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Conserved domains on  [gi|1034558874|ref|XP_016856874|]
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nuclear valosin-containing protein-like isoform X9 [Homo sapiens]

Protein Classification

CDC48 family AAA ATPase( domain architecture ID 13875340)

CDC48 family AAA ATPase is involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus; similar to yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-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 ...
 277-755 4.84e-142

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: 434.72  E-value: 4.84e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 277 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 355
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 356 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 435
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 436 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 515
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 516 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPskgvqeerlgteptSETQDELQrllgl 595
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIP--------------AEVLKELK----- 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 596 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 675
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 676 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
 2-72 8.66e-31

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: 115.03  E-value: 8.66e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034558874   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 ...
 277-755 4.84e-142

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: 434.72  E-value: 4.84e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 277 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 355
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 356 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 435
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 436 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 515
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 516 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPskgvqeerlgteptSETQDELQrllgl 595
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIP--------------AEVLKELK----- 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 596 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 675
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 676 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 300-493 2.90e-102

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: 311.26  E-value: 2.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGNDMTLKEVCKMLIHM-RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppas 378
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAG------------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 379 asqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 458
Cdd:cd19518    57 ---ELKVPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNN 133

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034558874 459 VA-ATARVLVIGATNRPDSLDPALRRAGRFDREICL 493
Cdd:cd19518   134 EKtAGGPVLVIGATNRPDSLDPALRRAGRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 252-547 1.89e-84

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 270.72  E-value: 1.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 252 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVV 330
Cdd:COG1222    31 LLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 331 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLREL 410
Cdd:COG1222   111 PPKGVLLYGPPGTGKTLLAKAVAG---------------------------ELGAPFIRVRGSELVSKYIGEGARNVREV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 411 FEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDR 489
Cdd:COG1222   164 FELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATNRPDLLDPALLRPGRFDR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874 490 EICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 547
Cdd:COG1222   241 VIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 276-547 2.14e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 211.61  E-value: 2.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 276 IEAVLQKKAKARGLEFQIS---NVKFEDVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAH 350
Cdd:PRK03992  105 IVEVLPSEKDPRVQAMEVIespNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAK 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 351 AIAGAecsgmitAHCSFdfsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAI 430
Cdd:PRK03992  184 AVAHE-------TNATF--------------------IRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 431 TPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQT 507
Cdd:PRK03992  237 AAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---RGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKI 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034558874 508 LCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 547
Cdd:PRK03992  314 HTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 335-494 3.14e-49

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: 168.93  E-value: 3.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQA 414
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVA---------------------------KELGAPFIEISGSELVSKYVGESEKRLRELFEAA 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 415 VSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREICLG 494
Cdd:pfam00004  54 KKLAPCVIFIDEIDALAGSRGSGGDSESRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
cell_div_CdvC NF041006
cell division protein CdvC;
252-566 3.88e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.56  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 252 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHh 326
Cdd:NF041006   66 KRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKEALKEaivypSKRPDLFP- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 327 LGVvpPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQK 406
Cdd:NF041006  131 LGW--PRGILLYGPPGCGKTMLAAAVA---------------------------NEIDSEFIHVDAASIMSKWLGEAEKN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 407 LRELFEQA-----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD- 478
Cdd:NF041006  182 VAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDe 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 479 PALRragRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQ 558
Cdd:NF041006  259 PFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGE 334


                  ....*...
gi 1034558874 559 KKNPEMED 566
Cdd:NF041006  335 PRPITMED 342
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
 2-72 8.66e-31

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: 115.03  E-value: 8.66e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034558874   2 KPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSiDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
cell_div_CdvC NF041006
cell division protein CdvC;
637-747 2.36e-27

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 114.45  E-value: 2.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 716
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558874 717 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDAL 747
Cdd:NF041006  175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDAL 210
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 331-497 3.22e-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: 84.73  E-value: 3.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  331 PPRGVLLHGPPGCGKTLLAHAIAG---AECSGMITAHCSFDFSGsndppasasqeldLPILKVAAPEIVSGVSGESEQKL 407
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEE-------------VLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  408 RELFEQAVSNAPCIIFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRF 487
Cdd:smart00382  68 RLALALARKLKPDVLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RF 138

                          170
                   ....*....|
gi 1034558874  488 DREICLGIPD 497
Cdd:smart00382 139 DRRIVLLLIL 148
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 277-755 4.84e-142

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: 434.72  E-value: 4.84e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 277 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 355
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 356 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 435
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 436 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 515
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 516 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPskgvqeerlgteptSETQDELQrllgl 595
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIP--------------AEVLKELK----- 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 596 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 675
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 676 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 300-493 2.90e-102

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: 311.26  E-value: 2.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGNDMTLKEVCKMLIHM-RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppas 378
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAG------------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 379 asqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 458
Cdd:cd19518    57 ---ELKVPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNN 133

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034558874 459 VA-ATARVLVIGATNRPDSLDPALRRAGRFDREICL 493
Cdd:cd19518   134 EKtAGGPVLVIGATNRPDSLDPALRRAGRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 252-547 1.89e-84

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 270.72  E-value: 1.89e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 252 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVV 330
Cdd:COG1222    31 LLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 331 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLREL 410
Cdd:COG1222   111 PPKGVLLYGPPGTGKTLLAKAVAG---------------------------ELGAPFIRVRGSELVSKYIGEGARNVREV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 411 FEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDR 489
Cdd:COG1222   164 FELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATNRPDLLDPALLRPGRFDR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874 490 EICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 547
Cdd:COG1222   241 VIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 300-493 1.37e-73

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: 236.03  E-value: 1.37e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppa 377
Cdd:cd19503     1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVA------------------------ 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 378 sasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLN 457
Cdd:cd19503    56 ---NEAGANFLSISGPSIVSKYLGESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMS 132

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034558874 458 NvaaTARVLVIGATNRPDSLDPALRRAGRFDREICL 493
Cdd:cd19503   133 S---RGKVVVIAATNRPDAIDPALRRPGRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 291-567 1.85e-69

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: 233.65  E-value: 1.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 291 FQISNVKFEDVGGNDMTLKEVCKMLIHMRH-PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdf 369
Cdd:COG0464   149 LELREAILDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAG--------------- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 370 sgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQL 449
Cdd:COG0464   214 ------------ELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTL 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 450 LTCMDDLNNvaataRVLVIGATNRPDSLDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPG 529
Cdd:COG0464   282 LTEMEELRS-----DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEG 354

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034558874 530 FVGADLMALCREAAMCAVnrvlmklqEQQKKNPEMEDL 567
Cdd:COG0464   355 LSGADIRNVVRRAALQAL--------RLGREPVTTEDL 384
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 647-755 6.00e-68

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: 220.82  E-value: 6.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 647 LEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 726
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1034558874 727 VFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGG 109
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 300-494 2.07e-62

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: 206.52  E-value: 2.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppas 378
Cdd:cd19519     1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVA------------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 379 asQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNn 458
Cdd:cd19519    56 --NETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK- 132

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034558874 459 vaATARVLVIGATNRPDSLDPALRRAGRFDREICLG 494
Cdd:cd19519   133 --QRAHVIVMAATNRPNSIDPALRRFGRFDREIDIG 166
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 276-547 2.14e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 211.61  E-value: 2.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 276 IEAVLQKKAKARGLEFQIS---NVKFEDVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAH 350
Cdd:PRK03992  105 IVEVLPSEKDPRVQAMEVIespNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAK 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 351 AIAGAecsgmitAHCSFdfsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAI 430
Cdd:PRK03992  184 AVAHE-------TNATF--------------------IRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 431 TPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQT 507
Cdd:PRK03992  237 AAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---RGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKI 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034558874 508 LCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 547
Cdd:PRK03992  314 HTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 283-549 2.18e-59

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: 209.06  E-value: 2.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 283 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmit 362
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAG-------- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 363 ahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE---VASK 439
Cdd:TIGR01241 111 -------------------EAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 440 DMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFD 519
Cdd:TIGR01241 172 DEREQTLNQLLVEMDGFGT---NTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248

                         250       260       270
                  ....*....|....*....|....*....|
gi 1034558874 520 FCHLAHLTPGFVGADLMALCREAAMCAVNR 549
Cdd:TIGR01241 249 LKAVARRTPGFSGADLANLLNEAALLAARK 278
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 650-754 5.13e-59

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: 196.74  E-value: 5.13e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 650 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 729
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                          90       100
                  ....*....|....*....|....*
gi 1034558874 730 RAKNSAPCVIFFDEVDALCPRRSDR 754
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQS 105
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 287-631 9.09e-59

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: 212.46  E-value: 9.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 287 RGLEFQISNVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmi 361
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGG----LEEVKQELREavewpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATE------ 510

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 362 tahcsfdfSGSNdppasasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA-SKD 440
Cdd:TIGR01243 511 --------SGAN-------------FIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTS 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 441 MERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDF 520
Cdd:TIGR01243 570 VTDRIVNQLLTEMDGIQELSN---VVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL 646

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 521 CHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqeqqkknpemedlpsKGVQEERLGTEptsetqdelqrllgllrdqd 600
Cdd:TIGR01243 647 EELAEMTEGYTGADIEAVCREAAMAALRESI------------------GSPAKEKLEVG-------------------- 688

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1034558874 601 plSEEQMQGLCIELNDFIVALSSVQPSAKRE 631
Cdd:TIGR01243 689 --EEEFLKDLKVEMRHFLEALKKVKPSVSKE 717
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
283-567 2.49e-57

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 205.66  E-value: 2.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 283 KAKARGLEFQISNVKFEDVGGND---MTLKEVCKMLihmRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaEcsg 359
Cdd:COG0465   126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAG-E--- 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 360 mitAHCSFdFSgsndppASASqeldlpilkvaapEIVS---GVsGESeqKLRELFEQAVSNAPCIIFIDEIDAITPKREV 436
Cdd:COG0465   199 ---AGVPF-FS------ISGS-------------DFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGA 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 437 A---SKDmER-RIVAQLLTCMD--DlnnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCR 510
Cdd:COG0465   253 GlggGHD-EReQTLNQLLVEMDgfE-----GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHAR 326

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034558874 511 KLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRvlmklqeqQKKNPEMEDL 567
Cdd:COG0465   327 KKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARR--------NKKAVTMEDF 375
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 572-753 2.83e-55

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 192.91  E-value: 2.83e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 572 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 651
Cdd:COG1222    12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 652 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 731
Cdd:COG1222    88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167

                         170       180
                  ....*....|....*....|..
gi 1034558874 732 KNSAPCVIFFDEVDALCPRRSD 753
Cdd:COG1222   168 REKAPSIIFIDEIDAIAARRTD 189
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
298-542 8.06e-54

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 185.86  E-value: 8.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 298 FEDVGGNDmTLKEVCKMLIH-MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndpp 376
Cdd:COG1223     1 LDDVVGQE-EAKKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAG---------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 377 asasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAvSNAPCIIFIDEIDAITPKREVASKDME-RRIVAQLLTCMDD 455
Cdd:COG1223    58 -----ELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDG 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 456 LNNvaataRVLVIGATNRPDSLDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADL 535
Cdd:COG1223   132 LPS-----GSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADI 204


                  ....*..
gi 1034558874 536 MALCREA 542
Cdd:COG1223   205 EKVLKTA 211
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 317-491 3.37e-51

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 175.55  E-value: 3.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 317 HMRHPEVyHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIV 396
Cdd:cd19481    12 PRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAG---------------------------ELGLPLIVVKLSSLL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 397 SGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPD 475
Cdd:cd19481    64 SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPD 140

                         170
                  ....*....|....*.
gi 1034558874 476 SLDPALRRAGRFDREI 491
Cdd:cd19481   141 LLDPALLRPGRFDEVI 156
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 308-491 1.60e-50

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: 173.62  E-value: 1.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 308 LKEVCKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmiTAHCSFdfsgsndppasasqeldl 385
Cdd:cd19511     1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALAS-------EAGLNF------------------ 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 386 piLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATAR 464
Cdd:cd19511    56 --ISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKG 130

                         170       180
                  ....*....|....*....|....*..
gi 1034558874 465 VLVIGATNRPDSLDPALRRAGRFDREI 491
Cdd:cd19511   131 VVVIAATNRPDMIDPALLRPGRLDKLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 335-494 3.14e-49

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: 168.93  E-value: 3.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQA 414
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVA---------------------------KELGAPFIEISGSELVSKYVGESEKRLRELFEAA 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 415 VSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREICLG 494
Cdd:pfam00004  54 KKLAPCVIFIDEIDALAGSRGSGGDSESRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
283-559 3.42e-49

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 183.70  E-value: 3.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 283 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmit 362
Cdd:PRK10733  136 KSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAG-------- 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 363 ahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SK 439
Cdd:PRK10733  208 -------------------EAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlggGH 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 440 DMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFD 519
Cdd:PRK10733  269 DEREQTLNQMLVEMDGFE---GNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDID 345

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034558874 520 FCHLAHLTPGFVGADLMALCREAAMCAV--NRVLMKLQEQQK 559
Cdd:PRK10733  346 AAIIARGTPGFSGADLANLVNEAALFAArgNKRVVSMVEFEK 387
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 296-491 2.46e-47

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: 165.48  E-value: 2.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 296 VKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndp 375
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAG--------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 376 pasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SKDMERRIVAQLLTC 452
Cdd:cd19501    60 ------EAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVE 133

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034558874 453 MDDLnnvAATARVLVIGATNRPDSLDPALRRAGRFDREI 491
Cdd:cd19501   134 MDGF---ESNTGVIVIAATNRPDVLDPALLRPGRFDRQV 169
ftsH CHL00176
cell division protein; Validated
 274-549 4.61e-47

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 177.55  E-value: 4.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 274 GEIEAVLQKKAKarglefqiSNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIA 353
Cdd:CHL00176  166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 354 GaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPK 433
Cdd:CHL00176  238 G---------------------------EAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQ 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 434 R--EVASKDMER-RIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCR 510
Cdd:CHL00176  291 RgaGIGGGNDEReQTLNQLLTEMDGFK---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHAR 367

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034558874 511 KLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNR 549
Cdd:CHL00176  368 NKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARR 406
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 295-549 7.46e-47

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 171.48  E-value: 7.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 295 NVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitaHCSFDFsgsn 373
Cdd:PTZ00454  141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAH---------HTTATF---- 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 374 dppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMER---RIVAQLL 450
Cdd:PTZ00454  208 --------------IRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELL 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 451 TCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGF 530
Cdd:PTZ00454  274 NQMDGFDQ---TTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKI 350

                         250
                  ....*....|....*....
gi 1034558874 531 VGADLMALCREAAMCAVNR 549
Cdd:PTZ00454  351 SAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 298-491 1.62e-46

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 163.28  E-value: 1.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 298 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmiTAHCSFdfsgsndpp 376
Cdd:cd19502     2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVAN-------HTDATF--------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 377 asasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDME-RRIVAQLLTCM 453
Cdd:cd19502    66 -----------IRVVGSELVQKYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQL 134

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034558874 454 DDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREI 491
Cdd:cd19502   135 DGFD---PRGNIKVIMATNRPDILDPALLRPGRFDRKI 169
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 563-753 1.42e-45

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: 168.17  E-value: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 563 EMEDLPSKGVQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREGFVTVPNVTWA 642
Cdd:COG0464    78 LLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 722
Cdd:COG0464   158 DLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEK 237

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034558874 723 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:COG0464   238 NLREVFDKARGLAPCVLFIDEADALAGKRGE 268
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 318-491 6.30e-45

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: 158.43  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 318 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahcsfdfSGSNdppasasqeldlpILKVAAPEIVS 397
Cdd:cd19529    13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE--------------SNAN-------------FISVKGPELLS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 398 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDS 476
Cdd:cd19529    66 KWVGESEKAIREIFRKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDI 142

                         170
                  ....*....|....*
gi 1034558874 477 LDPALRRAGRFDREI 491
Cdd:cd19529   143 IDPALLRAGRFDRLI 157
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 643-756 8.48e-45

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: 158.22  E-value: 8.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 722
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034558874 723 AVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDREE 756
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKReEDQRE 115
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 650-751 3.42e-43

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: 153.42  E-value: 3.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 650 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 729
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100
                  ....*....|....*....|..
gi 1034558874 730 RAKNSAPCVIFFDEVDALCPRR 751
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRR 102
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 298-563 4.77e-43

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 161.86  E-value: 4.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 298 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsNDPP 376
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVA-------------------NETS 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 377 ASasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDL 456
Cdd:PTZ00361  243 AT--------FLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQL 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 457 NNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLM 536
Cdd:PTZ00361  315 DGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIK 394

                         250       260
                  ....*....|....*....|....*...
gi 1034558874 537 ALCREAAMCAVNRVLMKL-QEQQKKNPE 563
Cdd:PTZ00361  395 AICTEAGLLALRERRMKVtQADFRKAKE 422
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 300-490 7.13e-43

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: 153.05  E-value: 7.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGND---MTLKEVckMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgAECSgmitahcsfdfsgsndpp 376
Cdd:cd19517     1 DIGGLShyiNQLKEM--VFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALA-AECS------------------ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 377 aSASQELDLPILKVAapEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDL 456
Cdd:cd19517    60 -KGGQKVSFFMRKGA--DCLSKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGL 136

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034558874 457 NNvaaTARVLVIGATNRPDSLDPALRRAGRFDRE 490
Cdd:cd19517   137 DN---RGQVVVIGATNRPDALDPALRRPGRFDRE 167
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 320-491 2.07e-40

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: 145.73  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 320 HPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitaHCSFDFsgsndppasasqeldlpiLKVAAPEIVSGV 399
Cdd:cd19528    15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIAN---------ECQANF------------------ISVKGPELLTMW 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 400 SGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDS 476
Cdd:cd19528    68 FGESEANVRDIFDKARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDI 144

                         170
                  ....*....|....*
gi 1034558874 477 LDPALRRAGRFDREI 491
Cdd:cd19528   145 IDPAILRPGRLDQLI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 650-752 3.82e-40

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: 144.96  E-value: 3.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 650 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 729
Cdd:cd19528     1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                          90       100
                  ....*....|....*....|...
gi 1034558874 730 RAKNSAPCVIFFDEVDALCPRRS 752
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARG 103
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 640-753 6.41e-39

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: 142.09  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 640 TWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 719
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034558874 720 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFD 114
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 318-489 6.98e-39

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: 141.47  E-value: 6.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 318 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahcsfdfSGSNdppasasqeldlpILKVAAPEIVS 397
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANE--------------SGAN-------------FISVKGPELLN 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 398 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSL 477
Cdd:cd19530    69 KYVGESERAVRQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDII 145

                         170
                  ....*....|..
gi 1034558874 478 DPALRRAGRFDR 489
Cdd:cd19530   146 DPAMLRPGRLDK 157
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 637-753 7.73e-39

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 148.44  E-value: 7.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 716
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034558874 717 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:PRK03992  206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTD 242
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 650-751 1.53e-38

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: 140.26  E-value: 1.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 650 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 729
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100
                  ....*....|....*....|..
gi 1034558874 730 RAKNSAPCVIFFDEVDALCPRR 751
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKR 102
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 646-753 1.26e-37

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: 137.80  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 646 ALEDIREeltmaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 725
Cdd:cd19481     1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75

                          90       100
                  ....*....|....*....|....*...
gi 1034558874 726 QVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:cd19481    76 KIFERARRLAPCILFIDEIDAIGRKRDS 103
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 650-751 3.60e-37

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: 136.49  E-value: 3.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 650 IREELTMAILAPVRNPDQFkALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 729
Cdd:cd19527     1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79

                          90       100
                  ....*....|....*....|..
gi 1034558874 730 RAKNSAPCVIFFDEVDALCPRR 751
Cdd:cd19527    80 KARDAKPCVIFFDELDSLAPSR 101
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 319-491 5.42e-37

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: 136.02  E-value: 5.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 319 RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahCSFDFsgsndppasasqeldlpiLKVAAPEIVSG 398
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASE---------CGLNF------------------ISVKGPELLNK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 399 VSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLD 478
Cdd:cd19526    67 YIGASEQNVRDLFSRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLD---GVEGLDGVYVLAATSRPDLID 143

                         170
                  ....*....|...
gi 1034558874 479 PALRRAGRFDREI 491
Cdd:cd19526   144 PALLRPGRLDKLV 156
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 276-505 1.24e-36

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: 144.85  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 276 IEAVLQKKAKARGLEfQISNVKFEDVGGNDMTLKevckmLIH------MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLA 349
Cdd:TIGR03689 160 FEAIPRTEVEDLVLE-EVPDVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 350 HAIAGAECSGMitahcsfdFSGSNDPPAsasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNA----PCIIFID 425
Cdd:TIGR03689 234 KAVANSLAARI--------GAEGGGKSY---------FLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFD 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 426 EIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERI 504
Cdd:TIGR03689 297 EMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADI 373


                  .
gi 1034558874 505 L 505
Cdd:TIGR03689 374 F 374
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 594-747 2.69e-36

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: 143.70  E-value: 2.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 594 GLLRDQDPLSEEQMQGLCIELndfiVALSSVQPSAKREgfvtVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGL 673
Cdd:TIGR03689 142 EGLRPGDTLLVDPRAGYAFEA----IPRTEVEDLVLEE----VPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGL 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 674 VTPAGVLLAGPPGCGKTLLAKAVAN-------ESGLN---FISVKGPELLNMYVGESERAVRQVFQRAKNSA----PCVI 739
Cdd:TIGR03689 214 KPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIV 293


                  ....*...
gi 1034558874 740 FFDEVDAL 747
Cdd:TIGR03689 294 FFDEMDSL 301
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 679-756 1.27e-35

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: 131.18  E-value: 1.27e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDREE 756
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGD 78
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 639-752 2.08e-35

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: 131.97  E-value: 2.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 639 VTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 718
Cdd:cd19501     1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034558874 719 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRS 752
Cdd:cd19501    80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRG 113
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 643-751 3.31e-35

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: 131.37  E-value: 3.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 722
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100
                  ....*....|....*....|....*....
gi 1034558874 723 AVRQVFQRAKNSAPCVIFFDEVDALCPRR 751
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKR 109
cell_div_CdvC NF041006
cell division protein CdvC;
252-566 3.88e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.56  E-value: 3.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 252 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHh 326
Cdd:NF041006   66 KRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKEALKEaivypSKRPDLFP- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 327 LGVvpPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQK 406
Cdd:NF041006  131 LGW--PRGILLYGPPGCGKTMLAAAVA---------------------------NEIDSEFIHVDAASIMSKWLGEAEKN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 407 LRELFEQA-----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD- 478
Cdd:NF041006  182 VAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDe 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 479 PALRragRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQ 558
Cdd:NF041006  259 PFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGE 334


                  ....*...
gi 1034558874 559 KKNPEMED 566
Cdd:NF041006  335 PRPITMED 342
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 643-753 9.46e-35

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: 129.86  E-value: 9.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 722
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034558874 723 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK 111
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 301-491 1.58e-34

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: 129.01  E-value: 1.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 301 VGGNDmTLKEVCK--MLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppas 378
Cdd:cd19509     1 IAGLD-DAKEALKeaVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVA------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 379 asQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 458
Cdd:cd19509    54 --SESGSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN 131

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034558874 459 vAATARVLVIGATNRPDSLDPALRRagRFDREI 491
Cdd:cd19509   132 -KPEDRVLVLGATNRPWELDEAFLR--RFEKRI 161
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 318-489 8.01e-34

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 127.24  E-value: 8.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 318 MRHPEVYHhLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgsndppasasqeldlpiLKVAAPEIVS 397
Cdd:cd19527    13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIA---------TECSLNF------------------LSVKGPELIN 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 398 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPD 475
Cdd:cd19527    65 MYIGESEANVREVFQKARDAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPD 142

                         170
                  ....*....|....
gi 1034558874 476 SLDPALRRAGRFDR 489
Cdd:cd19527   143 LLDPALLRPGRFDK 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 644-755 3.53e-32

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: 122.46  E-value: 3.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 644 IGALEDIREELTMAILAPVRNPDQFKaLGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 723
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034558874 724 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGE 111
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 637-755 4.18e-32

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: 122.66  E-value: 4.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 715
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034558874 716 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:cd19521    80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGE 119
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
 2-72 8.66e-31

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: 115.03  E-value: 8.66e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034558874   2 KPRPAGFVDNKLKQRVIQYLTSNKCGKYVDIGVLASDLQRVYSiDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 643-752 1.38e-30

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: 117.91  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALGLVT-PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 721
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1034558874 722 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRS 752
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRS 111
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 622-753 4.22e-30

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 123.33  E-value: 4.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 622 SSVQPSAKREGfvtvPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG 701
Cdd:PTZ00454  129 SSIQLLQMSEK----PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTT 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034558874 702 LNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:PTZ00454  205 ATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFD 256
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 643-756 1.41e-28

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: 112.39  E-value: 1.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 721
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034558874 722 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDREE 756
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEE 113
ftsH CHL00176
cell division protein; Validated
 639-751 3.53e-28

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 120.54  E-value: 3.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 639 VTWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 718
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFE-EVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034558874 719 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR 751
Cdd:CHL00176  259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQR 291
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 295-491 6.72e-28

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: 110.34  E-value: 6.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 295 NVKFEDVGGNDMTlKEVCK--MLIHMRHPEVYHHlGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgs 372
Cdd:cd19521     3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVA------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 373 ndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTC 452
Cdd:cd19521    62 --------TEANSTFFSVSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQ 133

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034558874 453 MDDLNNvaATARVLVIGATNRPDSLDPALRRagRFDREI 491
Cdd:cd19521   134 MNGVGN--DSQGVLVLGATNIPWQLDSAIRR--RFEKRI 168
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
641-756 9.86e-28

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 112.28  E-value: 9.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 641 WADIGALEDIREELTMaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES 720
Cdd:COG1223     1 LDDVVGQEEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558874 721 ERAVRQVFQRAKNsAPCVIFFDEVDALCPRRSDREE 756
Cdd:COG1223    80 ARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQND 114
cell_div_CdvC NF041006
cell division protein CdvC;
637-747 2.36e-27

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 114.45  E-value: 2.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 716
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558874 717 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDAL 747
Cdd:NF041006  175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDAL 210
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 637-753 3.43e-27

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 115.25  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 716
Cdd:PTZ00361  178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034558874 717 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSD 753
Cdd:PTZ00361  258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYD 294
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 300-483 3.64e-27

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: 108.28  E-value: 3.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGND---MTLKEvcKMLIHMRHPEVYHHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGAecsgmitAHCSFdfsgsndp 375
Cdd:cd19520     1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKE-------AGARF-------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 376 pasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDD 455
Cdd:cd19520    64 ------------INLQVSSLTDKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDG 131

                         170       180
                  ....*....|....*....|....*...
gi 1034558874 456 LNNvAATARVLVIGATNRPDSLDPALRR 483
Cdd:cd19520   132 LST-DGNCRVIVMGATNRPQDLDEAILR 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 637-755 2.91e-26

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: 106.23  E-value: 2.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 716
Cdd:cd19525    17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034558874 717 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:cd19525    96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE 134
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 296-491 1.25e-25

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: 104.68  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 296 VKFEDVGGNDM---TLKEVckMLIHMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgs 372
Cdd:cd19525    19 INWADIAGLEFakkTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIA---------SQSGATF--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 373 ndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTC 452
Cdd:cd19525    84 ---------------FSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQ 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034558874 453 MDDLnNVAATARVLVIGATNRPDSLDPALRRagRFDREI 491
Cdd:cd19525   149 LDGA-TTSSEDRILVVGATNRPQEIDEAARR--RLVKRL 184
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 643-756 1.70e-25

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: 103.74  E-value: 1.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 717
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034558874 718 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDREE 756
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQE 119
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
637-747 3.61e-25

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 110.90  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 637 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 716
Cdd:COG0465   137 PKVTFDDVAGVDEAKEEL-QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034558874 717 VG--ESeRaVRQVFQRAKNSAPCVIFFDEVDAL 747
Cdd:COG0465   216 VGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAV 246
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
640-751 9.49e-25

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 109.74  E-value: 9.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 640 TWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 719
Cdd:PRK10733  150 TFADVAGCDEAKEEVA-ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034558874 720 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRR 751
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQR 260
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 331-494 1.59e-24

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: 100.30  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 331 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasASQELDLPILKVAAPEIVSGVSGESEQK---L 407
Cdd:cd00009    18 PPKNLLLYGPPGTGKTTLARAIAN------------------------ELFRPGAPFLYLNASDLLEGLVVAELFGhflV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 408 RELFEQAVSNAPCIIFIDEIDAITpkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGR 486
Cdd:cd00009    74 RLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLNDlRIDRENVRVIGATNRPLLGDLDRALYDR 142


                  ....*...
gi 1034558874 487 FDREICLG 494
Cdd:cd00009   143 LDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
 289-535 6.19e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 106.26  E-value: 6.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 289 LEFQISNVKFEDVGGNDmtlkeVCKMLIHMRH---PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahc 365
Cdd:CHL00195  218 LEFYSVNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIAN----------- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 366 sfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERR 444
Cdd:CHL00195  282 ----------------DWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNR 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 445 IVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRlP---QAFDFC 521
Cdd:CHL00195  346 VLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIK 419

                         250
                  ....*....|....
gi 1034558874 522 HLAHLTPGFVGADL 535
Cdd:CHL00195  420 KLSKLSNKFSGAEI 433
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 331-491 4.01e-23

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: 96.98  E-value: 4.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 331 PPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLREL 410
Cdd:cd19522    32 PWKGVLMVGPPGTGKTLLAKAVA---------TECGTTF------------------FNVSSSTLTSKYRGESEKLVRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 411 FEQAVSNAPCIIFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPALRRag 485
Cdd:cd19522    85 FEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEALRR-- 162


                  ....*.
gi 1034558874 486 RFDREI 491
Cdd:cd19522   163 RLEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 643-755 4.05e-23

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: 96.46  E-value: 4.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKalGLVTPA-GVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 721
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034558874 722 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGE 112
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 321-491 6.40e-23

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: 96.40  E-value: 6.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 321 PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIagaecSGMITAhcsfdfsgsNDPPAsasqeldlpilkVAAPEIVSGVS 400
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQI-----GKMLNA---------REPKI------------VNGPEILNKYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 401 GESEQKLRELFEQA---------VSNAPCIIFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNVaatarvL 466
Cdd:cd19504    78 GESEANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNNI------L 150

                         170       180
                  ....*....|....*....|....*
gi 1034558874 467 VIGATNRPDSLDPALRRAGRFDREI 491
Cdd:cd19504   151 VIGMTNRKDLIDEALLRPGRLEVQM 175
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 328-489 6.51e-23

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: 95.90  E-value: 6.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 328 GVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKL 407
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAG---------------------------VWQLPLLRLDMGRLFGGLVGESESRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 408 RELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGR 486
Cdd:cd19507    80 RQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGR 154


                  ...
gi 1034558874 487 FDR 489
Cdd:cd19507   155 FDE 157
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 300-491 8.60e-23

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: 95.69  E-value: 8.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAgAECSGMItahcsfdfsgsndppas 378
Cdd:cd19524     1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVA-AESNATF----------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 379 asqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 458
Cdd:cd19524    62 ---------FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034558874 459 vAATARVLVIGATNRPDSLDPALRRagRFDREI 491
Cdd:cd19524   133 -NGDDRVLVMGATNRPQELDDAVLR--RFTKRV 162
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 643-745 1.26e-20

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: 89.35  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMailapvRNP---DQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 719
Cdd:cd19507     1 DVGGLDNLKDWLKK------RKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74

                          90       100
                  ....*....|....*....|....*.
gi 1034558874 720 SERAVRQVFQRAKNSAPCVIFFDEVD 745
Cdd:cd19507    75 SESRLRQMIQTAEAIAPCVLWIDEIE 100
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 669-756 7.24e-20

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: 86.82  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 669 KALGLVTPAGVLLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFD 742
Cdd:cd00009    12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFID 91

                          90
                  ....*....|....
gi 1034558874 743 EVDALCPRRSDREE 756
Cdd:cd00009    92 EIDSLSRGAQNALL 105
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 331-497 3.22e-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: 84.73  E-value: 3.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  331 PPRGVLLHGPPGCGKTLLAHAIAG---AECSGMITAHCSFDFSGsndppasasqeldLPILKVAAPEIVSGVSGESEQKL 407
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEE-------------VLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  408 RELFEQAVSNAPCIIFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRF 487
Cdd:smart00382  68 RLALALARKLKPDVLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RF 138

                          170
                   ....*....|
gi 1034558874  488 DREICLGIPD 497
Cdd:smart00382 139 DRRIVLLLIL 148
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 665-754 1.32e-16

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: 78.30  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 665 PDQFKALGLVTPAGVLLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYVGESERAVRQVF------QRAK- 732
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeeQRRLg 99

                          90       100
                  ....*....|....*....|...
gi 1034558874 733 -NSAPCVIFFDEVDALCPRRSDR 754
Cdd:cd19504   100 aNSGLHIIIFDEIDAICKQRGSM 122
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 643-755 2.13e-15

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: 74.54  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 643 DIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 722
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034558874 723 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 755
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEA 112
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 300-483 4.43e-15

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: 73.38  E-value: 4.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 300 DVGGNDM---TLKEvcKMLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndpp 376
Cdd:cd19523     1 DIAGLGAlkaAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLA----------------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 377 asasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKReVASKDMERRIVAQLLTCMDDL 456
Cdd:cd19523    55 ----SQLGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGV 129

                         170       180
                  ....*....|....*....|....*..
gi 1034558874 457 NNvAATARVLVIGATNRPDSLDPALRR 483
Cdd:cd19523   130 LG-SGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 318-491 9.92e-14

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: 69.30  E-value: 9.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 318 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAapeiVS 397
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG---------------------------ELDYDICDLN----LS 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 398 GVSGESEQKLRELfeqavSNAP--CIIFIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIG 469
Cdd:cd19510    58 EVVLTDDRLNHLL-----NTAPkqSIILLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALD---GVASSEERIVFM 129

                         170       180
                  ....*....|....*....|..
gi 1034558874 470 ATNRPDSLDPALRRAGRFDREI 491
Cdd:cd19510   130 TTNHIERLDPALIRPGRVDMKI 151
ycf46 CHL00195
Ycf46; Provisional
 582-745 2.52e-13

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 73.13  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 582 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVA-------LSSVQPSAKRE--------GFV 634
Cdd:CHL00195  144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATyktidenSIPLILEEKKQiisqteilEFY 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 635 TVpNVTWADIGALEDIREELTmailapvRNPDQF--KAL--GLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGP 710
Cdd:CHL00195  222 SV-NEKISDIGGLDNLKDWLK-------KRSTSFskQASnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVG 293

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034558874 711 ELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD 745
Cdd:CHL00195  294 KLFGGIVGESESRMRQMIRIAEALSPCILWIDEID 328
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 675-756 4.11e-13

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: 67.40  E-value: 4.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  675 TPAGVLLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 737
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90
                   ....*....|....*....
gi 1034558874  738 VIFFDEVDALCPRRSDREE 756
Cdd:smart00382  81 VLILDEITSLLDAEQEALL 99
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 518-557 8.97e-10

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: 54.47  E-value: 8.97e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034558874 518 FDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLMKLQEQ 557
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 333-481 6.47e-08

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 53.60  E-value: 6.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 333 RGVLLHGPPGCGKTLLAHAIAGAecsgmITAHCSFDFSGSNdppasasqeldlpILKVAAPEIVSGVSGESEQKLRELF- 411
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQK-----LSIRLSSRYRYGQ-------------LIEINSHSLFSKWFSESGKLVTKMFq 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874 412 --EQAVSNAPCIIF--IDEIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 481
Cdd:cd19508   115 kiQELIDDKDALVFvlIDEVESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKR---YHNNVILLTSNLLEKIDVAF 189
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 679-752 1.24e-07

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 51.76  E-value: 1.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRS 752
Cdd:cd19512    25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRS 98
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 326-491 3.62e-07

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 50.45  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 326 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGAECSGMITAhcsfdfsgsndppaSASQELD-LPILKVAAPEIVSGVSGESE 404
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRI--------------SLNKLLYnKPDFGNDDWIDGMLILKESL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 405 QKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 483
Cdd:cd19505    72 HRLNLQFELAKAMSPCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIA 151


                  ....*...
gi 1034558874 484 AGRFDREI 491
Cdd:cd19505   152 PNRLDTCI 159
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 679-749 5.06e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.78  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 744
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104

                          90
                  ....*....|
gi 1034558874 745 -----DALCP 749
Cdd:PRK13342  105 nkaqqDALLP 114
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 679-749 7.41e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 52.37  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFDEV--- 744
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVDEIhrf 117

                          90
                  ....*....|
gi 1034558874 745 -----DALCP 749
Cdd:COG2256   118 nkaqqDALLP 127
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 335-427 1.25e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 51.62  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAApeIVSGVsgeseQKLRELFEQA 414
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIA---------------------------GATDAPFEALSA--VTSGV-----KDLREVIEEA 84

                          90
                  ....*....|....*..
gi 1034558874 415 VSNA----PCIIFIDEI 427
Cdd:PRK13342   85 RQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 335-427 2.71e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.44  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAApeIVSGVSgeseqKLRELFEQA 414
Cdd:COG2256    52 MILWGPPGTGKTTLARLIA---------------------------NATDAEFVALSA--VTSGVK-----DIREVIEEA 97

                          90
                  ....*....|....*..
gi 1034558874 415 ----VSNAPCIIFIDEI 427
Cdd:COG2256    98 rerrAYGRRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
 297-354 3.08e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.30  E-value: 3.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874 297 KFEDVGGNDMTLKEVCKMLIHMRHPevyhhlgvVPPRGVLLHGPPGCGKTLLAHAIAG 354
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIESWLKG--------KPKKALLLYGPPGVGKTSLAHALAN 61
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 332-468 4.70e-06

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 47.50  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 332 PRGVLLHGPPGCGKTLLAHAI---AGAECSGMITAHC--------------SFDFSGSNDPPASASQELDLPILKVAAPE 394
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCdenlpyspllealtREGLLRQLLDELESSLLEAWRAALLEALA 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034558874 395 IVSGVSGESEQKLRELFEQAVSNA-----PCIIFIDEIDAItpkrevasKDMERRIVAQLLTCMDDLNnvaatarVLVI 468
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRLLDLLargerPLVLVLDDLQWA--------DEASLQLLAALLRLLESLP-------LLVV 167
ycf2 CHL00206
Ycf2; Provisional
 327-542 6.86e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 49.91  E-value: 6.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  327 LGVVPPRGVLLHGPPGCGKTLLAHAIAGAECSGMIT--------------AHCSFDFSGSNDPPASASQELDLPILKVAA 392
Cdd:CHL00206  1625 LALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfLIDDIDIDDSDDIDDSDDIDRDLDTELLTM 1704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874  393 PEIVSG--VSGESEQKLRELFEQAVSNAPCIIFIDEIdaitpkREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGA 470
Cdd:CHL00206  1705 MNALTMdmMPKIDRFYITLQFELAKAMSPCIIWIPNI------HDLNVNESNYLSLGLLVNSLSRDCERCSTRNILVIAS 1778

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874  471 TNRPDSLDPALRRAGRFDREIC---LGIPdeaSRERILQTLCRKLRLPQAFDFCHL---AHLTPGFVGADLMALCREA 542
Cdd:CHL00206  1779 THIPQKVDPALIAPNKLNTCIKirrLLIP---QQRKHFFTLSYTRGFHLEKKMFHTngfGSITMGSNARDLVALTNEA 1853
PRK04195 PRK04195
replication factor C large subunit; Provisional
 679-754 7.38e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.15  E-value: 7.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 750
Cdd:PRK04195   42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112


                  ....
gi 1034558874 751 RSDR 754
Cdd:PRK04195  113 NEDR 116
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 679-712 7.65e-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: 46.72  E-value: 7.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 712
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 680-751 1.70e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 48.30  E-value: 1.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034558874 680 LLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRR 751
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETG 391
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 335-543 2.06e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 47.08  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIAGAecsgmitAHCSF------------DFSGSNDPPASasqeldlpilkvaapeivsgvSGE 402
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARA-------LGLPFiriqftpdllpsDILGTYIYDQQ---------------------TGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 403 SEQKLRELFEQavsnapcIIFIDEIDAITPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS 476
Cdd:COG0714    86 FEFRPGPLFAN-------VLLADEINRAPPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQ 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034558874 477 -----LDPALRRagRFDREICLGIPDEASRERILqtlcrklrlpQAFDFCHLAHLTPGFVGADLMALCREAA 543
Cdd:COG0714   148 egtypLPEAQLD--RFLLKLYIGYPDAEEEREIL----------RRHTGRHLAEVEPVLSPEELLALQELVR 207
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 640-749 2.82e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 46.91  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 640 TWADIGALEDIREELTMAILAPVRNPDQfkalglvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGP------ELL 713
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPalekpgDLA 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034558874 714 NMYVGESERAvrqvfqraknsapcVIFFDEVDALCP 749
Cdd:TIGR00635  74 AILTNLEEGD--------------VLFIDEIHRLSP 95
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
679-712 2.84e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.05  E-value: 2.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 712
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 678-731 7.60e-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: 45.76  E-value: 7.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034558874 678 GVLLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 731
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 679-749 1.13e-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: 43.34  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 740
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80


                  ....*....
gi 1034558874 741 FDEVDALCP 749
Cdd:pfam07724  81 IDEIEKAHP 89
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 680-745 1.20e-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: 43.32  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 680 LLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIFFDEV 744
Cdd:cd19499    45 LFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVLLDEI 122


                  .
gi 1034558874 745 D 745
Cdd:cd19499   123 E 123
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
332-515 1.26e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 44.58  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 332 PRGVLLHGPPGCGKTLLAHAIAGAecsgmitAHCSfdfsgSNDPPASASQELDLPILKVAAPEivsgvsgeseqkLRELF 411
Cdd:COG0470    18 PHALLLHGPPGIGKTTLALALARD-------LLCE-----NPEGGKACGQCHSRLMAAGNHPD------------LLELN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 412 EQAVSNApciIFIDEIDAITPKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPAL 481
Cdd:COG0470    74 PEEKSDQ---IGIDQIRELGEFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTI 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034558874 482 RragrfdreiclgipdeaSRerilqtlCRKLRLP 515
Cdd:COG0470   149 R-----------------SR-------CQVIRFR 158
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 679-745 1.38e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 44.39  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESERAVRQ--VFQRaknsapcVIFFDEVD 745
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGEFEFRPgpLFAN-------VLLADEIN 104
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 613-750 1.65e-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: 43.14  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 613 ELNDFIVAlssvQPSAKREGFVTVPNvTWADIGALEDIREEltmailapvrnpdqfkalglVTPAGVLLAGPPGCGKTLL 692
Cdd:cd19498     8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDE--------------------VTPKNILMIGPTGVGKTEI 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034558874 693 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 750
Cdd:cd19498    63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
678-725 2.05e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034558874 678 GVLLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 725
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 679-710 2.22e-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: 43.92  E-value: 2.22e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLNFISVKGP 710
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 662-704 5.96e-04

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: 40.80  E-value: 5.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034558874 662 VRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNF 704
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDI 51
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 671-739 6.01e-04

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: 41.21  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 671 LGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 736
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86


                  ...
gi 1034558874 737 CVI 739
Cdd:cd19505    87 CII 89
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 679-752 6.60e-04

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: 41.66  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 679 VLLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIfFDE 743
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVL-IDE 133


                  ....*....
gi 1034558874 744 VDALCPRRS 752
Cdd:cd19508   134 VESLAAARS 142
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 649-756 8.71e-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: 40.59  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 649 DIREELTMAILAPVRNPDQFKALGLVTpaGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQ 726
Cdd:cd19506     1 DVRQLLTLYGILPLGSQAVHEKAPLVK--SLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034558874 727 VFQRAKNSAPCVIFFDEVDALCPRRSDREE 756
Cdd:cd19506    79 VLKVARQLQPSVIWIGDAEKTFYKKVPKTE 108
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 332-435 1.01e-03

recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange.


Pssm-ID: 410863 [Multi-domain]  Cd Length: 235  Bit Score: 41.39  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 332 PRG--VLLHGPPGCGKTLLA-HAIAGAECSGMItahCSF-DFSGSNDPPASASQELDLPILKVAAPEivsgvSGEseQKL 407
Cdd:cd00983    22 PRGriIEIYGPESSGKTTLAlHAIAEAQKLGGT---AAFiDAEHALDPEYAKKLGVDIDNLLVSQPD-----TGE--QAL 91

                          90       100
                  ....*....|....*....|....*....
gi 1034558874 408 rELFEQAV-SNAPCIIFIDEIDAITPKRE 435
Cdd:cd00983    92 -EIADTLIrSGAVDLIVVDSVAALVPKAE 119
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 335-353 1.02e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.56  E-value: 1.02e-03
                          10
                  ....*....|....*....
gi 1034558874 335 VLLHGPPGCGKTLLAHAIA 353
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIA 54
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 332-428 1.02e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.62  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 332 PRGVLL-HGPPGCGKTLLAHAIAGAECSG---MITahcsFDFSgsndppaSASQELDLPILKVAAPEIVsgvsGESEQKL 407
Cdd:cd19499    40 PIGSFLfLGPTGVGKTELAKALAELLFGDednLIR----IDMS-------EYMEKHSVSRLIGAPPGYV----GYTEGGQ 104

                          90       100
                  ....*....|....*....|.
gi 1034558874 408 reLFEQAVSNAPCIIFIDEID 428
Cdd:cd19499   105 --LTEAVRRKPYSVVLLDEIE 123
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 678-745 1.55e-03

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.58  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 678 GVLLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 745
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 335-353 1.74e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 41.22  E-value: 1.74e-03
                          10
                  ....*....|....*....
gi 1034558874 335 VLLHGPPGCGKTLLAHAIA 353
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIA 75
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
335-353 2.50e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.88  E-value: 2.50e-03
                          10
                  ....*....|....*....
gi 1034558874 335 VLLHGPPGCGKTLLAHAIA 353
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIA 72
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 335-432 3.25e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 39.10  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIA---GAECSGMITAHCSfDFSGSNdppaSASQeldlpiLKVAAPEIVSgvSGESEQklreLF 411
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellFGDERALIRIDMS-EYMEEH----SVSR------LIGAPPGYVG--YEEGGQ----LT 68

                          90       100
                  ....*....|....*....|.
gi 1034558874 412 EQAVSNAPCIIFIDEIDAITP 432
Cdd:pfam07724  69 EAVRRKPYSIVLIDEIEKAHP 89
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 335-367 3.55e-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: 3.55e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034558874 335 VLLHGPPGCGKTLLAHAIAGAECSGMITAHCSF 367
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSV 33
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 680-747 3.92e-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: 39.08  E-value: 3.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034558874 680 LLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 747
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
678-744 6.62e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 6.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034558874 678 GVLLAGPPGCGKTLLAKAVANE---SGLN--FISVkgPELLN-MYVGESERAVRQVFQRAKnSAPCVIfFDEV 744
Cdd:COG1484   101 NLILLGPPGTGKTHLAIALGHEacrAGYRvrFTTA--PDLVNeLKEARADGRLERLLKRLA-KVDLLI-LDEL 169
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 683-706 6.81e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.85  E-value: 6.81e-03
                          10        20
                  ....*....|....*....|....
gi 1034558874 683 GPPGCGKTLLAKAVANESGLNFIS 706
Cdd:cd02020     6 GPAGSGKSTVAKLLAKKLGLPYLD 29
AAA_22 pfam13401
AAA domain;
335-433 8.05e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034558874 335 VLLHGPPGCGKTLLAHAIA---GAECSGMITAHCsfdfsgsndPPASASQELDLPILKvaapEI-VSGVSGESEQKLREL 410
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVDL---------PSGTSPKDLLRALLR----ALgLPLSGRLSKEELLAA 74

                          90       100
                  ....*....|....*....|....*
gi 1034558874 411 FEQAVS--NAPCIIFIDEIDAITPK 433
Cdd:pfam13401  75 LQQLLLalAVAVVLIIDEAQHLSLE 99
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 289-352 8.95e-03

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


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 39.71  E-value: 8.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034558874 289 LEFQISNVK----FEDVGGNDMTLK---EVCKMLIHmrhpevYhhlgvvPPRG--VLLHGPPGCGKTLLAHAI 352
Cdd:COG1221    90 LAEKENNEEeedpFDNLIGANGSLKnaiEQAKAAIL------Y------PPKGlhTLILGPTGVGKSFFAELM 150
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 659-695 9.92e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.29  E-value: 9.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034558874 659 LAPVRNPDQFKALGLVTPAG---VLLAGPPGCGKTLLAKA 695
Cdd:pfam01078   2 LADVKGQEQAKRALEIAAAGghnLLMIGPPGSGKTMLAKR 41
 
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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