 170.08  E-value: 6.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   415 MLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGneH 494
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG--D 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   495 ESSRRLKTEFLIQWssltnaapDKQTGHSPRVLVLAATNLPWCIDEAARRRFVKRTYIPL 554
Cdd:pfam00004  79 SESRRVVNQLLTEL--------DGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 413-556 1.72e-15

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: 73.95  E-value: 1.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067    413 QGMLLFGPPGTGKTMLARAVATEAKAT---FFSISASSLTS--------------KYLGDSEKLVRALFEVAKRQTCSVI 475
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDVL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067    476 FVDEIDSILSArndsgnehessrrlKTEFLIQWSSLTNAapDKQTGHSPRVLVLAATNLPWCIDEAA-RRRFVKRTYIPL 554
Cdd:smart00382  83 ILDEITSLLDA--------------EQEALLLLLEELRL--LLLLKSEKNLTVILTTNDEKDLGPALlRRRFDRRIVLLL 146


                   ..
gi 19112067    555 PE 556
Cdd:smart00382 147 IL 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 623-657 3.13e-10

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: 55.97  E-value: 3.13e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19112067   623 PPISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFG 657
Cdd:pfam09336  27 PPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 577-614 1.85e-08

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: 50.61  E-value: 1.85e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 19112067   577 EEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDAL 614
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 221-359 5.07e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.28  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   221 NSTTFPTAMKSQSTTKPTLSNS-VSSPSiQVSNNQNANNSTPL------SFHAPIPPLHVPavplTSASHSSSDGKSRKH 293
Cdd:pfam05109 450 SSTHVPTNLTAPASTGPTVSTAdVTSPT-PAGTTSGASPVTPSpsprdnGTESKAPDMTSP----TSAVTTPTPNATSPT 524

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112067   294 PSPYKPYLNSSHDTLGsSTRPSSADTAGSP-ATSPPATADSKTIVSKTISASTTQQTEPLQQTTPSS 359
Cdd:pfam05109 525 PAVTTPTPNATSPTLG-KTSPTSAVTTPTPnATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNA 590
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 416-442 8.13e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.22  E-value: 8.13e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 19112067  416 LLFGPPGTGKTMLARAVATEA-----KATFFS 442
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAAcrqgyRVRFTT 125
 
Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 381-552 2.01e-85

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: 264.98  E-value: 2.01e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLV 460
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 461 RALFEVAKRQTCSVIFVDEIDSILSARNDSgnEHESSRRLKTEFLIQWSSLTNAAPDkqtghspRVLVLAATNLPWCIDE 540
Cdd:cd19509  81 RALFALARELQPSIIFIDEIDSLLSERGSG--EHEASRRVKTEFLVQMDGVLNKPED-------RVLVLGATNRPWELDE 151

                       170
                ....*....|..
gi 19112067 541 AARRRFVKRTYI 552
Cdd:cd19509 152 AFLRRFEKRIYI 163
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 365-552 3.46e-81

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: 254.91  E-value: 3.46e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 365 IMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSIS 444
Cdd:cd19525   8 IMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSIS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 445 ASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSgnEHESSRRLKTEFLIQWSSLTNAAPDkqtghsp 524
Cdd:cd19525  88 ASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG--EHESSRRIKTEFLVQLDGATTSSED------- 158

                       170       180
                ....*....|....*....|....*...
gi 19112067 525 RVLVLAATNLPWCIDEAARRRFVKRTYI 552
Cdd:cd19525 159 RILVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 337-646 1.56e-80

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 258.01  E-value: 1.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 337 VSKTISASTTQQTEPLQQTTPSSDFEYAIMNEIISNHEP-VYWSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLrEPVQ 413
Cdd:COG1222  35 PVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPdVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGI-EPPK 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 414 GMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNE 493
Cdd:COG1222 114 GVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTS 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 494 HEsSRRLKTEFLIQ---WSSLTNaapdkqtghsprVLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLSHLL 568
Cdd:COG1222 194 GE-VQRTVNQLLAEldgFESRGD------------VLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHL 260

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112067 569 HNqVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDAllttsaemippISLNHFKASLRTIRPSVSQEGI 646
Cdd:COG1222 261 RD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLEKAIEKVKKKTETATN 326
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 380-552 2.22e-72

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: 230.89  E-value: 2.22e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKL 459
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 460 VRALFEVAKRQTCSVIFVDEIDSILSARNDsgNEHESSRRLKTEFLIQWSSLtnaapdkQTGHSPRVLVLAATNLPWCID 539
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSE--GEHEASRRLKTEFLIEFDGV-------QSNGDDRVLVMGATNRPQELD 151

                       170
                ....*....|...
gi 19112067 540 EAARRRFVKRTYI 552
Cdd:cd19524 152 DAVLRRFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 376-552 7.25e-72

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: 229.75  E-value: 7.25e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 376 VYWSDIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGD 455
Cdd:cd19521   4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 456 SEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDsgNEHESSRRLKTEFLIQWSSLTNaapdkqtgHSPRVLVLAATNLP 535
Cdd:cd19521  84 SEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE--GESEASRRIKTELLVQMNGVGN--------DSQGVLVLGATNIP 153

                       170
                ....*....|....*..
gi 19112067 536 WCIDEAARRRFVKRTYI 552
Cdd:cd19521 154 WQLDSAIRRRFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 380-552 4.14e-71

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: 227.95  E-value: 4.14e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKL 459
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 460 VRALFEVAKRQTCSVIFVDEIDSILSARNDSGnEHESSRRLKTEFLIQWSSLTNAAPDKqtGHSPRVLVLAATNLPWCID 539
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSE-EHEASRRVKSELLVQMDGVGGASEND--DPSKMVMVLAATNFPWDID 157

                       170
                ....*....|...
gi 19112067 540 EAARRRFVKRTYI 552
Cdd:cd19522 158 EALRRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 378-638 1.85e-64

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: 218.24  E-value: 1.85e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 378 WSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLREPVqGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGD 455
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALPLKRPELREeyGLPPPR-GLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 456 SEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHesSRRLKTEFLiQWSSltnaapdkqtGHSPRVLVLAATNLP 535
Cdd:COG0464 235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGV--GRRVVNTLL-TEME----------ELRSDVVVIAATNRP 301

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 536 WCIDEAARRRFVKRTYIPLPEKETRYKHLSHLLHnQVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDall 615
Cdd:COG0464 302 DLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLR-KRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE--- 377

                       250       260
                ....*....|....*....|...
gi 19112067 616 ttsaemipPISLNHFKASLRTIR 638
Cdd:COG0464 378 --------PVTTEDLLEALERED 392
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 360-657 6.97e-58

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: 208.22  E-value: 6.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   360 DFEYAIMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAK 437
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESG 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   438 ATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSR---RLKTEfliqwssLTNA 514
Cdd:TIGR01243 513 ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRivnQLLTE-------MDGI 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   515 APDKQtghsprVLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLShlLHNQVHCLTEE-DLEELVNLTEGYS 591
Cdd:TIGR01243 586 QELSN------VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLAEDvDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112067   592 GSDITALAKDAAMGPLRNLGDALLTTSAEMIPP-------ISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFG 657
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEeflkdlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 347-612 9.44e-57

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 196.98  E-value: 9.44e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  347 QQTEPLQQTTPSSDFEYAIMNEIIsnHEP-VYWSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLrEPVQGMLLFGPPGT 423
Cdd:PRK03992 100 QQSLAIVEVLPSEKDPRVQAMEVI--ESPnVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGT 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  424 GKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGN--EHESSRRLk 501
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTsgDREVQRTL- 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  502 TEFLiqwssltnAAPDkqtGHSPR--VLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLshllhnQVHC--- 574
Cdd:PRK03992 256 MQLL--------AEMD---GFDPRgnVKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEIL------KIHTrkm 318

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 19112067  575 -LTEE-DLEELVNLTEGYSGSDITALAKDAAMGPLRNLGD 612
Cdd:PRK03992 319 nLADDvDLEELAELTEGASGADLKAICTEAGMFAIRDDRT 358
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 380-552 2.37e-56

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: 188.40  E-value: 2.37e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQ--GLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSE 457
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDnsRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 458 KLVRALFEVAKRQTCSVIFVDEIDSILsaRNDSGNEHESSRRLKTEFLIQWSSLTnaapdkqTGHSPRVLVLAATNLPWC 537
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFL--RQRSSTDHEATAMMKAEFMSLWDGLS-------TDGNCRVIVMGATNRPQD 151

                       170
                ....*....|....*
gi 19112067 538 IDEAARRRFVKRTYI 552
Cdd:cd19520 152 LDEAILRRMPKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 321-644 4.13e-53

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: 194.74  E-value: 4.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   321 GSPATSPPATADSKTIVSKTISASTTQQTEplqqTTPSSDFEYAIMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFL 400
Cdd:TIGR01243 124 GETVIVPVLEGALPFVVVSTQPAGFVYVTE----ATEVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   401 RPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDE 479
Cdd:TIGR01243 200 HPELFEHLGiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDE 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   480 IDSILSARNDSGNEHEssRRLKTEFLIQWSSLtnaapdKQTGhspRVLVLAATNLPWCIDEAARR--RFVKRTYIPLPEK 557
Cdd:TIGR01243 280 IDAIAPKREEVTGEVE--KRVVAQLLTLMDGL------KGRG---RVIVIGATNRPDALDPALRRpgRFDREIVIRVPDK 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   558 ETRYKHLShlLHNQVHCLTEE-DLEELVNLTEGYSGSDITALAKDAAMGPLRN-LGDALLTTSAEMIP-------PISLN 628
Cdd:TIGR01243 349 RARKEILK--VHTRNMPLAEDvDLDKLAEVTHGFVGADLAALAKEAAMAALRRfIREGKINFEAEEIPaevlkelKVTMK 426

                         330
                  ....*....|....*.
gi 19112067   629 HFKASLRTIRPSVSQE 644
Cdd:TIGR01243 427 DFMEALKMVEPSAIRE 442
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 415-554 6.01e-50

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 170.08  E-value: 6.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   415 MLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGneH 494
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG--D 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   495 ESSRRLKTEFLIQWssltnaapDKQTGHSPRVLVLAATNLPWCIDEAARRRFVKRTYIPL 554
Cdd:pfam00004  79 SESRRVVNQLLTEL--------DGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 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 ...
 380-552 3.05e-49

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: 169.39  E-value: 3.05e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQ--GLRePVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSE 457
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 458 KLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHEssRRLKTEFLIQWSSLTNAapdkqtghsPRVLVLAATNLPWC 537
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVE--RRVVAQLLTLMDGMSSR---------GKVVVIAATNRPDA 148

                       170
                ....*....|....*..
gi 19112067 538 IDEAARR--RFVKRTYI 552
Cdd:cd19503 149 IDPALRRpgRFDREVEI 165
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 380-552 6.45e-45

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: 157.74  E-value: 6.45e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKL 459
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 460 VRALFEVAKRQTCSVIFVDEIDSILSARNDsgnEHESSRRLKTEFLIQWSSLTNAAPDKqtghsprVLVLAATNLPWCID 539
Cdd:cd19523  81 LQASFLAARCRQPSVLFISDLDALLSSQDD---EASPVGRLQVELLAQLDGVLGSGEDG-------VLVVCTTSKPEEID 150

                       170
                ....*....|...
gi 19112067 540 EAARRRFVKRTYI 552
Cdd:cd19523 151 ESLRRYFSKRLLV 163
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 387-546 7.55e-44

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: 154.36  E-value: 7.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 387 AKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEV 466
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 467 AKRQTCSVIFVDEIDSILSARnDSGNEHESSRRLKTEFLIQWSSLTnaapdkqtgHSPRVLVLAATNLPWCIDEAARR-- 544
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKR-DSSGESGELRRVLNQLLTELDGVN---------SRSKVLVIAATNRPDLLDPALLRpg 150


                ..
gi 19112067 545 RF 546
Cdd:cd19481 151 RF 152
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
378-602 9.33e-44

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 157.35  E-value: 9.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 378 WSDIAGLDDAKNSLKEAVIYpFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDS 456
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGlWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 457 EKLVRALFEVAKRQTCsVIFVDEIDSILSARNDSgNEHESSRRLKTEFLIQWSSLTNaapdkqtghspRVLVLAATNLPW 536
Cdd:COG1223  80 ARNLRKLFDFARRAPC-VIFFDEFDAIAKDRGDQ-NDVGEVKRVVNALLQELDGLPS-----------GSVVIAATNHPE 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112067 537 CIDEAARRRFVKRTYIPLPEKETRYKHLSHLLhNQVHCLTEEDLEELVNLTEGYSGSDITALAKDA 602
Cdd:COG1223 147 LLDSALWRRFDEVIEFPLPDKEERKEILELNL-KKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 378-546 3.12e-42

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: 150.57  E-value: 3.12e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 378 WSDIAGLDDAKNSLKEAVIYPFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDS 456
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 457 EKLVRALFEVAKRQTCSVIFVDEIDSILSARNDS--GNEHESSRRLkTEFLIQWSsltnaapdkqtGHSPR--VLVLAAT 532
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSgtGGDREVQRTM-LELLNQLD-----------GFDPRgnIKVIMAT 149

                       170
                ....*....|....*.
gi 19112067 533 NLPWCIDEAARR--RF 546
Cdd:cd19502 150 NRPDILDPALLRpgRF 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 387-552 3.56e-40

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: 144.35  E-value: 3.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 387 AKNSLKEAVIYPFLRPELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALF 464
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 465 EVAKRQTCSVIFVDEIDSILSARNDSGNEHESSRRLktefliqwSSLTNaapdKQTGHSPR--VLVLAATNLPWCIDEAA 542
Cdd:cd19511  80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVV--------SQLLT----ELDGIESLkgVVVIAATNRPDMIDPAL 147

                       170
                ....*....|..
gi 19112067 543 RR--RFVKRTYI 552
Cdd:cd19511 148 LRpgRLDKLIYV 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 380-553 6.54e-40

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: 143.73  E-value: 6.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEK 458
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 459 LVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHEssRRLKTEFLIQWSSLtnaapdKQTGHsprVLVLAATNLPWCI 538
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVE--RRIVSQLLTLMDGL------KQRAH---VIVMAATNRPNSI 149

                       170
                ....*....|....*..
gi 19112067 539 DEAARR--RFVKRTYIP 553
Cdd:cd19519 150 DPALRRfgRFDREIDIG 166
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 378-608 1.09e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 151.46  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  378 WSDIAGLDDAKNSLKEAVIYPFLRPELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGD 455
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  456 SEKLVRALFEVAKRQTCSVIFVDEIDSILSARND--SGNEHESSRRLkTEFLIQWSsltnaapdkqtGHSPR--VLVLAA 531
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatSGGEKEIQRTM-LELLNQLD-----------GFDSRgdVKVIMA 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  532 TNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLShlLHNQVHCLTEE-DLEELVNLTEGYSGSDITALAKDAAMGPLR 608
Cdd:PTZ00361 329 TNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFE--IHTSKMTLAEDvDLEEFIMAKDELSGADIKAICTEAGLLALR 406
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 380-546 1.03e-38

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: 140.62  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEK 458
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGvEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 459 LVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHEssRRLKTEFLIQWSSLTNAAPDKQtghspRVLVLAATNLPWCI 538
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREME--RRIVSQLLTCMDELNNEKTAGG-----PVLVIGATNRPDSL 153

                       170
                ....*....|
gi 19112067 539 DEAARR--RF 546
Cdd:cd19518 154 DPALRRagRF 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 357-608 2.15e-38

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 146.83  E-value: 2.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  357 PSSDFEYAIMNeiISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATE 435
Cdd:PTZ00454 125 PEADSSIQLLQ--MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHH 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  436 AKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARND--SGNEHESSRRLkTEFLIQWSSLtn 513
Cdd:PTZ00454 203 TTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDaqTGADREVQRIL-LELLNQMDGF-- 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  514 aapDKQTGhsprVLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKetRYKHLSHLLHNQVHCLTEE-DLEELVNLTEGY 590
Cdd:PTZ00454 280 ---DQTTN----VKVIMATNRADTLDPALLRpgRLDRKIEFPLPDR--RQKRLIFQTITSKMNLSEEvDLEDFVSRPEKI 350

                        250
                 ....*....|....*...
gi 19112067  591 SGSDITALAKDAAMGPLR 608
Cdd:PTZ00454 351 SAADIAAICQEAGMQAVR 368
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 387-552 3.14e-37

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: 136.09  E-value: 3.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 387 AKNSLKEAVIYPFLRPELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALF 464
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 465 EVAKRQTCSVIFVDEIDSILSARNDSGNEHeSSRRLKTEFLIQWSSLTNAApdkqtghspRVLVLAATNLPWCIDEAARR 544
Cdd:cd19529  80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSG-VTERVVNQLLTELDGLEEMN---------GVVVIAATNRPDIIDPALLR 149

                       170
                ....*....|
gi 19112067 545 --RFVKRTYI 552
Cdd:cd19529 150 agRFDRLIYI 159
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 376-552 1.09e-34

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: 129.66  E-value: 1.09e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 376 VYWSDIAGLDDAKNSLKEAViyPFLR-PELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKY 452
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVV--EFLKnPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 453 LGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARND-SGNEHESSRRLKTEFLIQWSSLTNaapdkqtghSPRVLVLAA 531
Cdd:cd19501  78 VGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAgLGGGHDEREQTLNQLLVEMDGFES---------NTGVIVIAA 148

                       170       180
                ....*....|....*....|...
gi 19112067 532 TNLPWCIDEAARR--RFVKRTYI 552
Cdd:cd19501 149 TNRPDVLDPALLRpgRFDRQVYV 171
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 384-552 2.76e-32

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: 122.21  E-value: 2.76e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 384 LDDAKNSLKEAVIYPFLRPELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVR 461
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 462 ALFEVAKRQTCSVIFVDEIDSILSARNDSGNehESSRRLKTEFLIQWSSLTnaapDKQtghspRVLVLAATNLPWCIDEA 541
Cdd:cd19530  80 QVFQRARASAPCVIFFDEVDALVPKRGDGGS--WASERVVNQLLTEMDGLE----ERS-----NVFVIAATNRPDIIDPA 148

                       170
                ....*....|...
gi 19112067 542 ARR--RFVKRTYI 552
Cdd:cd19530 149 MLRpgRLDKTLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 388-552 5.45e-32

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: 121.46  E-value: 5.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 388 KNSLKEAVIYPFLRPELFQ--GLrEPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFE 465
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLkfGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 466 VAKRQTCSVIFVDEIDSILSARNDS-GNEHESSRRLKTEFLIQWSSLTNaapdKQTghsprVLVLAATNLPWCIDEAARR 544
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNiGDAGGAADRVINQILTEMDGMNT----KKN-----VFIIGATNRPDIIDPAILR 151

                       170
                ....*....|
gi 19112067 545 --RFVKRTYI 552
Cdd:cd19528 152 pgRLDQLIYI 161
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
379-603 1.60e-30

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 126.69  E-value: 1.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 379 SDIAGLDDAKNSLKEAViyPFLR-PELFQGL--REPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKY--L 453
Cdd:COG0465 142 DDVAGVDEAKEELQEIV--DFLKdPEKFTRLgaKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFvgV 218

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 454 GDSEklVRALFEVAKRQTCSVIFVDEIDSILSAR---NDSGN-EHEssrrlktefliqwssltnaapdkQT--------- 520
Cdd:COG0465 219 GASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGHdERE-----------------------QTlnqllvemd 273

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 521 GHSPR--VLVLAATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLshllhnQVHC----LTEE-DLEELVNLTEGYS 591
Cdd:COG0465 274 GFEGNegVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAIL------KVHArkkpLAPDvDLEVIARRTPGFS 347

                       250
                ....*....|..
gi 19112067 592 GSDITALAKDAA 603
Cdd:COG0465 348 GADLANLVNEAA 359
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
378-604 3.66e-30

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 126.30  E-value: 3.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  378 WSDIAGLDDAKNSLKEAVIYpfLR-PELFQGLREPV-QGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGD 455
Cdd:PRK10733 151 FADVAGCDEAKEEVAELVEY--LRePSRFQKLGGKIpKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  456 SEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDS-GNEHESSRRLKTEFLIQWSSLTNaapdkqtghSPRVLVLAATNL 534
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlGGGHDEREQTLNQMLVEMDGFEG---------NEGIIVIAATNR 299

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112067  535 PWCIDEAARR--RFVKRTYIPLPEKETRYKHLS-HLlhNQVHCLTEEDLEELVNLTEGYSGSDITALAKDAAM 604
Cdd:PRK10733 300 PDVLDPALLRpgRFDRQVVVGLPDVRGREQILKvHM--RRVPLAPDIDAAIIARGTPGFSGADLANLVNEAAL 370
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 380-551 9.75e-30

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: 115.68  E-value: 9.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAVIYPFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEA-----KATFFSISASSLTSKYL 453
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 454 GDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSrrLKTEFLIQWSSLTNAApdkqtghspRVLVLAATN 533
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS--IVSTLLALMDGLDNRG---------QVVVIGATN 149

                       170       180
                ....*....|....*....|
gi 19112067 534 LPWCIDEAARR--RFVKRTY 551
Cdd:cd19517 150 RPDALDPALRRpgRFDREFY 169
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 388-552 4.04e-29

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: 113.38  E-value: 4.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 388 KNSLKEAVIYPFLRPELF-QGLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEV 466
Cdd:cd19527   2 KKEILDTIQLPLEHPELFsSGLRKR-SGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 467 AKRQTCSVIFVDEIDSILSARNDSGNEHESSRRLKTEFLIQWSSLTNAAPDkqtghsprVLVLAATNLPWCIDEAARR-- 544
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDRVVSQLLAELDGMSSSGQD--------VFVIGATNRPDLLDPALLRpg 152


                ....*...
gi 19112067 545 RFVKRTYI 552
Cdd:cd19527 153 RFDKLLYL 160
ftsH CHL00176
cell division protein; Validated
 376-634 1.23e-26

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 115.15  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  376 VYWSDIAGLDDAKNSLKEAVIypFLR-PELFQ--GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKY 452
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVS--FLKkPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  453 LGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSAR--NDSGNEHESSRRLkTEFLIQWSSLtnaapDKQTGhsprVLVLA 530
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgaGIGGGNDEREQTL-NQLLTEMDGF-----KGNKG----VIVIA 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  531 ATNLPWCIDEAARR--RFVKRTYIPLPEKETRYKHLS-HL----LHNQVhclteeDLEELVNLTEGYSGSDitalakdaa 603
Cdd:CHL00176 327 ATNRVDILDAALLRpgRFDRQITVSLPDREGRLDILKvHArnkkLSPDV------SLELIARRTPGFSGAD--------- 391

                        250       260       270
                 ....*....|....*....|....*....|...
gi 19112067  604 mgpLRNLGD--ALLTTSAEmIPPISLNHFKASL 634
Cdd:CHL00176 392 ---LANLLNeaAILTARRK-KATITMKEIDTAI 420
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 387-551 6.93e-24

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: 98.27  E-value: 6.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 387 AKNSLKEAVIYPFLRPELFQGLREPVQ-GMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFE 465
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 466 VAKRQTCSVIFVDEIDSILSARNdsgneHESS---RRLKTEFLIQWSSLtnaapDKQTGhsprVLVLAATNLPWCIDEAA 542
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRG-----HDSTgvtDRVVNQLLTQLDGV-----EGLDG----VYVLAATSRPDLIDPAL 146

                       170
                ....*....|.
gi 19112067 543 RR--RFVKRTY 551
Cdd:cd19526 147 LRpgRLDKLVY 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 382-554 1.25e-18

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: 82.96  E-value: 1.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 382 AGLDDAKNSLKEAViypflrpelfqgLREPVQGMLLFGPPGTGKTMLARAVATEA---KATFFSISASSLTSKYLGDSEK 458
Cdd:cd00009   1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 459 ---LVRALFEVAKRQTCSVIFVDEIDSIlsarndsgnehesSRRLKTEFLIQWSSLTNAAPDKQtghspRVLVLAATNLP 535
Cdd:cd00009  69 ghfLVRLLFELAEKAKPGVLFIDEIDSL-------------SRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRP 130

                       170       180
                ....*....|....*....|.
gi 19112067 536 WC--IDEAARRRFVKRTYIPL 554
Cdd:cd00009 131 LLgdLDRALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 413-556 1.72e-15

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: 73.95  E-value: 1.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067    413 QGMLLFGPPGTGKTMLARAVATEAKAT---FFSISASSLTS--------------KYLGDSEKLVRALFEVAKRQTCSVI 475
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDVL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067    476 FVDEIDSILSArndsgnehessrrlKTEFLIQWSSLTNAapDKQTGHSPRVLVLAATNLPWCIDEAA-RRRFVKRTYIPL 554
Cdd:smart00382  83 ILDEITSLLDA--------------EQEALLLLLEELRL--LLLLKSEKNLTVILTTNDEKDLGPALlRRRFDRRIVLLL 146


                   ..
gi 19112067    555 PE 556
Cdd:smart00382 147 IL 148
ycf46 CHL00195
Ycf46; Provisional
 379-595 1.18e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.98  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  379 SDIAGLDDAKNSLKeaviypfLRPELFQ------GLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKY 452
Cdd:CHL00195 228 SDIGGLDNLKDWLK-------KRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  453 LGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSRRLKTefLIQWSSltnaapDKQtghSPRVLVLAAT 532
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVLAT--FITWLS------EKK---SPVFVVATAN 368

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112067  533 NLPWCIDEAARR-RFVKRTYIPLPEKETRYK----HLSHLLHNQVHcltEEDLEELVNLTEGYSGSDI 595
Cdd:CHL00195 369 NIDLLPLEILRKgRFDEIFFLDLPSLEEREKifkiHLQKFRPKSWK---KYDIKKLSKLSNKFSGAEI 433
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 380-505 1.82e-14

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: 71.25  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKEAViYPFLRPELFQGLREPvQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKL 459
Cdd:cd19507   1 DVGGLDNLKDWLKKRK-AAFSKQASAYGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESR 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19112067 460 VRALFEVAKRQTCSVIFVDEIDSILSaRNDSGNEHESSRRLKTEFL 505
Cdd:cd19507  79 LRQMIQTAEAIAPCVLWIDEIEKGFS-NADSKGDSGTSSRVLGTFL 123
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 381-544 3.67e-14

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: 70.98  E-value: 3.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSL-KEAVIYPFLRPELFQGLR-EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSI-SASSLTSKYLGDSE 457
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGcKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 458 KLVRALFEVAKRQ--------TCSVIFVDEIDSILSARNDSGNEHESSRRLKTEFLIQW---SSLTNaapdkqtghsprV 526
Cdd:cd19504  82 ANIRKLFADAEEEqrrlgansGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIdgvEQLNN------------I 149

                       170
                ....*....|....*...
gi 19112067 527 LVLAATNLPWCIDEAARR 544
Cdd:cd19504 150 LVIGMTNRKDLIDEALLR 167
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 415-552 1.09e-13

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 70.17  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 415 MLLFGPPGTGKTMLARAVA---------TEAKATFFSISASSLTSKYLGDSEKLVRALF----EVAKRQTCSV-IFVDEI 480
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKDALVfVLIDEV 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112067 481 DSILSARN--DSGNEHESSRRLKTEFLIQWSSLTNAAPdkqtghsprVLVLAATNLPWCIDEAarrrFVKRTYI 552
Cdd:cd19508 135 ESLAAARSasSSGTEPSDAIRVVNAVLTQIDRIKRYHN---------NVILLTSNLLEKIDVA----FVDRADI 195
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 381-498 2.30e-12

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: 65.86  E-value: 2.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSLKEAVIYPFLRPELFQGLREPV--QGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTS-KYLG-DS 456
Cdd:cd19498  13 IIGQDEAKRAVAIALRNRWRRMQLPEELRDEVtpKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDV 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19112067 457 EKLVRALFEvakrqtcSVIFVDEIDSIlsARNDSGNEHESSR 498
Cdd:cd19498  93 ESIIRDLVE-------GIVFIDEIDKI--AKRGGSSGPDVSR 125
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 415-480 2.53e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 69.34  E-value: 2.53e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112067  415 MLLFGPPGTGKTMLARAVATEAKATFFSISASSltskylgDSEKLVRALFEVAK------RQTcsVIFVDEI 480
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARqrrsagRRT--ILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 415-480 7.27e-12

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 67.77  E-value: 7.27e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112067 415 MLLFGPPGTGKTMLARAVATEAKATFFSISASSltskylgDSEKLVRALFEVAK------RQTcsVIFVDEI 480
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSAVT-------SGVKDIREVIEEARerraygRRT--ILFVDEI 114
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 412-549 6.53e-11

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: 61.00  E-value: 6.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 412 VQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDS--EKLVRALFEVAKRQTCSVIFVDEIDSILSARND 489
Cdd:cd19506  26 VKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVP 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 490 SGNEHESSRRLKTEFLiqwSSLTNAAPDKqtghspRVLVLAATNLPWCIDEAARRRFVKR 549
Cdd:cd19506 106 KTEKQLDPKRLKKDLP---KILKSLKPED------RVLIVGTTSRPFEADLKSFCKVYNK 156
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 623-657 3.13e-10

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: 55.97  E-value: 3.13e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19112067   623 PPISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFG 657
Cdd:pfam09336  27 PPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 383-492 1.32e-08

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: 57.93  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   383 GLDDAKNS---LKEAVIYPFLRPElfQGLREPVQG--MLLFGPPGTGKTMLARAVATE-------AKATFFSISASSLTS 450
Cdd:TIGR03922 280 GLERVKRQvaaLKSSTAMALARAE--RGLPVAQTSnhMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIG 357

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 19112067   451 KYLGDSEKLVRALFEVAkrqTCSVIFVDEIDSILSARNDSGN 492
Cdd:TIGR03922 358 QYIGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGYGQKD 396
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 577-614 1.85e-08

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: 50.61  E-value: 1.85e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 19112067   577 EEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDAL 614
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 414-545 2.94e-08

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: 53.12  E-value: 2.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 414 GMLLFGPPGTGKTMLARAVATEAKatfFSISASSLTSKylGDSEKLVRALFEVAKRQtcSVIFVDEIDSILSARNDSGNE 493
Cdd:cd19510  25 GYLLYGPPGTGKSSFIAALAGELD---YDICDLNLSEV--VLTDDRLNHLLNTAPKQ--SIILLEDIDAAFESREHNKKN 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19112067 494 HESSRRLKTeflIQWSSLTNAApDKQTGHSPRVLVLaATNLPWCIDEAARRR 545
Cdd:cd19510  98 PSAYGGLSR---VTFSGLLNAL-DGVASSEERIVFM-TTNHIERLDPALIRP 144
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 381-483 1.26e-07

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: 53.37  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSLKEAVIYPFLRpeLFQGLREPVQG-------MLLFGPPGTGKTMLARAVATEAKATFFSISASSLT-SKY 452
Cdd:cd19497  14 VIGQERAKKVLSVAVYNHYKR--IRNNLKQKDDDveleksnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19112067 453 LGDS-----EKLVR-ALFEVAKRQTcSVIFVDEIDSI 483
Cdd:cd19497  92 VGEDvenilLKLLQaADYDVERAQR-GIVYIDEIDKI 127
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 409-546 1.80e-07

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: 50.99  E-value: 1.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 409 REPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSkyLG-DSEKLVRALFEVAKRQTCSVI-FVDEIDSILSA 486
Cdd:cd19512  19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGLLlFVDEADAFLRK 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112067 487 RNDSGNEhESSRRLKTEFLIqwssltnaapdkQTG-HSPRVLVLAATNLPWCIDEAARRRF 546
Cdd:cd19512  97 RSTEKIS-EDLRAALNAFLY------------RTGeQSNKFMLVLASNQPEQFDWAINDRI 144
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 416-483 9.51e-07

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: 49.12  E-value: 9.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   416 LLFGPPGTGKTMLARAVATE---AKATFFSISASSLT-----SKYLGDSEKLVRA-----LFEVAKRQTCSVIFVDEIDS 482
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMeehsvSRLIGAPPGYVGYeeggqLTEAVRRKPYSIVLIDEIEK 86


                  .
gi 19112067   483 I 483
Cdd:pfam07724  87 A 87
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
375-480 3.23e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.74  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  375 PVYWSDIAGLDDAKNSLKeaviypflrpeLF----QGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTS 450
Cdd:PRK00080  21 PKSLDEFIGQEKVKENLK-----------IFieaaKKRGEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEK 89

                         90       100       110
                 ....*....|....*....|....*....|
gi 19112067  451 KylGDsekLVRALFEVAKRqtcSVIFVDEI 480
Cdd:PRK00080  90 P--GD---LAAILTNLEEG---DVLFIDEI 111
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 375-480 1.07e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 45.95  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   375 PVYWSDIAGLDDAKNSLKEAViypflrpELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKylG 454
Cdd:pfam05496   3 PRTLDEYIGQEKVKENLKIFI-------EAAKQRGEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP--G 73

                          90       100
                  ....*....|....*....|....*.
gi 19112067   455 DsekLVRALFEVAKRQtcsVIFVDEI 480
Cdd:pfam05496  74 D---LAAILTNLEPGD---VLFIDEI 93
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
414-463 1.10e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.43  E-value: 1.10e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19112067 414 GMLLFGPPGTGKTMLARAVATE--AKATFFSISASSLTSKYLGDSEKLVRAL 463
Cdd:COG1224  66 GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEFLMQAL 117
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 416-501 1.35e-05

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 48.29  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  416 LLFGPPGTGKTMLARAVATE----------AKATFFSISASSLT--SKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSI 483
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                         90
                 ....*....|....*...
gi 19112067  484 LSARNDSGNEHESSRRLK 501
Cdd:PRK11034 291 IGAGAASGGQVDAANLIK 308
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 380-483 1.38e-05

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: 46.01  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 380 DIAGLDDAKNSLKE--AViypflrpelfQGLREPVQG--MLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSK---- 451
Cdd:cd19500  11 DHYGLEDVKERILEylAV----------RKLKGSMKGpiLCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeir 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19112067 452 -----YLGDSE-KLVRALFEVAKRQtcSVIFVDEIDSI 483
Cdd:cd19500  81 ghrrtYVGAMPgRIIQALKKAGTNN--PVFLLDEIDKI 116
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 416-559 2.34e-05

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: 46.70  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 416 LLFGPPGTGKTMLARAVATEAKATFFSISASS--LTSKYLGDS--------EKLV-RALFevakrqtCSVIFVDEIDsil 484
Cdd:COG0714  35 LLEGVPGVGKTTLAKALARALGLPFIRIQFTPdlLPSDILGTYiydqqtgeFEFRpGPLF-------ANVLLADEIN--- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 485 saRNDSgnehessrrlKTEfliqwSSL--------------TNAAPdkqtghsPRVLVLAATN---------LPwcidEA 541
Cdd:COG0714 105 --RAPP----------KTQ-----SALleameerqvtipggTYKLP-------EPFLVIATQNpieqegtypLP----EA 156

                       170
                ....*....|....*...
gi 19112067 542 ARRRFVKRTYIPLPEKET 559
Cdd:COG0714 157 QLDRFLLKLYIGYPDAEE 174
AAA_22 pfam13401
AAA domain;
415-483 2.55e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 44.25  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   415 MLLFGPPGTGKTMLARAVA---TEAKATFFSISASSLTS----------------KYLGDSEKLVRALFEVAKRQ-TCSV 474
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVDLPSGTSpkdllrallralglplSGRLSKEELLAALQQLLLALaVAVV 87


                  ....*....
gi 19112067   475 IFVDEIDSI 483
Cdd:pfam13401  88 LIIDEAQHL 96
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 410-480 2.74e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 46.52  E-value: 2.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112067   410 EPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKylGDSEKLVRALfevakrQTCSVIFVDEI 480
Cdd:TIGR00635  28 EALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GDLAAILTNL------EEGDVLFIDEI 90
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
416-487 5.89e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.92  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  416 LLFGPPGTGKTMLARavaTEAKatF----FSIS-ASSLT-SKYLG-DSE----KLV-RALFEVAKRQTcSVIFVDEIDSI 483
Cdd:PRK05342 112 LLIGPTGSGKTLLAQ---TLAR--IldvpFAIAdATTLTeAGYVGeDVEnillKLLqAADYDVEKAQR-GIVYIDEIDKI 185


                 ....
gi 19112067  484 lsAR 487
Cdd:PRK05342 186 --AR 187
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 414-463 1.31e-04

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: 44.61  E-value: 1.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19112067   414 GMLLFGPPGTGKTMLARAVATE--AKATFFSISASSLTSKYLGDSEKLVRAL 463
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVYSLEMKKTEALTQAF 103
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
 373-504 1.81e-04

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 44.21  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  373 HEPVYWSDIAGLDDAKNSLKEAVIYPFLrPELfqglrepvqgmLLFGPPGTGKTMLARAVATEA-----KATFFSISAS- 446
Cdd:PRK12402   9 YRPALLEDILGQDEVVERLSRAVDSPNL-PHL-----------LVQGPPGSGKTAAVRALARELygdpwENNFTEFNVAd 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  447 --SLTSKYLGDSEKLVRaLFEVAKRQTCSVIfvDEIDSILsarndsgNEHESSRRLKTEF 504
Cdd:PRK12402  77 ffDQGKKYLVEDPRFAH-FLGTDKRIRSSKI--DNFKHVL-------KEYASYRPLSADY 126
PRK04195 PRK04195
replication factor C large subunit; Provisional
 379-491 3.23e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 43.76  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  379 SDIAGLDDAKNSLKE-AVIYPFLRPelfqglREPVqgmLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKylGDSE 457
Cdd:PRK04195  14 SDVVGNEKAKEQLREwIESWLKGKP------KKAL---LLYGPPGVGKTSLAHALANDYGWEVIELNASDQRTA--DVIE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19112067  458 KLV------RALFEVAKRqtcsVIFVDEIDSIlSARNDSG 491
Cdd:PRK04195  83 RVAgeaatsGSLFGARRK----LILLDEVDGI-HGNEDRG 117
PRK13341 PRK13341
AAA family ATPase;
415-489 3.33e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.89  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067  415 MLLFGPPGTGKTMLARAVATEAKATFfsisaSSLTSKYLGDSEklVRALFEVAKRQ-----TCSVIFVDEIDSILSARND 489
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIANHTRAHF-----SSLNAVLAGVKD--LRAEVDRAKERlerhgKRTILFIDEVHRFNKAQQD 127
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 415-434 4.03e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.49  E-value: 4.03e-04
                        10        20
                ....*....|....*....|
gi 19112067 415 MLLFGPPGTGKTMLARAVAT 434
Cdd:COG0606 214 LLMIGPPGSGKTMLARRLPG 233
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
413-480 1.03e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 41.30  E-value: 1.03e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112067 413 QGMLLFGPPGTGKTMLARAVATEA----KATFFsISASSL-----TSKYLGDSEKLVRALfevaKRqtCSVIFVDEI 480
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEAcragYRVRF-TTAPDLvnelkEARADGRLERLLKRL----AK--VDLLILDEL 169
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 381-481 1.15e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.24  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 381 IAGLDDAKNSLKEAVIypflRPELfqGLREPVQG---MLLFGPPGTGKTMLARAVATE---AKATFFSISASSLTSK--- 451
Cdd:cd19499  13 VVGQDEAVKAVSDAIR----RARA--GLSDPNRPigsFLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKhsv 86

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19112067 452 ---------YLGDSEKLVraLFEVAKRQTCSVIFVDEID 481
Cdd:cd19499  87 srligappgYVGYTEGGQ--LTEAVRRKPYSVVLLDEIE 123
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 415-434 1.45e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.60  E-value: 1.45e-03
                          10        20
                  ....*....|....*....|
gi 19112067   415 MLLFGPPGTGKTMLARAVAT 434
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 414-546 1.50e-03

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.20  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   414 GMLLFGPPGTGKTMLARAVA----------------TEAKATFFSISASSLTSKYLgDSEkLVRALfevakrQTCSVIFV 477
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqltrdTTEEDLFGRRNIDPGGASWV-DGP-LVRAA------REGEIAVL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112067   478 DEIDSILSARNDSGNEHESSRRLKTEfliqwsSLTNAAPDKQTGhsprVLVLAATNLP----WCIDEAARRRF 546
Cdd:pfam07728  73 DEINRANPDVLNSLLSLLDERRLLLP------DGGELVKAAPDG----FRLIATMNPLdrglNELSPALRSRF 135
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
400-489 1.56e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 41.37  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 400 LRPeLFQGlrEPVQGMLLFGPPGTGKTMLARAVATEAKA---------TFFSISASSLTSKY-----LGDS--------- 456
Cdd:COG1474  42 LRP-ALRG--ERPSNVLIYGPTGTGKTAVAKYVLEELEEeaeergvdvRVVYVNCRQASTRYrvlsrILEElgsgedips 118

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19112067 457 -----EKLVRALFEVAKRQTCSVIFV-DEIDSILSARND 489
Cdd:COG1474 119 tglstDELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD 157
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 375-480 2.03e-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: 40.83  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 375 PVYWSDIAGLDDAKNSLK---EAViypflrpelfQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSK 451
Cdd:COG2255  24 PKRLDEYIGQEKVKENLKifiEAA----------KKRGEALDHVLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAIEKP 93

                        90       100
                ....*....|....*....|....*....
gi 19112067 452 ylGDsekLVRALFEVAKRqtcSVIFVDEI 480
Cdd:COG2255  94 --GD---LAAILTNLEEG---DVLFIDEI 114
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
416-549 4.08e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.36  E-value: 4.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 416 LLFGPPGTGKTMLARAVATEAKATFFSI---------SASSLTSKYLGDSEKLVRALFEVAK---RQTCSVIFvdeidsi 483
Cdd:COG0645   3 LVCGLPGSGKSTLARALAERLGAVRLRSdvvrkrlfgAGLAPLERSPEATARTYARLLALARellAAGRSVIL------- 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112067 484 lsarnDSGNEHESSRRlktefliQWSSLTnaapdKQTGHSPRVLVLAATnlpwciDEAARRRFVKR 549
Cdd:COG0645  76 -----DATFLRRAQRE-------AFRALA-----EEAGAPFVLIWLDAP------EEVLRERLEAR 118
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 221-359 5.07e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.28  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067   221 NSTTFPTAMKSQSTTKPTLSNS-VSSPSiQVSNNQNANNSTPL------SFHAPIPPLHVPavplTSASHSSSDGKSRKH 293
Cdd:pfam05109 450 SSTHVPTNLTAPASTGPTVSTAdVTSPT-PAGTTSGASPVTPSpsprdnGTESKAPDMTSP----TSAVTTPTPNATSPT 524

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112067   294 PSPYKPYLNSSHDTLGsSTRPSSADTAGSP-ATSPPATADSKTIVSKTISASTTQQTEPLQQTTPSS 359
Cdd:pfam05109 525 PAVTTPTPNATSPTLG-KTSPTSAVTTPTPnATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNA 590
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 387-431 7.29e-03

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


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 39.71  E-value: 7.29e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19112067 387 AKNSLKE-------AVIYPflrPelfQGLRepvqgMLLFGPPGTGKTMLARA 431
Cdd:COG1221 109 ANGSLKNaieqakaAILYP---P---KGLH-----TLILGPTGVGKSFFAEL 149
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 416-442 8.13e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.22  E-value: 8.13e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 19112067  416 LLFGPPGTGKTMLARAVATEA-----KATFFS 442
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAAcrqgyRVRFTT 125
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 403-632 9.59e-03

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 38.39  E-value: 9.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 403 ELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFsISASSLTSKylgdseklvRALFEvakrqtcsvifvdEIDS 482
Cdd:COG2842  41 EALDEARALPGIGVVYGESGVGKTTAAREYANRNPNVIY-VTASPSWTS---------KELLE-------------ELAE 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 483 ILSARNDSGNEHESSRRLKtEFLIQwssltnaapdkqtghSPRVLVlaatnlpwcIDEAAR---------RRFVKRTYIP 553
Cdd:COG2842  98 ELGIPAPPGTIADLRDRIL-ERLAG---------------TGRLLI---------IDEADHlkpkaleelRDIHDETGVG 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112067 554 --------LPEKETRYKHlshlLHN------QVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDALltTSA 619
Cdd:COG2842 153 vvligmerLPAKLKRYEQ----LYSrigfwvEFKPLSLEDVRALAEAWGELTDPDLLELLHRITRGNLRRLDRTL--RLA 226

                       250
                ....*....|....*....
gi 19112067 620 EMI------PPISLNHFKA 632
Cdd:COG2842 227 ARAakrnglTKITLDHVRA 245
 
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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