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Conserved domains on  [gi|341865581|ref|NP_001230076|]
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nuclear valosin-containing protein-like isoform 4 [Homo sapiens]

Protein Classification

Nucleolin_bd and RecA-like_NVL_r1-like domain-containing protein( domain architecture ID 13875340)

Nucleolin_bd and RecA-like_NVL_r1-like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
152-765 0e+00

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.


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 578.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  152 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 230
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  231 LDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 310
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  311 ARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREA 390
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  391 AMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgllrdqdplseeqmqglcIELNDFIVALS 470
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPA--------------EVLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  471 SVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGL 550
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  551 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLEARQQVFI 629
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  630 MAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGdlRCDCYTGADLSALVREA 709
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581  710 SICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIMYERLQESLSR 765
Cdd:TIGR01243 669 AMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
2-72 7.62e-30

Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged helix motif. It binds nucleolin.


:

Pssm-ID: 465247  Cd Length: 70  Bit Score: 112.34  E-value: 7.62e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865581    2 KPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSiDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
152-765 0e+00

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: 578.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  152 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 230
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  231 LDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 310
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  311 ARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREA 390
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  391 AMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgllrdqdplseeqmqglcIELNDFIVALS 470
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPA--------------EVLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  471 SVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGL 550
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  551 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLEARQQVFI 629
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  630 MAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGdlRCDCYTGADLSALVREA 709
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581  710 SICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIMYERLQESLSR 765
Cdd:TIGR01243 669 AMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
175-341 7.41e-107

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: 323.59  E-value: 7.41e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGNDMTLKEVCKMLIHM-RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 253
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 254 KLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 332
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 341865581 333 GRFDREICL 341
Cdd:cd19518  161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
420-751 1.65e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 328.50  E-value: 1.65e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 420 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 499
Cdd:COG1222   12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 500 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 579
Cdd:COG1222   88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 580 KNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLP 658
Cdd:COG1222  168 REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 659 PPADRLAILKTITKNgtkPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRQEMARqksgnekgelkVSHKHFE 738
Cdd:COG1222  248 DEEAREEILKIHLRD---MPLADDVDLDKLAKLT--EGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLE 311
                        330
                 ....*....|...
gi 341865581 739 EAFKKVRSSISKK 751
Cdd:COG1222  312 KAIEKVKKKTETA 324
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
485-756 7.51e-79

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 258.22  E-value: 7.51e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN----QLLTEMDGLEARQQVFIMAATNRPDIID 640
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 641 PAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRqemar 720
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAELT--EGASGADLKAICTEAGMFAIR----- 354
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 341865581 721 qksgNEKGElkVSHKHFEEAFKKVRS----SISKKDQIMY 756
Cdd:PRK03992 355 ----DDRTE--VTMEDFLKAIEKVMGkeekDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
527-657 6.24e-56

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 187.42  E-value: 6.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 606
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341865581  607 SVRVVNQLLTEMDGLEARQQ-VFIMAATNRPDIIDPAILrpGRLDKTLFVGL 657
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
485-761 5.01e-49

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 176.85  E-value: 5.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLEARQQ---VFIMAATNRP 636
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 637 DIIDPAILRpgRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRq 716
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVK- 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 341865581 717 EMARQKSGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQE 761
Cdd:NF041006 326 EMFEKGLGEPR---PITMEDFKEVLKIRKPSVNQEMLKAYEAWHE 367
cell_div_CdvC NF041006
cell division protein CdvC;
110-414 2.47e-39

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 149.50  E-value: 2.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 110 YPD-PQDSKDSSLLESDMKRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCK 188
Cdd:NF041006  48 YPDsPLRHAYEQMINEYKKRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 189 MLIH-----MRHPEVYHhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQA- 262
Cdd:NF041006 114 ALKEaivypSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAr 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 263 ----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD-PALRragRF 335
Cdd:NF041006 191 ekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDePFLR---RF 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 336 DREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQKKNPEMED 414
Cdd:NF041006 265 QKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGEPRPITMED 342
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
2-72 7.62e-30

Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged helix motif. It binds nucleolin.


Pssm-ID: 465247  Cd Length: 70  Bit Score: 112.34  E-value: 7.62e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865581    2 KPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSiDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
206-345 1.83e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 85.50  E-value: 1.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581   206 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKV-----------------AAPEIVSGVSGESEQKLRELFEQAVSNAPC 268
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581   269 IIFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRFDREICLGIPD 345
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
152-765 0e+00

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: 578.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  152 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 230
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  231 LDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 310
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  311 ARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREA 390
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  391 AMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgllrdqdplseeqmqglcIELNDFIVALS 470
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPA--------------EVLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  471 SVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGL 550
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  551 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLEARQQVFI 629
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  630 MAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGdlRCDCYTGADLSALVREA 709
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581  710 SICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIMYERLQESLSR 765
Cdd:TIGR01243 669 AMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
175-341 7.41e-107

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: 323.59  E-value: 7.41e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGNDMTLKEVCKMLIHM-RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 253
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 254 KLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 332
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 341865581 333 GRFDREICL 341
Cdd:cd19518  161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
420-751 1.65e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 328.50  E-value: 1.65e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 420 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 499
Cdd:COG1222   12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 500 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 579
Cdd:COG1222   88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 580 KNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLP 658
Cdd:COG1222  168 REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 659 PPADRLAILKTITKNgtkPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRQEMARqksgnekgelkVSHKHFE 738
Cdd:COG1222  248 DEEAREEILKIHLRD---MPLADDVDLDKLAKLT--EGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLE 311
                        330
                 ....*....|...
gi 341865581 739 EAFKKVRSSISKK 751
Cdd:COG1222  312 KAIEKVKKKTETA 324
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
495-655 8.10e-106

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: 320.59  E-value: 8.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 495 LEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 574
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 575 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                 .
gi 341865581 655 V 655
Cdd:cd19530  161 V 161
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
498-655 1.38e-94

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: 291.11  E-value: 1.38e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 578 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFV 655
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
127-395 2.87e-87

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 278.43  E-value: 2.87e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 127 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVV 205
Cdd:COG1222   31 LLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 206 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EV 284
Cdd:COG1222  111 PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 285 ASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQ 364
Cdd:COG1222  191 GTSGEVQRTVNQLLAELDGFES---RGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLAD 267
                        250       260       270
                 ....*....|....*....|....*....|.
gi 341865581 365 AFDFCHLAHLTPGFVGADLMALCREAAMCAV 395
Cdd:COG1222  268 DVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
411-745 9.16e-83

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: 269.09  E-value: 9.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 411 EMEDLPSKGVQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREGFVTVPNVTWA 490
Cdd:COG0464   78 LLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:COG0464  158 DLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEK 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLeaRQQVFIMAATNRPDIIDPAILRpgRLD 650
Cdd:COG0464  238 NLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFD 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 651 KTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRQemarqksgnekGEL 730
Cdd:COG0464  314 EIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL-----------GRE 377
                        330
                 ....*....|....*
gi 341865581 731 KVSHKHFEEAFKKVR 745
Cdd:COG0464  378 PVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
485-756 7.51e-79

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 258.22  E-value: 7.51e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN----QLLTEMDGLEARQQVFIMAATNRPDIID 640
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 641 PAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRqemar 720
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAELT--EGASGADLKAICTEAGMFAIR----- 354
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 341865581 721 qksgNEKGElkVSHKHFEEAFKKVRS----SISKKDQIMY 756
Cdd:PRK03992 355 ----DDRTE--VTMEDFLKAIEKVMGkeekDSMEEPGVMF 388
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
175-341 4.00e-77

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: 245.66  E-value: 4.00e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 252
Cdd:cd19503    1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 253 QKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRA 332
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSS---RGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 341865581 333 GRFDREICL 341
Cdd:cd19503  157 GRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
166-415 2.60e-71

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 238.66  E-value: 2.60e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 166 FQISNVKFEDVGGNDMTLKEVCKMLIHMRH-PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV 244
Cdd:COG0464  149 LELREAILDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 245 SGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPDS 324
Cdd:COG0464  229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRS-----DVVVIAATNRPDL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 325 LDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVnrvlmklqE 404
Cdd:COG0464  304 LDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL--------R 373
                        250
                 ....*....|.
gi 341865581 405 QQKKNPEMEDL 415
Cdd:COG0464  374 LGREPVTTEDL 384
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
498-655 1.29e-70

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: 228.15  E-value: 1.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 578 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFV 655
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
498-655 3.89e-70

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: 227.01  E-value: 3.89e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 578 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 341865581 655 V 655
Cdd:cd19528  161 I 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
485-758 3.00e-69

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 236.03  E-value: 3.00e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  485 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRP 636
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  637 DIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtkPPLDADVNLEAIAgdLRCDCYTGADLSALVREASICALRq 716
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVA--RRTPGFSGADLANLLNEAALLAAR- 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 341865581  717 emarqksgneKGELKVSHKHFEEAFKKVRSSISKKDQIMYER 758
Cdd:TIGR01241 278 ----------KNKTEITMNDIEEAIDRVIAGPEKKSRVISEK 309
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
491-651 7.74e-69

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: 223.71  E-value: 7.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 650
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 .
gi 341865581 651 K 651
Cdd:cd19503  161 R 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
498-654 2.44e-67

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: 219.22  E-value: 2.44e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581 578 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
175-342 1.02e-66

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 218.07  E-value: 1.02e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 253
Cdd:cd19519    1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 254 KLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAG 333
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK---QRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 341865581 334 RFDREICLG 342
Cdd:cd19519  158 RFDREIDIG 166
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
485-758 6.36e-65

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 226.46  E-value: 6.36e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:COG0465  137 PKVTFDDVAGVDEAKEEL-QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLEARQQVFIMAATN 634
Cdd:COG0465  216 VGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGVIVIAATN 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 635 RPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtKpPLDADVNLEAIA----GdlrcdcYTGADLSALVREAS 710
Cdd:COG0465  289 RPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIArrtpG------FSGADLANLVNEAA 359
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 341865581 711 ICAlrqemARqksgneKGELKVSHKHFEEAFKKVRSSISKKDQIMYER 758
Cdd:COG0465  360 LLA-----AR------RNKKAVTMEDFEEAIDRVIAGPERKSRVISEK 396
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
151-395 1.23e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 220.47  E-value: 1.23e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 151 IEAVLQKKAKARGLEFQIS---NVKFEDVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAH 225
Cdd:PRK03992 105 IVEVLPSEKDPRVQAMEVIespNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 226 AIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMD 302
Cdd:PRK03992 184 AVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMD 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 303 DLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGAD 382
Cdd:PRK03992 264 GFDP---RGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGAD 340
                        250
                 ....*....|...
gi 341865581 383 LMALCREAAMCAV 395
Cdd:PRK03992 341 LKAICTEAGMFAI 353
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
158-397 2.43e-63

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 219.85  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  158 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK 237
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  238 VAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE---VASKDMERRIVAQLLTCMDDLNNvaaTARVL 314
Cdd:TIGR01241 119 ISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGT---NTGVI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  315 VIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCA 394
Cdd:TIGR01241 196 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275

                  ...
gi 341865581  395 VNR 397
Cdd:TIGR01241 276 ARK 278
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
494-655 3.51e-61

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: 202.90  E-value: 3.51e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 494 ALEDIREeltmaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 573
Cdd:cd19481    1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 574 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKT 652
Cdd:cd19481   76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                 ...
gi 341865581 653 LFV 655
Cdd:cd19481  156 IEF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
488-651 1.01e-60

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: 202.18  E-value: 1.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 488 TWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 567
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 568 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAIL 644
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*..
gi 341865581 645 RPGRLDK 651
Cdd:cd19502  161 RPGRFDR 167
ftsH CHL00176
cell division protein; Validated
487-744 3.08e-60

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 214.91  E-value: 3.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 487 VTWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 566
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFE-EVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 567 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLEARQQVFIMAATNRPDI 638
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRVDI 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 639 IDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtkPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRQEM 718
Cdd:CHL00176 334 LDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARRKK 408
                        250       260
                 ....*....|....*....|....*.
gi 341865581 719 ArqksgnekgelKVSHKHFEEAFKKV 744
Cdd:CHL00176 409 A-----------TITMKEIDTAIDRV 423
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
158-415 1.78e-59

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 211.43  E-value: 1.78e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 158 KAKARGLEFQISNVKFEDVGGND---MTLKEVCKMLihmRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLP 234
Cdd:COG0465  126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 235 ILKVAAPEIVS---GVsGESeqKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SKDmER-RIVAQLLTCMD--Dln 305
Cdd:COG0465  203 FFSISGSDFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGHD-EReQTLNQLLVEMDgfE-- 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 306 nvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMA 385
Cdd:COG0465  277 ---GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLAN 353
                        250       260       270
                 ....*....|....*....|....*....|
gi 341865581 386 LCREAAMCAVNRvlmklqeqQKKNPEMEDL 415
Cdd:COG0465  354 LVNEAALLAARR--------NKKAVTMEDF 375
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
487-655 3.58e-59

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: 197.84  E-value: 3.58e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 487 VTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 566
Cdd:cd19501    1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 567 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAI 643
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 341865581 644 LRPGRLDKTLFV 655
Cdd:cd19501  160 LRPGRFDRQVYV 171
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
498-655 4.63e-59

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: 197.35  E-value: 4.63e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 498 IREELTMAILAPVRNPDQFkALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19527    1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 578 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-ARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                 .
gi 341865581 655 V 655
Cdd:cd19527  160 L 160
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
485-753 2.45e-57

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 200.76  E-value: 2.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDP 641
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTNVKVIMATNRADTLDP 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 642 AILRPGRLDKTLFVGLPPPADRLAILKTITkngTKPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRqemarq 721
Cdd:PTZ00454 300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAICQEAGMQAVR------ 368
                        250       260       270
                 ....*....|....*....|....*....|..
gi 341865581 722 ksgneKGELKVSHKHFEEAFKKVrssISKKDQ 753
Cdd:PTZ00454 369 -----KNRYVILPKDFEKGYKTV---VRKTDR 392
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
491-656 2.89e-57

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: 192.65  E-value: 2.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 650
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 341865581 651 KTLFVG 656
Cdd:cd19519  161 REIDIG 166
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
173-390 2.95e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 195.49  E-value: 2.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 173 FEDVGGNDmTLKEVCKMLIH-MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 251
Cdd:COG1223    1 LDDVVGQE-EAKKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 252 EQKLRELFEQAvSNAPCIIFIDEIDAITPKREVASKDME-RRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALR 330
Cdd:COG1223   80 ARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDGLPS-----GSVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 331 RagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREA 390
Cdd:COG1223  154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
484-716 3.54e-57

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 203.40  E-value: 3.54e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  484 VPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVAN-------ESGLN---FI 553
Cdd:TIGR03689 176 VPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  554 SVKGPELLNMYVGESERAVRQVFQRAKNSA----PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLEAR 624
Cdd:TIGR03689 256 NIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESL 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  625 QQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAIL-KTITKNgtkPPLDADvnLEAIAGDlrcdcytgadls 703
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDD---LPLPED--LAAHDGD------------ 394
                         250
                  ....*....|...
gi 341865581  704 alvREASICALRQ 716
Cdd:TIGR03689 395 ---REATAAALIQ 404
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
488-762 2.05e-56

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 204.50  E-value: 2.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 488 TWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 567
Cdd:PRK10733 150 TFADVAGCDEAKEEVA-ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 568 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLEARQQVFIMAATNRPDII 639
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 640 DPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDlrCDCYTGADLSALVREASICALRqema 719
Cdd:PRK10733 304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 341865581 720 rqksGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQES 762
Cdd:PRK10733 375 ----GNKR---VVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
527-657 6.24e-56

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 187.42  E-value: 6.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 606
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341865581  607 SVRVVNQLLTEMDGLEARQQ-VFIMAATNRPDIIDPAILrpGRLDKTLFVGL 657
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
192-339 4.09e-55

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: 186.33  E-value: 4.09e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 192 HMRHPEVyHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIF 271
Cdd:cd19481   12 PRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPCILF 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 272 IDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19481   91 IDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
183-339 4.11e-54

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: 183.64  E-value: 4.11e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 183 LKEVCKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFE 260
Cdd:cd19511    1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 261 QAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
158-407 7.39e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 197.18  E-value: 7.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 158 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK 237
Cdd:PRK10733 136 KSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFT 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 238 VAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREV---ASKDMERRIVAQLLTCMDDLNnvaATARVL 314
Cdd:PRK10733 216 ISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE---GNEGII 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 315 VIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCA 394
Cdd:PRK10733 293 VIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFA 372
                        250
                 ....*....|....*
gi 341865581 395 V--NRVLMKLQEQQK 407
Cdd:PRK10733 373 ArgNKRVVSMVEFEK 387
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
210-342 2.40e-53

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 180.48  E-value: 2.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDM 289
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 341865581  290 ERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREICLG 342
Cdd:pfam00004  81 SRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
171-339 1.73e-51

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: 177.04  E-value: 1.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 171 VKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 250
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 251 SEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SKDMERRIVAQLLTCMDDLnnvAATARVLVIGATNRPDSLDP 327
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGF---ESNTGVIVIAATNRPDVLDP 157
                        170
                 ....*....|..
gi 341865581 328 ALRRAGRFDREI 339
Cdd:cd19501  158 ALLRPGRFDRQV 169
ftsH CHL00176
cell division protein; Validated
149-397 1.97e-51

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 190.26  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 149 GEIEAVLQKKAKarglefqiSNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIA 228
Cdd:CHL00176 166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 229 GELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDMER-RIVAQLLTCMDDLN 305
Cdd:CHL00176 238 GEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgaGIGGGNDEReQTLNQLLTEMDGFK 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 306 nvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMA 385
Cdd:CHL00176 318 ---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLAN 394
                        250
                 ....*....|..
gi 341865581 386 LCREAAMCAVNR 397
Cdd:CHL00176 395 LLNEAAILTARR 406
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
496-745 3.96e-51

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 178.54  E-value: 3.96e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 496 EDIREELTMaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 575
Cdd:COG1223    8 EEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 576 FQRAKNsAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLeaRQQVFIMAATNRPDIIDPAILRpgRLDKTLF 654
Cdd:COG1223   87 FDFARR-APCVIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 655 VGLPPPADRLAILKtitKNGTKPPLDADVNLEAIAGdlRCDCYTGADLSALVREasicalrqemARQKSGNEKGElKVSH 734
Cdd:COG1223  162 FPLPDKEERKEILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----------ALKKAILEDRE-KVTK 225
                        250
                 ....*....|.
gi 341865581 735 KHFEEAFKKVR 745
Cdd:COG1223  226 EDLEEALKQRK 236
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
491-651 7.18e-51

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: 175.29  E-value: 7.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----EARQQVFIMAATNRPDIIDPAILRP 646
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*
gi 341865581 647 GRLDK 651
Cdd:cd19518  161 GRFDR 165
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
173-339 1.44e-50

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: 174.45  E-value: 1.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 173 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 251
Cdd:cd19502    2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 252 EQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPA 328
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFD---PRGNIKVIMATNRPDILDPA 158
                        170
                 ....*....|.
gi 341865581 329 LRRAGRFDREI 339
Cdd:cd19502  159 LLRPGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
170-397 2.01e-50

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 181.88  E-value: 2.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 170 NVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVS 248
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 249 GESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMER---RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSL 325
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQ---TTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341865581 326 DPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNR 397
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
492-655 1.05e-49

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: 171.77  E-value: 1.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 492 IGALEDIREELTMAILAPVRNPDQFKaLGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 571
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 572 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEAR--QQVFIMAATNRPDIIDPAILRpgRL 649
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                 ....*.
gi 341865581 650 DKTLFV 655
Cdd:cd19509  158 EKRIYI 163
cell_div_CdvC NF041006
cell division protein CdvC;
485-761 5.01e-49

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 176.85  E-value: 5.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLEARQQ---VFIMAATNRP 636
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 637 DIIDPAILRpgRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRq 716
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVK- 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 341865581 717 EMARQKSGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQE 761
Cdd:NF041006 326 EMFEKGLGEPR---PITMEDFKEVLKIRKPSVNQEMLKAYEAWHE 367
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
193-339 9.07e-49

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: 169.21  E-value: 9.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 193 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFI 272
Cdd:cd19529   13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341865581 273 DEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19529   93 DEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDIIDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
173-411 3.21e-47

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 173.80  E-value: 3.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 173 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 251
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 252 EQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 331
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 332 AGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLMKL-QEQQKKNP 410
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVtQADFRKAK 421

                 .
gi 341865581 411 E 411
Cdd:PTZ00361 422 E 422
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
485-744 5.93e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 170.34  E-value: 5.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDP 641
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 642 AILRPGRLDKTLFVGLPPPADRLAILKTITkngTKPPLDADVNLEAIAgdLRCDCYTGADLSALVREASICALRQEmarq 721
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFI--MAKDELSGADIKAICTEAGLLALRER---- 408
                        250       260
                 ....*....|....*....|...
gi 341865581 722 ksgnekgELKVSHKHFEEAFKKV 744
Cdd:PTZ00361 409 -------RMKVTQADFRKAKEKV 424
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
195-339 3.04e-44

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: 156.52  E-value: 3.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 195 HPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDE 274
Cdd:cd19528   15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFFDE 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341865581 275 IDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19528   95 LDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
175-338 3.23e-44

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: 156.90  E-value: 3.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGND---MTLKEVckMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA-----APEIVSG 246
Cdd:cd19517    1 DIGGLShyiNQLKEM--VFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 247 VSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLD 326
Cdd:cd19517   79 WVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN---RGQVVVIGATNRPDALD 155
                        170
                 ....*....|..
gi 341865581 327 PALRRAGRFDRE 338
Cdd:cd19517  156 PALRRPGRFDRE 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
193-337 3.11e-43

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: 153.80  E-value: 3.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 193 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFI 272
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341865581 273 DEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 337
Cdd:cd19530   96 DEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
491-654 1.02e-42

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: 152.66  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 565
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 566 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILR 645
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*....
gi 341865581 646 PGRLDKTLF 654
Cdd:cd19517  161 PGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
485-655 2.56e-42

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: 151.55  E-value: 2.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 563
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 564 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-EARQQVFIMAATNRPDIIDPA 642
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 341865581 643 ILRpgRLDKTLFV 655
Cdd:cd19521  160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
491-655 3.31e-42

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: 151.04  E-value: 3.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVT-PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 569
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 570 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPAILRpg 647
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILR-- 158

                 ....*...
gi 341865581 648 RLDKTLFV 655
Cdd:cd19520  159 RMPKRFHI 166
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
194-339 2.13e-41

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: 148.35  E-value: 2.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 194 RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFID 273
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341865581 274 EIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19526   94 EFDSIAPKRGHDSTGVTDRVVNQLLTQLD---GVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
491-655 1.11e-39

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: 143.97  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 569
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 570 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------EARQQVFIMAATNRPDIIDP 641
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 341865581 642 AILRpgRLDKTLFV 655
Cdd:cd19522  159 ALRR--RLEKRIYI 170
cell_div_CdvC NF041006
cell division protein CdvC;
110-414 2.47e-39

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 149.50  E-value: 2.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 110 YPD-PQDSKDSSLLESDMKRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCK 188
Cdd:NF041006  48 YPDsPLRHAYEQMINEYKKRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 189 MLIH-----MRHPEVYHhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQA- 262
Cdd:NF041006 114 ALKEaivypSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAr 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 263 ----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD-PALRragRF 335
Cdd:NF041006 191 ekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDePFLR---RF 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 336 DREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQKKNPEMED 414
Cdd:NF041006 265 QKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGEPRPITMED 342
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
176-339 2.57e-39

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: 142.88  E-value: 2.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 176 VGGNDmTLKEVCK--MLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 253
Cdd:cd19509    1 IAGLD-DAKEALKeaVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 254 KLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRRag 333
Cdd:cd19509   79 IVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN-KPEDRVLVLGATNRPWELDEAFLR-- 155

                 ....*.
gi 341865581 334 RFDREI 339
Cdd:cd19509  156 RFEKRI 161
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
193-337 5.93e-38

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: 138.80  E-value: 5.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 193 MRHPEVYHhLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFI 272
Cdd:cd19527   13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581 273 DEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRRAGRFDR 337
Cdd:cd19527   92 DELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
485-655 5.84e-36

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: 134.35  E-value: 5.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPA 642
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEA 175
                        170
                 ....*....|...
gi 341865581 643 ILRpgRLDKTLFV 655
Cdd:cd19525  176 ARR--RLVKRLYI 186
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
151-353 1.51e-35

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 141.77  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  151 IEAVLQKKAKARGLEfQISNVKFEDVGGNDMTLKevckmLIH------MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLA 224
Cdd:TIGR03689 160 FEAIPRTEVEDLVLE-EVPDVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIA 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  225 HAIAGELDLPI----------LKVAAPEIVSGVSGESEQKLRELFEQAVSNA----PCIIFIDEIDAITPKREVA-SKDM 289
Cdd:TIGR03689 234 KAVANSLAARIgaegggksyfLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGvSSDV 313
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341865581  290 ERRIVAQLLTcmdDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERIL 353
Cdd:TIGR03689 314 ETTVVPQLLA---EIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF 374
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
513-650 6.39e-35

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: 130.69  E-value: 6.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 513 PDQFKALGLVTPAGVLLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYVGESERAVRQVF------QRAK- 580
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeeQRRLg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581 581 -NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 650
Cdd:cd19504  100 aNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
491-655 1.30e-34

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: 129.58  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKalGLVTPA-GVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 569
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 570 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEAR--QQVFIMAATNRPDIIDPAILRpg 647
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                 ....*...
gi 341865581 648 RLDKTLFV 655
Cdd:cd19524  157 RFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
170-339 6.00e-33

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: 124.97  E-value: 6.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 170 NVKFEDVGGNDMTlKEVCK--MLIHMRHPEVYHHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 247
Cdd:cd19521    3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 248 SGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDP 327
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGN--DSQGVLVLGATNIPWQLDS 158
                        170
                 ....*....|..
gi 341865581 328 ALRRagRFDREI 339
Cdd:cd19521  159 AIRR--RFEKRI 168
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
491-655 4.56e-31

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: 119.40  E-value: 4.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMailapvRNP---DQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 567
Cdd:cd19507    1 DVGGLDNLKDWLKK------RKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 568 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglEARQQVFIMAATNRPDIIDPAILRP 646
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                 ....*....
gi 341865581 647 GRLDKTLFV 655
Cdd:cd19507  153 GRFDEIFFV 161
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
175-331 6.45e-31

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: 119.07  E-value: 6.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGND---MTLKEvcKMLIHMRHPEVYHHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 250
Cdd:cd19520    1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 251 SEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALR 330
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLST-DGNCRVIVMGATNRPQDLDEAIL 157

                 .
gi 341865581 331 R 331
Cdd:cd19520  158 R 158
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
2-72 7.62e-30

Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged helix motif. It binds nucleolin.


Pssm-ID: 465247  Cd Length: 70  Bit Score: 112.34  E-value: 7.62e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865581    2 KPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSiDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
171-339 1.08e-29

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: 116.24  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 171 VKFEDVGGNDM---TLKEVckMLIHMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 247
Cdd:cd19525   19 INWADIAGLEFakkTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 248 SGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLnNVAATARVLVIGATNRPDSLDP 327
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGA-TTSSEDRILVVGATNRPQEIDE 174
                        170
                 ....*....|..
gi 341865581 328 ALRRagRFDREI 339
Cdd:cd19525  175 AARR--RLVKRL 184
ycf46 CHL00195
Ycf46; Provisional
164-383 1.63e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 120.12  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 164 LEFQISNVKFEDVGGNDmtlkeVCKMLIHMRH---PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAA 240
Cdd:CHL00195 218 LEFYSVNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDV 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 241 PEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGAT 319
Cdd:CHL00195 293 GKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATA 367
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581 320 NRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRlP---QAFDFCHLAHLTPGFVGADL 383
Cdd:CHL00195 368 NNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIKKLSKLSNKFSGAEI 433
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
517-657 4.01e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 110.31  E-value: 4.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 517 KALGLVTPAGVLLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFD 590
Cdd:cd00009   12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFID 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581 591 EVDALCPRrsdretgASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGL 657
Cdd:cd00009   92 EIDSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
203-337 5.16e-28

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: 110.54  E-value: 5.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 203 GVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEID-AITPK 281
Cdd:cd19507   27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341865581 282 REVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDR 337
Cdd:cd19507  107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
206-339 1.13e-27

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: 110.07  E-value: 1.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 206 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA 285
Cdd:cd19522   32 PWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTS 111
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 286 SK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPALRRagRFDREI 339
Cdd:cd19522  112 EEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEALRR--RLEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
175-339 2.87e-27

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: 108.40  E-value: 2.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 253
Cdd:cd19524    1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 254 KLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRRag 333
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS-NGDDRVLVMGATNRPQELDDAVLR-- 156

                 ....*.
gi 341865581 334 RFDREI 339
Cdd:cd19524  157 RFTKRV 162
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
206-342 4.14e-27

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: 107.62  E-value: 4.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 206 PPRGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSGVSGESEQK---LRELFEQAVSNAPCIIFIDEIDAIT 279
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDSLS 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341865581 280 pkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGRFDREICLG 342
Cdd:cd00009   98 -----------RGAQNALLRVLETLNDlRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
196-339 3.04e-25

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: 102.95  E-value: 3.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 196 PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK-VAAPEIVSGVSGESEQKLRELFEQA---------VSN 265
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESEANIRKLFADAeeeqrrlgaNSG 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 266 APCIIFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNvaatarVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19504  104 LHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNN------ILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
430-668 5.68e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 106.26  E-value: 5.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 430 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVA-------LSSVQPSAKRE--------GFV 482
Cdd:CHL00195 144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATyktidenSIPLILEEKKQiisqteilEFY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 483 TVpNVTWADIGALEDIREELTmailapvRNPDQF--KAL--GLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGP 558
Cdd:CHL00195 222 SV-NEKISDIGGLDNLKDWLK-------KRSTSFskQASnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVG 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 559 ELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglEARQQVFIMAATNRPD 637
Cdd:CHL00195 294 KLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVATANNID 371
                        250       260       270
                 ....*....|....*....|....*....|.
gi 341865581 638 IIDPAILRPGRLDKTLFVGLPPPADRLAILK 668
Cdd:CHL00195 372 LLPLEILRKGRFDEIFFLDLPSLEEREKIFK 402
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
491-655 1.39e-21

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: 92.25  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 491 DIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPAILRpgR 648
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR--Y 156

                 ....*..
gi 341865581 649 LDKTLFV 655
Cdd:cd19523  157 FSKRLLV 163
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
175-331 8.03e-20

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 87.25  E-value: 8.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 175 DVGGNDM---TLKEvcKMLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 251
Cdd:cd19523    1 DIAGLGAlkaAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 252 EQKLRELFEQAVSNAPCIIFIDEIDAITPKReVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRR 331
Cdd:cd19523   78 EKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLG-SGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
206-345 1.83e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 85.50  E-value: 1.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581   206 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKV-----------------AAPEIVSGVSGESEQKLRELFEQAVSNAPC 268
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581   269 IIFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRFDREICLGIPD 345
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
193-339 8.01e-19

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: 83.94  E-value: 8.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 193 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESEQKLRELfeqavSNAP--CII 270
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN----LSEVVLTDDRLNHLL-----NTAPkqSII 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341865581 271 FIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19510   80 LLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALD---GVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
523-658 1.69e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581   523 TPAGVLLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 585
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581   586 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPgRLDKTLFVGLP 658
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
510-650 8.06e-13

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: 66.61  E-value: 8.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 510 VRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 588
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865581 589 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGL---EARqqVFIMaATNRPDIIDPAILRPGRLD 650
Cdd:cd19510   81 LEDIDAAFESREHNkknpsAYGGLSRVtFSGLLNALDGVassEER--IVFM-TTNHIERLDPALIRPGRVD 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
527-642 1.51e-12

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: 67.09  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 591
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 341865581 592 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPA 642
Cdd:cd19508  134 VESLAAARSASSSGTepsdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
201-339 5.19e-11

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 61.62  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 201 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA--------------APEIVSGVSGESEQKLRELFEQAVSNA 266
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341865581 267 PCIIFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCI 159
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
527-643 5.39e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 61.39  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 605
Cdd:cd19512   25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 341865581 606 ASVR-VVNQLLTEMdGLEARQQVFIMaATNRPDIIDPAI 643
Cdd:cd19512  104 EDLRaALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI 140
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
210-275 8.05e-11

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 64.72  E-value: 8.05e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVsgeseQKLRELFEQAVSNA----PCIIFIDEI 275
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA--VTSGV-----KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
210-275 2.37e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 2.37e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVSgeseqKLRELFEQA----VSNAPCIIFIDEI 275
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA--VTSGVK-----DIREVIEEArerrAYGRRTILFVDEI 114
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
208-329 1.42e-09

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 58.61  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 208 RGVLLHGPPGCGKTLLAHAIAGELDL---------PILKVAAPEIVSGVSGESEQKLRELF---EQAVSNAPCIIF--ID 273
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFqkiQELIDDKDALVFvlID 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 274 EIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 329
Cdd:cd19508  133 EVESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKR---YHNNVILLTSNLLEKIDVAF 189
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
208-336 1.53e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 57.15  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 208 RGVLLHGPPGCGKTLLAHAIA--GELDLPILKVA--APEIVSGVSgeseqKLRELFEQA-VSNAPCIIFIDEIDAITPKR 282
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLAlhSGMDYAIMTGGdvAPMGREGVT-----AIHKVFDWAnTSRRGLLLFVDEADAFLRKR 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341865581 283 --EVASKDMeRRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRraGRFD 336
Cdd:cd19512   98 stEKISEDL-RAALNAFLYRTGEQSN-----KFMLVLASNQPEQFDWAIN--DRID 145
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
366-405 2.49e-09

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: 53.31  E-value: 2.49e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 341865581  366 FDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLMKLQEQ 405
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
519-651 5.85e-09

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 55.84  E-value: 5.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 519 LGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 584
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341865581 585 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLEARQQVFImAATNRPDIIDPAILRPGRLDK 651
Cdd:cd19505   87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
205-281 1.06e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 58.39  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 205 VPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAApeivsgvsgeSEQKLRELFEQAVSNAPC----------IIFIDE 274
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNA----------SDQRTADVIERVAGEAATsgslfgarrkLILLDE 106

                 ....*..
gi 341865581 275 IDAITPK 281
Cdd:PRK04195 107 VDGIHGN 113
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
210-391 3.77e-08

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 55.56  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAA-----PEIVSGVS------GESEQKLRELFEQavsnapcIIFIDEIDAI 278
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllPSDILGTYiydqqtGEFEFRPGPLFAN-------VLLADEINRA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 279 TPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS-----LDPALRRagRFDREICLGIPDEA 347
Cdd:COG0714  107 PPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYPDAE 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 341865581 348 SRERILqtlcrklrlpQAFDFCHLAHLTPGFVGADLMALCREAA 391
Cdd:COG0714  174 EEREIL----------RRHTGRHLAEVEPVLSPEELLALQELVR 207
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
205-335 5.09e-08

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: 53.54  E-value: 5.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 205 VPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEI--VSGVSGESEQKLRELFEQavsnapcIIFIDEIDAITPKR 282
Cdd:cd19498   44 VTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVEG-------IVFIDEIDKIAKRG 116
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581 283 EVASKDMERRIVAQLL------TCMDDLNNVAATARVLVIGA----TNRPDSLDPALRraGRF 335
Cdd:cd19498  117 GSSGPDVSREGVQRDLlpivegSTVSTKYGPVKTDHILFIAAgafhVAKPSDLIPELQ--GRF 177
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
682-739 9.13e-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: 48.69  E-value: 9.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341865581  682 DVNLEAIAGdlRCDCYTGADLSALVREASICALRQEMArqksgnekgelKVSHKHFEE 739
Cdd:pfam17862   1 DVDLEELAE--RTEGFSGADLEALCREAALAALRRGLE-----------AVTQEDLEE 45
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
528-629 7.40e-07

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 52.54  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  528 LLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRRS 600
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY 392
                          90       100
                  ....*....|....*....|....*....
gi 341865581  601 DRETGASVRVVNQLLTEMDGLEARQQVFI 629
Cdd:TIGR03922 393 GQKDPFGLEAIDTLLARMENDRDRLVVIG 421
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
527-597 1.02e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 51.62  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 592
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                         90
                 ....*....|
gi 341865581 593 -----DALCP 597
Cdd:PRK13342 105 nkaqqDALLP 114
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
209-335 1.04e-06

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: 48.44  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  209 GVLLHGPPGCGKTLLAHAIAGELD-LPILKVAAP------EIVSGVsgESEQKLRELFEQAVSNA---PCIIFIDEIDAI 278
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRR--NIDPGGASWVDGPLVRAareGEIAVLDEINRA 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  279 TPKrevaskdmerrIVAQLLTCMDD----LNN-----VAATARVLVIGATNRPD----SLDPALRRagRF 335
Cdd:pfam07728  79 NPD-----------VLNSLLSLLDErrllLPDggelvKAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
527-597 1.69e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.21  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFDEV--- 592
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVDEIhrf 117
                         90
                 ....*....|
gi 341865581 593 -----DALCP 597
Cdd:COG2256  118 nkaqqDALLP 127
PRK04195 PRK04195
replication factor C large subunit; Provisional
527-693 2.40e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.69  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 598
Cdd:PRK04195  42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 599 RSDReTGAS--VRVVNqlltemdglEARQQVfIMAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--LAILKTITKN- 673
Cdd:PRK04195 113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                        170       180
                 ....*....|....*....|....
gi 341865581 674 GTKPPLDAdvnLEAIA----GDLR 693
Cdd:PRK04195 177 GIECDDEA---LKEIAersgGDLR 197
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
527-689 2.48e-06

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: 49.78  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESERAVRQ--VFQRaknsapcVIFFDEVDal 595
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGEFEFRPgpLFAN-------VLLADEIN-- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 596 cprRSDRETGASvrvvnqLLTEMdgleARQQV-------------FIMAATNRPDIID-----PAILRpgRLDKTLFVGL 657
Cdd:COG0714  105 ---RAPPKTQSA------LLEAM----EERQVtipggtyklpepfLVIATQNPIEQEGtyplpEAQLD--RFLLKLYIGY 169
                        170       180       190
                 ....*....|....*....|....*....|..
gi 341865581 658 PPPADRLAILKTiTKNGTKPPLDADVNLEAIA 689
Cdd:COG0714  170 PDAEEEREILRR-HTGRHLAEVEPVLSPEELL 200
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
210-335 3.29e-06

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: 47.49  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSgvSGESEQKLRELFEQAVsnapciIFIDEIDAITPK-REVASKD 288
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIER--PGDLAAILTNLEPGDV------LFIDEIHRLNRAvEEILYPA 107
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 341865581  289 MERRivaqlltCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 335
Cdd:pfam05496 108 MEDF-------RLDIVIGKGPSARSIrldlppftLVGATTRAGLLTSPLR--DRF 153
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
208-339 4.07e-06

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: 50.23  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  208 RGVLLHGPPGCGKTLLAHAIA------GELDLP-ILKVAAPEIVSGVSGESEQKLRELFEQAVSNapcIIFIDEIDAITP 280
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341865581  281 KREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPD-----SLDPALRRagRFDREI 339
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMENDRD-----RLVVIGAGYRKDldkflEVNEGLRS--RFTRVI 446
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
208-266 4.45e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 49.97  E-value: 4.45e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865581 208 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSgvsgeSEQKLRELFEQAVSNA 266
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYS-----AELKKTEFLMQALRKA 120
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
210-283 4.99e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 48.75  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV-SGVSGES-EQKLRELFEQA---VSNAP-CIIFIDEIDAITPKRE 283
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvENILLKLLQAAdydVERAQrGIVYIDEIDKIARKSE 132
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
207-330 5.82e-06

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 48.82  E-value: 5.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 207 PRGVLLHGPPGCGKTLLAHAIAGEL-------DLPILKVAAPEIVSGVSGEseqkLRELFEQAVSNApciIFIDEIDAIT 279
Cdd:COG0470   18 PHALLLHGPPGIGKTTLALALARDLlcenpegGKACGQCHSRLMAAGNHPD----LLELNPEEKSDQ---IGIDQIRELG 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865581 280 PKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPALR 330
Cdd:COG0470   91 EFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTIR 149
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
527-560 1.20e-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: 1.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 341865581  527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 560
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
526-645 1.93e-05

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: 44.98  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  526 GVLLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 593
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341865581  594 alcprRSDRETgasVRVVNQLLTE-----MDGLE----ARQQVFIMAATNRPDI----IDPAILR 645
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS 133
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
208-326 4.70e-05

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: 44.44  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 208 RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES--EQKLRELFEQAVSNAPCIIFIDEIDAI----TPK 281
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTfykkVPK 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 341865581 282 REvasKDMERRIVAQLLTCMddLNNVAATARVLVIGATNRPDSLD 326
Cdd:cd19506  107 TE---KQLDPKRLKKDLPKI--LKSLKPEDRVLIVGTTSRPFEAD 146
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
527-560 4.99e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.28  E-value: 4.99e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 560
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
208-263 5.39e-05

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: 46.15  E-value: 5.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341865581  208 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSGVSGESEQkLRELFEQAV 263
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTEA-LTQAFRKAI 107
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
488-560 6.15e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 45.75  E-value: 6.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865581  488 TWADIGALEDIREELTMAILAPVRNPDQfkalglvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 560
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
210-280 6.79e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 6.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQK-------LRELFEQAVsnapciIFIDEIDAITP 280
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL---------EKpgdlaaiLTNLEEGDV------LFIDEIHRLSP 116
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
210-335 7.27e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 45.37  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFeQAVSN--APCIIFIDEIDAITPK-REVAS 286
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLA-AILTNleEGDVLFIDEIHRLSPAvEELLY 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581  287 KDMERrivaqllTCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 335
Cdd:TIGR00635 103 PAMED-------FRLDIVIGKGPSARSVrldlppftLVGATTRAGMLTSPLR--DRF 150
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
40-275 7.49e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.92  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  40 QRVYSIDYGRRKRNAFRIQVEKVFSIISSEKELKNLTELEDEHLAKRARQGEEDNEYTESYSDDDSSMEDYPDPQDSKDS 119
Cdd:COG1401   58 DRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 120 SLLESDMKRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQisnvkfEDVGGNDMTLKEVCKMLIHMRHPEVY 199
Cdd:COG1401  138 LLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAE------ELYSEDLESEDDYLKDLLREKFEETL 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 200 H--HLGVVPPRGVLLHGPPGCGKT----LLAHAIAGELDLPILKVAA------PEIVSG-VSGESEQKLR---ELFEQAV 263
Cdd:COG1401  212 EafLAALKTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVQFhpswsyEDFLLGyRPSLDEGKYEptpGIFLRFC 291
                        250
                 ....*....|....*...
gi 341865581 264 SNA------PCIIFIDEI 275
Cdd:COG1401  292 LKAeknpdkPYVLIIDEI 309
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
526-579 1.32e-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: 44.99  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341865581  526 GVLLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 579
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
210-235 1.94e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 44.30  E-value: 1.94e-04
                         10        20
                 ....*....|....*....|....*.
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPI 235
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
497-636 2.12e-04

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 42.51  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 497 DIREELTMAILAPVRNPDQFKALGLVTpaGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQ 574
Cdd:cd19506    1 DVRQLLTLYGILPLGSQAVHEKAPLVK--SLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341865581 575 VFQRAKNSAPCVIFFDEVDALCPR---RSDRETGASvRVVNQLLTEMDGLEARQQVFIMAATNRP 636
Cdd:cd19506   79 VLKVARQLQPSVIWIGDAEKTFYKkvpKTEKQLDPK-RLKKDLPKILKSLKPEDRVLIVGTTSRP 142
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
528-593 2.17e-04

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: 42.55  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 528 LLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIFFDEV 592
Cdd:cd19499   45 LFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVLLDEI 122

                 .
gi 341865581 593 D 593
Cdd:cd19499  123 E 123
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
527-597 2.39e-04

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: 42.57  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  527 VLLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 588
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 341865581  589 FDEVDALCP 597
Cdd:pfam07724  81 IDEIEKAHP 89
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
461-598 3.73e-04

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: 41.98  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 461 ELNDFIVAlssvQPSAKREGFVTVPNvTWADIGALEDIREEltmailapvrnpdqfkalglVTPAGVLLAGPPGCGKTLL 540
Cdd:cd19498    8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDE--------------------VTPKNILMIGPTGVGKTEI 62
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 341865581 541 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 598
Cdd:cd19498   63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
527-558 3.91e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 43.15  E-value: 3.91e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 341865581 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGP 558
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
PRK08116 PRK08116
hypothetical protein; Validated
208-277 3.96e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 43.09  E-value: 3.96e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341865581 208 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVS---GVSGESEQKLRELFEQAVSNAPCIIfIDEIDA 277
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANELiekGVPVIFVNFPQLLNrikSTYKSSGKEDENEIIRSLVNADLLI-LDDLGA 189
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
526-573 4.41e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.42  E-value: 4.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 341865581 526 GVLLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 573
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
210-326 4.97e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.56  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 210 VLLHGPPGCGKTLLAHAIAGELDLPILKVAapeIVSGVSGESEQKLRELFEqavsNAPCIIFIDEIDAITPKREVASKDM 289
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVI---FISFLDTILEAIEDLIEE----KKLDIIIIDSLSSLARASQGDRSSE 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 341865581 290 ERRIVAQLLtcmddlnNVAATARVLVIgATNRPDSLD 326
Cdd:cd01120   74 LLEDLAKLL-------RAARNTGITVI-ATIHSDKFD 102
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
210-280 6.42e-04

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: 41.03  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  210 VLLHGPPGCGKTLLAHAIAGELD-----LPI--------------LKVAAPEIVSgvSGESEQklreLFEQAVSNAPCII 270
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFgderaLIRidmseymeehsvsrLIGAPPGYVG--YEEGGQ----LTEAVRRKPYSIV 79
                          90
                  ....*....|
gi 341865581  271 FIDEIDAITP 280
Cdd:pfam07724  80 LIDEIEKAHP 89
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
211-279 9.57e-04

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: 41.00  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 211 LLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESE-----------------QKLRelfeQAVSNAPcIIFID 273
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEirghrrtyvgampgriiQALK----KAGTNNP-VFLLD 111

                 ....*.
gi 341865581 274 EIDAIT 279
Cdd:cd19500  112 EIDKIG 117
AAA_22 pfam13401
AAA domain;
210-281 1.03e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581  210 VLLHGPPGCGKTLLAHAIAGELDL---PILKVAAPE---------------IVSGVSGESEQKLRELFEQAVS--NAPCI 269
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSgtspkdllrallralGLPLSGRLSKEELLAALQQLLLalAVAVV 87
                          90
                  ....*....|..
gi 341865581  270 IFIDEIDAITPK 281
Cdd:pfam13401  88 LIIDEAQHLSLE 99
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
208-286 2.05e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.53  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 208 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSG-VSGESEQKLRELFEQaVSNAPCIIfIDEIDAITPKRE 283
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVNElKEARADGRLERLLKR-LAKVDLLI-LDELGYLPLDAE 177

                 ...
gi 341865581 284 VAS 286
Cdd:COG1484  178 GAE 180
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
210-231 3.08e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.58  E-value: 3.08e-03
                          10        20
                  ....*....|....*....|..
gi 341865581  210 VLLHGPPGCGKTLLAHAIAGEL 231
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL 22
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
527-645 6.01e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.99  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 527 VLLAGPPGCGKTLLAKAVANE----SGlnFISVKGPELLNMYVGESERAVRQVFQ------------RAKNSAPCVIFFD 590
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAGLlkptSG--EILIDGKDIAKLPLEELRRRIGYVPQlsggqrqrvalaRALLLNPDLLLLD 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341865581 591 EVD-ALcprrsDRETGASVRvvnQLLTEMdgleARQQVFIMAATNRPDIIDPAILR 645
Cdd:cd00267  106 EPTsGL-----DPASRERLL---ELLREL----AEEGRTVIIVTHDPELAELAADR 149
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
528-595 6.62e-03

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: 38.31  E-value: 6.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865581 528 LLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 595
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
207-361 8.07e-03

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.74  E-value: 8.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 207 PRG--VLLHGPPGCGKTLLAHAIAGELdlpilkVAAPE---IVSgvSGESEQKLREL-------FEQAVSNApCIIFIDe 274
Cdd:COG0467   18 PRGssTLLSGPPGTGKTTLALQFLAEG------LRRGEkglYVS--FEESPEQLLRRaeslgldLEEYIESG-LLRIID- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865581 275 idaITPKREVASKDMerrIVAQLLTCMDDLNnvaatARVLVIgatnrpDSLDPalrragrfdreICLGIPDEASRERILQ 354
Cdd:COG0467   88 ---LSPEELGLDLEE---LLARLREAVEEFG-----AKRVVI------DSLSG-----------LLLALPDPERLREFLH 139

                 ....*..
gi 341865581 355 TLCRKLR 361
Cdd:COG0467  140 RLLRYLK 146
 
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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