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Conserved domains on  [gi|15231775|ref|NP_190891|]
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ATPase, AAA-type, CDC48 protein [Arabidopsis thaliana]

Protein Classification

CDC48 family AAA ATPase( domain architecture ID 1001098)

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 ...
30-767 0e+00

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


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 787.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775    30 RLVVDEAINDD--NSVVSLHPDTMEKLQLFRGDTILIKGKKRKdTVCIALADETCDEPK--IRMNKVVRSNLRVRLGDVI 105
Cdd:TIGR01243   3 ELRVAEAYPRDvgRGIVRIDRQTAARLGVEPGDFVEIEKGDRS-VVAIVWPLRPDDEGRgiIRMDGYLRANAGVTIGDTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   106 SVHQCpDVKYGNRVHILPlddTIEGVSGNIFDAYLKPYFLEayRPVRKGDLFLVRGGMRSIEFKVIETDPAEYCVVAPDT 185
Cdd:TIGR01243  82 TVERA-EVKEAKKVVLAP---TQPIRFGRDFVDYVKEFLLG--KPISKGETVIVPVLEGALPFVVVSTQPAGFVYVTEAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   186 EIFCEGEPIKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANE 265
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   266 TGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHV 345
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   346 IVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQ 425
Cdd:TIGR01243 316 IVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   426 CIREKMDV--IDLDDEEIDAEILNSMAVSNDHFQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEH 503
Cdd:TIGR01243 396 ALRRFIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKH 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   504 PEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDEL 583
Cdd:TIGR01243 476 PEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEI 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   584 DSIATQRGNSVGDAggAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKS 663
Cdd:TIGR01243 556 DAIAPARGARFDTS--VTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKI 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   664 CLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIeKDIEKERKRAESpeameEDEEEIAEIKAGHFEESM 743
Cdd:TIGR01243 634 HTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESI-GSPAKEKLEVGE-----EEFLKDLKVEMRHFLEAL 707
                         730       740
                  ....*....|....*....|....
gi 15231775   744 KYARRSVSDADIRKYQAFAQTLQQ 767
Cdd:TIGR01243 708 KKVKPSVSKEDMLRYERLAKELKR 731
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
30-767 0e+00

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 787.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775    30 RLVVDEAINDD--NSVVSLHPDTMEKLQLFRGDTILIKGKKRKdTVCIALADETCDEPK--IRMNKVVRSNLRVRLGDVI 105
Cdd:TIGR01243   3 ELRVAEAYPRDvgRGIVRIDRQTAARLGVEPGDFVEIEKGDRS-VVAIVWPLRPDDEGRgiIRMDGYLRANAGVTIGDTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   106 SVHQCpDVKYGNRVHILPlddTIEGVSGNIFDAYLKPYFLEayRPVRKGDLFLVRGGMRSIEFKVIETDPAEYCVVAPDT 185
Cdd:TIGR01243  82 TVERA-EVKEAKKVVLAP---TQPIRFGRDFVDYVKEFLLG--KPISKGETVIVPVLEGALPFVVVSTQPAGFVYVTEAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   186 EIFCEGEPIKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANE 265
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   266 TGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHV 345
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   346 IVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQ 425
Cdd:TIGR01243 316 IVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   426 CIREKMDV--IDLDDEEIDAEILNSMAVSNDHFQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEH 503
Cdd:TIGR01243 396 ALRRFIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKH 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   504 PEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDEL 583
Cdd:TIGR01243 476 PEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEI 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   584 DSIATQRGNSVGDAggAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKS 663
Cdd:TIGR01243 556 DAIAPARGARFDTS--VTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKI 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   664 CLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIeKDIEKERKRAESpeameEDEEEIAEIKAGHFEESM 743
Cdd:TIGR01243 634 HTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESI-GSPAKEKLEVGE-----EEFLKDLKVEMRHFLEAL 707
                         730       740
                  ....*....|....*....|....
gi 15231775   744 KYARRSVSDADIRKYQAFAQTLQQ 767
Cdd:TIGR01243 708 KKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
489-649 5.56e-121

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: 361.06  E-value: 5.56e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19528   1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIY 648
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 15231775 649 I 649
Cdd:cd19528 161 I 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
474-719 2.51e-119

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 363.17  E-value: 2.51e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 474 EVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 553
Cdd:COG1222  71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 554 MWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSvGDaGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDII 633
Cdd:COG1222 151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD-GT-SGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 634 DPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIREN------- 706
Cdd:COG1222 229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGrdtvtme 308
                       250
                ....*....|....
gi 15231775 707 -IEKDIEKERKRAE 719
Cdd:COG1222 309 dLEKAIEKVKKKTE 322
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
472-721 6.94e-96

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 304.45  E-value: 6.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  472 VVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 551
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  552 LTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSvgDAGGAAD--RVLNQLLTEMDGMNAKKTVFIIGATNR 629
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDS--GTSGDREvqRTLMQLLAEMDGFDPRGNVKIIAATNR 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  630 PDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIREN--- 706
Cdd:PRK03992 280 IDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDrte 359
                        250       260
                 ....*....|....*....|....
gi 15231775  707 ---------IEKDIEKERKRAESP 721
Cdd:PRK03992 360 vtmedflkaIEKVMGKEEKDSMEE 383
cell_div_CdvC NF041006
cell division protein CdvC;
444-761 1.41e-60

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 209.59  E-value: 1.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  444 EILNSMAVSNdhfQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEkfgMSPSKGVLFYGP 523
Cdd:NF041006  69 EVLEELVPAE---PAGPDVEKESDEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGP 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  524 PGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSA-----PCVLFFDELDSIATQRGNSVgdaG 598
Cdd:NF041006 143 PGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEV---G 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  599 GAAdRVLNQLLTEMDGM---NAKKTVFIIGATNRPDIIDPALLRpgRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVD 675
Cdd:NF041006 220 GEV-RVRNQFLKEMDGLqdkSENYHVYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVD 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  676 LRALAKYTQGFSGADITEICQRSCKYAIRENIEKDIEKERKRAESpeameedeeeiaeikagHFEESMKYARRSVSDADI 755
Cdd:NF041006 297 LDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGEPRPITME-----------------DFKEVLKIRKPSVNQEML 359

                 ....*.
gi 15231775  756 RKYQAF 761
Cdd:NF041006 360 KAYEAW 365
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
245-375 5.51e-55

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: 185.49  E-value: 5.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEV 324
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15231775   325 ERRIVSQLLTLMDGLKSRAH-VIVMGATNRPNSIDPALRrfGRFDREIDIGV 375
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
31-110 1.35e-22

Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain.


Pssm-ID: 215012 [Multi-domain]  Cd Length: 82  Bit Score: 92.29  E-value: 1.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775     31 LVVDEAINDD---NSVVSLHPDTMEKLQLFRGDTILIKGKKRkdTVCIALADETCDEPK-IRMNKVVRSNLRVRLGDVIS 106
Cdd:smart01073   1 LRVAEAPSDEdvgRGIARLSPEDMDELGLFPGDYVLITGKRR--TVAIVWPAYPEDPGGiIRIDGVQRKNAGVSIGDTVT 78

                   ....
gi 15231775    107 VHQC 110
Cdd:smart01073  79 VRKA 82
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
518-543 2.85e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 2.85e-03
                         10        20
                 ....*....|....*....|....*..
gi 15231775  518 VLFYGPPGCGKTLLAKAIANE-CQANF 543
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAaCRQGY 119
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
30-767 0e+00

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 787.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775    30 RLVVDEAINDD--NSVVSLHPDTMEKLQLFRGDTILIKGKKRKdTVCIALADETCDEPK--IRMNKVVRSNLRVRLGDVI 105
Cdd:TIGR01243   3 ELRVAEAYPRDvgRGIVRIDRQTAARLGVEPGDFVEIEKGDRS-VVAIVWPLRPDDEGRgiIRMDGYLRANAGVTIGDTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   106 SVHQCpDVKYGNRVHILPlddTIEGVSGNIFDAYLKPYFLEayRPVRKGDLFLVRGGMRSIEFKVIETDPAEYCVVAPDT 185
Cdd:TIGR01243  82 TVERA-EVKEAKKVVLAP---TQPIRFGRDFVDYVKEFLLG--KPISKGETVIVPVLEGALPFVVVSTQPAGFVYVTEAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   186 EIFCEGEPIKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANE 265
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   266 TGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHV 345
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   346 IVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQ 425
Cdd:TIGR01243 316 IVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   426 CIREKMDV--IDLDDEEIDAEILNSMAVSNDHFQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEH 503
Cdd:TIGR01243 396 ALRRFIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKH 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   504 PEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDEL 583
Cdd:TIGR01243 476 PEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEI 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   584 DSIATQRGNSVGDAggAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKS 663
Cdd:TIGR01243 556 DAIAPARGARFDTS--VTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKI 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   664 CLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIeKDIEKERKRAESpeameEDEEEIAEIKAGHFEESM 743
Cdd:TIGR01243 634 HTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESI-GSPAKEKLEVGE-----EEFLKDLKVEMRHFLEAL 707
                         730       740
                  ....*....|....*....|....
gi 15231775   744 KYARRSVSDADIRKYQAFAQTLQQ 767
Cdd:TIGR01243 708 KKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
489-649 5.56e-121

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: 361.06  E-value: 5.56e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19528   1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIY 648
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 15231775 649 I 649
Cdd:cd19528 161 I 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
474-719 2.51e-119

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 363.17  E-value: 2.51e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 474 EVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 553
Cdd:COG1222  71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 554 MWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSvGDaGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDII 633
Cdd:COG1222 151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD-GT-SGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 634 DPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIREN------- 706
Cdd:COG1222 229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGrdtvtme 308
                       250
                ....*....|....
gi 15231775 707 -IEKDIEKERKRAE 719
Cdd:COG1222 309 dLEKAIEKVKKKTE 322
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
209-374 1.05e-116

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: 350.20  E-value: 1.05e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESES 288
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 289 NLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFD 368
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                ....*.
gi 15231775 369 REIDIG 374
Cdd:cd19519 161 REIDIG 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
190-438 2.40e-116

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 355.47  E-value: 2.40e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 190 EGEPIKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAF 269
Cdd:COG1222  60 LGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAP 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 270 FFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKR--EKTHGEVeRRIVSQLLTLMDGLKSRAHVIV 347
Cdd:COG1222 140 FIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtdDGTSGEV-QRTVNQLLAELDGFESRGDVLI 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 348 MGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCI 427
Cdd:COG1222 219 IAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
                       250
                ....*....|.
gi 15231775 428 REKMDVIDLDD 438
Cdd:COG1222 299 REGRDTVTMED 309
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
209-373 5.67e-101

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: 309.22  E-value: 5.67e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESES 288
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 289 NLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFD 368
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                ....*
gi 15231775 369 REIDI 373
Cdd:cd19503 161 REVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
489-649 3.02e-98

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: 301.90  E-value: 3.02e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGNSvgDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIY 648
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQS--DSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                .
gi 15231775 649 I 649
Cdd:cd19511 159 V 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
325-717 3.90e-97

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: 307.99  E-value: 3.90e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 325 ERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVS 404
Cdd:COG0464   1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 405 KDTHGYVGADLAALCTEAALQCIREKMDVIDLDDEEIDAEILNSMAVSNDHFQTALGNSNPSALRETVVEVPNVSWEDIG 484
Cdd:COG0464  81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 485 GLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVR 564
Cdd:COG0464 161 GLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 565 EIFDKARQSAPCVLFFDELDSIATQRGnsvGDAGGAADRVLNQLLTEMDGMNAKktVFIIGATNRPDIIDPALLRpgRLD 644
Cdd:COG0464 241 EVFDKARGLAPCVLFIDEADALAGKRG---EVGDGVGRRVVNTLLTEMEELRSD--VVVIAATNRPDLLDPALLR--RFD 313
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775 645 QLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIE----KDIEKERKR 717
Cdd:COG0464 314 EIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREpvttEDLLEALER 390
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
472-721 6.94e-96

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 304.45  E-value: 6.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  472 VVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 551
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  552 LTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSvgDAGGAAD--RVLNQLLTEMDGMNAKKTVFIIGATNR 629
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDS--GTSGDREvqRTLMQLLAEMDGFDPRGNVKIIAATNR 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  630 PDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIREN--- 706
Cdd:PRK03992 280 IDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDrte 359
                        250       260
                 ....*....|....*....|....
gi 15231775  707 ---------IEKDIEKERKRAESP 721
Cdd:PRK03992 360 vtmedflkaIEKVMGKEEKDSMEE 383
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
204-438 1.48e-95

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 303.68  E-value: 1.48e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  204 EVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLA 283
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  284 GESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPA 360
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775  361 LRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDD 438
Cdd:PRK03992 287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMED 364
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
197-438 1.69e-89

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 286.70  E-value: 1.69e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   197 EDEERlDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGP 276
Cdd:TIGR01242 112 EVEER-PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   277 EIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKSRAHVIVMGATNR 353
Cdd:TIGR01242 191 ELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAELDGFDPRGNVKVIAATNR 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   354 PNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDV 433
Cdd:TIGR01242 271 PDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY 350

                  ....*
gi 15231775   434 IDLDD 438
Cdd:TIGR01242 351 VTMDD 355
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
190-444 1.55e-87

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: 282.96  E-value: 1.55e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 190 EGEPIKREDEERLDEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAF 269
Cdd:COG0464 139 EDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLP 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 270 FFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRahVIVMG 349
Cdd:COG0464 219 LIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD--VVVIA 296
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 350 ATNRPNSIDPALRRfgRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIRE 429
Cdd:COG0464 297 ATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRL 374
                       250
                ....*....|....*..
gi 15231775 430 KMDVIDLDD--EEIDAE 444
Cdd:COG0464 375 GREPVTTEDllEALERE 391
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
489-649 3.09e-79

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: 252.03  E-value: 3.09e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGnSVGDAgGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIY 648
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRG-TTGDS-GVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                .
gi 15231775 649 I 649
Cdd:cd19529 159 I 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
474-717 1.94e-75

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: 253.75  E-value: 1.94e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   474 EVPNVSWEDIGGLENVKRELQETVQYpVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 553
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   554 MWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDII 633
Cdd:TIGR01241 127 MFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   634 DPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIREN----IEK 709
Cdd:TIGR01241 207 DPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNkteiTMN 286

                  ....*...
gi 15231775   710 DIEKERKR 717
Cdd:TIGR01241 287 DIEEAIDR 294
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
205-442 2.07e-75

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: 253.75  E-value: 2.07e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   205 VGYDDVGGVRKQMAQIRELVELpLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAG 284
Cdd:TIGR01241  52 VTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   285 ESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREK----THGEVERRIvSQLLTLMDGLKSRAHVIVMGATNRPNSIDPA 360
Cdd:TIGR01241 131 VGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglggGNDEREQTL-NQLLVEMDGFGTNTGVIVIAATNRPDVLDPA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   361 LRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDD-- 438
Cdd:TIGR01241 210 LLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDie 289

                  ....
gi 15231775   439 EEID 442
Cdd:TIGR01241 290 EAID 293
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
476-691 3.41e-74

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 253.04  E-value: 3.41e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 476 PNVSWEDIGGLENVKRELQETVQYpVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 555
Cdd:COG0465 137 PKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 556 FGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGdaGGAADR--VLNQLLTEMDGMNAKKTVFIIGATNRPDII 633
Cdd:COG0465 216 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLG--GGHDEReqTLNQLLVEMDGFEGNEGVIVIAATNRPDVL 293
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 634 DPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADI 691
Cdd:COG0465 294 DPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADL 351
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
486-649 4.38e-74

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: 238.54  E-value: 4.38e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 486 LENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVRE 565
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 566 IFDKARQSAPCVLFFDELDSIATQRGNSvgdAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQ 645
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDG---GSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                ....
gi 15231775 646 LIYI 649
Cdd:cd19530 158 TLYV 161
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
489-649 8.10e-74

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: 237.80  E-value: 8.10e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKFEKfGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19527   1 VKKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGNSvGDAGGAADRVLNQLLTEMDGMN-AKKTVFIIGATNRPDIIDPALLRPGRLDQLI 647
Cdd:cd19527  80 KARDAKPCVIFFDELDSLAPSRGNS-GDSGGVMDRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                ..
gi 15231775 648 YI 649
Cdd:cd19527 159 YL 160
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
474-717 3.16e-72

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 241.98  E-value: 3.16e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  474 EVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 553
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  554 MWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDII 633
Cdd:PTZ00454 218 KYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  634 DPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIREN----IEK 709
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNryviLPK 377

                 ....*...
gi 15231775  710 DIEKERKR 717
Cdd:PTZ00454 378 DFEKGYKT 385
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
207-437 3.58e-72

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 243.14  E-value: 3.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  207 YDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGES 286
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  287 ESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTH--GEVE-RRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRR 363
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATsgGEKEiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775  364 FGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLER--VSKDThgYVGADLAALCTEAALQCIRE-KMDVIDLD 437
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEfiMAKDE--LSGADIKAICTEAGLLALRErRMKVTQAD 416
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
205-438 8.05e-72

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 246.49  E-value: 8.05e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 205 VGYDDVGGVRKQMAQIRELVELpLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAG 284
Cdd:COG0465 139 VTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 217
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 285 ESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEV--ER-RIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPAL 361
Cdd:COG0465 218 VGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGhdEReQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPAL 297
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775 362 RRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDD 438
Cdd:COG0465 298 LRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
209-371 1.79e-71

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: 231.52  E-value: 1.79e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESES 288
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 289 NLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLK----SRAHVIVMGATNRPNSIDPALRRF 364
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPALRRA 160

                ....*..
gi 15231775 365 GRFDREI 371
Cdd:cd19518 161 GRFDREI 167
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
482-649 6.93e-71

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: 229.87  E-value: 6.93e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGgaaDRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPG 641
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVE---RRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                ....*...
gi 15231775 642 RLDQLIYI 649
Cdd:cd19503 158 RFDREVEI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
480-721 2.14e-70

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 231.70  E-value: 2.14e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 480 WEDIGGLENVKRELQETVQYpVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGES 559
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 560 EANVREIFDKARQsAPCVLFFDELDSIATQRG--NSVGDAGgaadRVLNQLLTEMDGMNAKktVFIIGATNRPDIIDPAL 637
Cdd:COG1223  80 ARNLRKLFDFARR-APCVIFFDEFDAIAKDRGdqNDVGEVK----RVVNALLQELDGLPSG--SVVIAATNHPELLDSAL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 638 LRpgRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIEK-------- 709
Cdd:COG1223 153 WR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKvtkedlee 230
                       250
                ....*....|....
gi 15231775 710 --DIEKERKRAESP 721
Cdd:COG1223 231 alKQRKERKKEPKK 244
ftsH CHL00176
cell division protein; Validated
478-718 2.67e-69

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 241.11  E-value: 2.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  478 VSWEDIGGLENVKRELQETVQYpVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFG 557
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  558 ESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPAL 637
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  638 LRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIEKDIEKERKR 717
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418

                 .
gi 15231775  718 A 718
Cdd:CHL00176 419 A 419
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
489-648 3.09e-68

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: 222.69  E-value: 3.09e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGNsvgDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIY 648
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGH---DSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
219-371 1.24e-67

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: 221.00  E-value: 1.24e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 219 QIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAE 298
Cdd:cd19511   4 ELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKAR 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231775 299 KNAPSIIFIDEIDSIAPKR-EKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREI 371
Cdd:cd19511  84 QAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
479-647 5.77e-66

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: 216.82  E-value: 5.77e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 479 SWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGE 558
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 559 SEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALL 638
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                ....*....
gi 15231775 639 RPGRLDQLI 647
Cdd:cd19502 161 RPGRFDRKI 169
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
478-649 6.33e-66

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: 216.71  E-value: 6.33e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 478 VSWEDIGGLENVKRELQETVQYpVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFG 557
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 558 ESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPAL 637
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 15231775 638 LRPGRLDQLIYI 649
Cdd:cd19501 160 LRPGRFDRQVYV 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
199-440 7.81e-66

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 224.64  E-value: 7.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  199 EERLDeVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEI 278
Cdd:PTZ00454 137 SEKPD-VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  279 MSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVER---RIVSQLLTLMDGLKSRAHVIVMGATNRPN 355
Cdd:PTZ00454 216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTNVKVIMATNRAD 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  356 SIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVID 435
Cdd:PTZ00454 296 TLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVIL 375

                 ....*
gi 15231775  436 LDDEE 440
Cdd:PTZ00454 376 PKDFE 380
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
207-373 3.90e-65

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: 214.89  E-value: 3.90e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 207 YDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGES 286
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 287 ESNLRKAFEEAEKNAPSIIFIDEIDSIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRR 363
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161
                       170
                ....*....|
gi 15231775 364 FGRFDREIDI 373
Cdd:cd19502 162 PGRFDRKIEF 171
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
489-649 7.83e-65

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: 213.30  E-value: 7.83e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 489 VKRELQETVQYPVEHPEKfEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 568
Cdd:cd19481   1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 569 KARQSAPCVLFFDELDSIATQRGNSVGDagGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIY 648
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDSSGES--GELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 15231775 649 I 649
Cdd:cd19481 158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
219-373 3.39e-64

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: 211.59  E-value: 3.39e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 219 QIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAE 298
Cdd:cd19529   4 ELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKAR 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231775 299 KNAPSIIFIDEIDSIAPKREKTHGE-VERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDI 373
Cdd:cd19529  84 QVAPCVIFFDEIDSIAPRRGTTGDSgVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
459-706 2.46e-63

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 224.53  E-value: 2.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  459 ALGNSNPSALRETVVEVpnvSWEDIGGLENVKRELQETVQYpVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANE 538
Cdd:PRK10733 133 SFGKSKARMLTEDQIKT---TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGE 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  539 CQANFISIKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAK 618
Cdd:PRK10733 209 AKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGN 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  619 KTVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRS 698
Cdd:PRK10733 289 EGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEA 368

                 ....*...
gi 15231775  699 CKYAIREN 706
Cdd:PRK10733 369 ALFAARGN 376
ftsH CHL00176
cell division protein; Validated
205-445 8.85e-63

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 223.00  E-value: 8.85e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  205 VGYDDVGGVRKQMAQIRELVELpLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAG 284
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  285 ESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREK----THGEVERrIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPA 360
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiggGNDEREQ-TLNQLLTEMDGFKGNKGVIVIAATNRVDILDAA 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  361 LRRFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDdeE 440
Cdd:CHL00176 338 LLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMK--E 415

                 ....*
gi 15231775  441 IDAEI 445
Cdd:CHL00176 416 IDTAI 420
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
482-650 7.03e-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: 205.75  E-value: 7.03e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDaggAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPG 641
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGE---VERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 15231775 642 RLDQLIYIP 650
Cdd:cd19519 158 RFDREIDIG 166
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
472-705 7.12e-61

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 212.32  E-value: 7.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  472 VVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 551
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEL 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  552 LTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSvgDAGGAAD--RVLNQLLTEMDGMNAKKTVFIIGATNR 629
Cdd:PTZ00361 254 IQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDA--TSGGEKEiqRTMLELLNQLDGFDSRGDVKVIMATNR 331
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231775  630 PDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVDLRALAKYTQGFSGADITEICQRSCKYAIRE 705
Cdd:PTZ00361 332 IESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRE 407
cell_div_CdvC NF041006
cell division protein CdvC;
444-761 1.41e-60

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 209.59  E-value: 1.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  444 EILNSMAVSNdhfQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEkfgMSPSKGVLFYGP 523
Cdd:NF041006  69 EVLEELVPAE---PAGPDVEKESDEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGP 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  524 PGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSA-----PCVLFFDELDSIATQRGNSVgdaG 598
Cdd:NF041006 143 PGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEV---G 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  599 GAAdRVLNQLLTEMDGM---NAKKTVFIIGATNRPDIIDPALLRpgRLDQLIYIPLPDEESRYQIFKSCLRKSPVAKDVD 675
Cdd:NF041006 220 GEV-RVRNQFLKEMDGLqdkSENYHVYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVD 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  676 LRALAKYTQGFSGADITEICQRSCKYAIRENIEKDIEKERKRAESpeameedeeeiaeikagHFEESMKYARRSVSDADI 755
Cdd:NF041006 297 LDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGEPRPITME-----------------DFKEVLKIRKPSVNQEML 359

                 ....*.
gi 15231775  756 RKYQAF 761
Cdd:NF041006 360 KAYEAW 365
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
218-373 1.62e-60

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: 201.74  E-value: 1.62e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 218 AQIRELVELPLRHPQLFKSiGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEA 297
Cdd:cd19481   3 ASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775 298 EKNAPSIIFIDEIDSIAPKREKT-HGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDI 373
Cdd:cd19481  82 RRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
474-673 4.84e-59

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: 209.57  E-value: 4.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   474 EVPNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANE-CQ---------ANF 543
Cdd:TIGR03689 175 EVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAArigaegggkSYF 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   544 ISIKGPELLTMWFGESEANVREIFDKARQSA----PCVLFFDELDSIATQRGNSVgdAGGAADRVLNQLLTEMDGMNAKK 619
Cdd:TIGR03689 255 LNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGV--SSDVETTVVPQLLAEIDGVESLD 332
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15231775   620 TVFIIGATNRPDIIDPALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKS-PVAKD 673
Cdd:TIGR03689 333 NVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTDDlPLPED 387
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
209-370 4.05e-58

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: 195.81  E-value: 4.05e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGA-----FFFCINGPEIMSKLA 283
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 284 GESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRR 363
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                ....*..
gi 15231775 364 FGRFDRE 370
Cdd:cd19517 161 PGRFDRE 167
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
192-447 1.02e-57

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 205.71  E-value: 1.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   192 EPIKREDEERL-----DEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANET 266
Cdd:TIGR03689 161 EAIPRTEVEDLvleevPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSL 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   267 G----------AFFFCINGPEIMSKLAGESESNLRKAFEEAEKNA----PSIIFIDEIDSIApkreKTHG-----EVERR 327
Cdd:TIGR03689 241 AarigaegggkSYFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLF----RTRGsgvssDVETT 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   328 IVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHtknmkLAEDVDLERVSKDT 407
Cdd:TIGR03689 317 VVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPEDLAAH 391
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 15231775   408 HGYVGADLAALCTEA--ALQCIREKMDVIDLDDEEIDAEILN 447
Cdd:TIGR03689 392 DGDREATAAALIQRVvdALYARSEANRYVEVTYANGSTEVLY 433
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
208-438 2.38e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 196.26  E-value: 2.38e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 208 DDVGGVRKQMAQIRELVElPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESE 287
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 288 SNLRKAFEEAeKNAPSIIFIDEIDSIAPKREKTH--GEVeRRIVSQLLTLMDGLKSraHVIVMGATNRPNSIDPALRRfg 365
Cdd:COG1223  81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNdvGEV-KRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR-- 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231775 366 RFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDD 438
Cdd:COG1223 155 RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKED 227
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
205-373 7.49e-57

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: 192.06  E-value: 7.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 205 VGYDDVGGVRKQMAQIRELVELpLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAG 284
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 285 ESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREK----THGEVERRIvSQLLTLMDGLKSRAHVIVMGATNRPNSIDPA 360
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglggGHDEREQTL-NQLLVEMDGFESNTGVIVIAATNRPDVLDPA 158
                       170
                ....*....|...
gi 15231775 361 LRRFGRFDREIDI 373
Cdd:cd19501 159 LLRPGRFDRQVYV 171
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
482-647 1.41e-56

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: 191.46  E-value: 1.41e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDaggAADRVLNQLLTEMDGMNAKKT----VFIIGATNRPDIIDPAL 637
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQRE---MERRIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 15231775 638 LRPGRLDQLI 647
Cdd:cd19518 158 RRAGRFDREI 167
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
207-436 1.60e-55

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 202.57  E-value: 1.60e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  207 YDDVGGVRKQMAQIRELVELpLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGES 286
Cdd:PRK10733 151 FADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  287 ESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKT----HGEVERRIvSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALR 362
Cdd:PRK10733 230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgggHDEREQTL-NQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231775  363 RFGRFDREIDIGVPDEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDL 436
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSM 382
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
245-375 5.51e-55

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: 185.49  E-value: 5.51e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEV 324
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15231775   325 ERRIVSQLLTLMDGLKSRAH-VIVMGATNRPNSIDPALRrfGRFDREIDIGV 375
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
518-651 1.04e-54

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: 184.72  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   518 VLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSvgdA 597
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG---G 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15231775   598 GGAADRVLNQLLTEMDGM-NAKKTVFIIGATNRPDIIDPALLrpGRLDQLIYIPL 651
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
219-373 4.06e-54

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: 184.25  E-value: 4.06e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 219 QIRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAE 298
Cdd:cd19528   4 ELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKAR 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 299 KNAPSIIFIDEIDSIAPKREKTHGE---VERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREIDI 373
Cdd:cd19528  84 AAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
210-373 6.20e-53

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: 181.01  E-value: 6.20e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 210 VGGVRKQMAQIRELVELPLRHPQLFKSIgVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESN 289
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 290 LRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGL--KSRAHVIVMGATNRPNSIDPALRRfgRF 367
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR--RF 157

                ....*.
gi 15231775 368 DREIDI 373
Cdd:cd19509 158 EKRIYI 163
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
483-649 1.14e-52

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: 180.24  E-value: 1.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 483 IGGLENVKRELQETVQYPVEHPEKFeKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEAN 562
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 563 VREIFDKARQSAPCVLFFDELDSIATQRGNsvGDAGGAAdRVLNQLLTEMDGMNAK--KTVFIIGATNRPDIIDPALLRp 640
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGS--GEHEASR-RVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR- 155

                ....*....
gi 15231775 641 gRLDQLIYI 649
Cdd:cd19509 156 -RFEKRIYI 163
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
212-369 2.14e-52

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: 179.61  E-value: 2.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 212 GVRKQ--MAQIRelvelPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESN 289
Cdd:cd19530   3 HVREEltMSILR-----PIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 290 LRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDR 369
Cdd:cd19530  78 VRQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
220-371 1.59e-49

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: 171.46  E-value: 1.59e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 220 IRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEK 299
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231775 300 NAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREI 371
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
219-369 7.10e-47

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: 164.22  E-value: 7.10e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 219 QIRELVELPLRHPQLFKSiGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAE 298
Cdd:cd19527   4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231775 299 KNAPSIIFIDEIDSIAPKR--EKTHGEVERRIVSQLLTLMDGL-KSRAHVIVMGATNRPNSIDPALRRFGRFDR 369
Cdd:cd19527  83 DAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
482-648 9.63e-47

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: 164.22  E-value: 9.63e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANEC-----QANFISIKGPELLTMWF 556
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 557 GESEANVREIFDKARQSAPCVLFFDELDSIATQRgNSVGDAGGAAdrVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPA 636
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-SSKQEQIHAS--IVSTLLALMDGLDNRGQVVVIGATNRPDALDPA 157
                       170
                ....*....|..
gi 15231775 637 LLRPGRLDQLIY 648
Cdd:cd19517 158 LRRPGRFDREFY 169
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
209-363 9.21e-46

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: 161.44  E-value: 9.21e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGV-KPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESE 287
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 288 SNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAH--VIVMGATNRPNSIDPALRR 363
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAILR 158
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
482-639 2.53e-44

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: 157.20  E-value: 2.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFGM-SPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESE 560
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 561 ANVREIFDKARQSAPCVLFFDELDSIATQRgnSVGDAGGAAdRVLNQLLTEMDGM--NAKKTVFIIGATNRPDIIDPALL 638
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR--SSTDHEATA-MMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAIL 157

                .
gi 15231775 639 R 639
Cdd:cd19520 158 R 158
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
205-373 4.37e-44

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: 156.95  E-value: 4.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 205 VGYDDVGGVRKQMAQIRELVELPLRHPQLFKSiGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAG 284
Cdd:cd19521   4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 285 ESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGL-KSRAHVIVMGATNRPNSIDPALRR 363
Cdd:cd19521  83 ESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSAIRR 162
                       170
                ....*....|
gi 15231775 364 fgRFDREIDI 373
Cdd:cd19521 163 --RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
203-373 1.54e-43

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: 155.92  E-value: 1.54e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 203 DEVGYDDVGGVRKQMAQIRELVELPLRHPQLFKSIGvKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKL 282
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 283 AGESESNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLK--SRAHVIVMGATNRPNSIDPA 360
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEA 175
                       170
                ....*....|...
gi 15231775 361 LRRfgRFDREIDI 373
Cdd:cd19525 176 ARR--RLVKRLYI 186
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
476-649 1.89e-43

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: 155.02  E-value: 1.89e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 476 PNVSWEDIGGLENVKRELQETVQYPVEHPEKFeKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 555
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 556 FGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDaggAADRVLNQLLTEMDGM-NAKKTVFIIGATNRPDIID 634
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESE---ASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                       170
                ....*....|....*
gi 15231775 635 PALLRpgRLDQLIYI 649
Cdd:cd19521 158 SAIRR--RFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
482-649 2.99e-41

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: 148.59  E-value: 2.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFgMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGI-RRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSIATQRGNSvgDAGGAADRVLNQLLTEMDGM-------NAKKTVFIIGATNRPDIID 634
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTS--EEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDID 157
                       170
                ....*....|....*
gi 15231775 635 PALLRpgRLDQLIYI 649
Cdd:cd19522 158 EALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
504-644 1.05e-40

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: 147.64  E-value: 1.05e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 504 PEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISI-KGPELLTMWFGESEANVREIFDKARQ--------SA 574
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEeqrrlganSG 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 575 PCVLFFDELDSIATQRGnSVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLD 644
Cdd:cd19504 104 LHIIIFDEIDAICKQRG-SMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
476-649 1.79e-40

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: 147.06  E-value: 1.79e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 476 PNVSWEDIGGLENVKRELQETVQYPVEHPEKFEKFgMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 555
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 556 FGESEANVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDaggAADRVLNQLLTEMDGMN--AKKTVFIIGATNRPDII 633
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHE---SSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEI 172
                       170
                ....*....|....*.
gi 15231775 634 DPALLRpgRLDQLIYI 649
Cdd:cd19525 173 DEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
209-373 4.36e-40

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: 145.51  E-value: 4.36e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGvKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESES 288
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 289 NLRKAFEEAEKNAPSIIFIDEIDSIAPKR--EKTHgEVERRIVSQLLTLMDGL-------KSRAHVIVMGATNRPNSIDP 359
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRgtSEEH-EASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                       170
                ....*....|....
gi 15231775 360 ALRRfgRFDREIDI 373
Cdd:cd19522 159 ALRR--RLEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
209-364 2.04e-37

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: 137.67  E-value: 2.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIGvKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESES 288
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231775 289 NLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRA--HVIVMGATNRPNSIDPA-LRRF 364
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGddRVLVMGATNRPQELDDAvLRRF 158
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
482-649 9.68e-36

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: 132.67  E-value: 9.68e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFgMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGL-RAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSIATQRGNSVGDaggAADRVLNQLLTEMDGM--NAKKTVFIIGATNRPDIIDPALLR 639
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHE---ASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR 156
                       170
                ....*....|
gi 15231775 640 pgRLDQLIYI 649
Cdd:cd19524 157 --RFTKRVYV 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
210-373 4.86e-35

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 131.46  E-value: 4.86e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 210 VGGVRKQMAQI-RELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCI-NGPEIMSKLAGESE 287
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 288 SNLRKAFEEAE-----KNAPS---IIFIDEIDSIAPKREKTHGE--VERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSI 357
Cdd:cd19504  82 ANIRKLFADAEeeqrrLGANSglhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLI 161
                       170
                ....*....|....*.
gi 15231775 358 DPALRRFGRFDREIDI 373
Cdd:cd19504 162 DEALLRPGRLEVQMEI 177
ycf46 CHL00195
Ycf46; Provisional
476-708 1.30e-33

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 135.53  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  476 PNVSWEDIGGLENVKRELQetvQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 555
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLK---KRSTSFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  556 FGESEANVREIFDKARQSAPCVLFFDELDSiATQRGNSVGDaGGAADRVLNQLLTEMDgmNAKKTVFIIGATNRPDIIDP 635
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDK-AFSNSESKGD-SGTTNRVLATFITWLS--EKKSPVFVVATANNIDLLPL 375
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231775  636 ALLRPGRLDQLIYIPLPDEESRYQIFKSCLRKS-PVA-KDVDLRALAKYTQGFSGADITEICQRSCKYAIRENIE 708
Cdd:CHL00195 376 EILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKRE 450
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
211-374 9.72e-32

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: 121.10  E-value: 9.72e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 211 GGVRKQMAQIRELVELPlrhpqlfksigvkPPKGILLYGPPGSGKTLIARAVANET---GAFFFCINGPEIMSKLAGESE 287
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 288 ---SNLRKAFEEAEKNAPSIIFIDEIDSIAPkrekthgEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRF 364
Cdd:cd00009  68 fghFLVRLLFELAEKAKPGVLFIDEIDSLSR-------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140
                       170
                ....*....|
gi 15231775 365 GRFDREIDIG 374
Cdd:cd00009 141 DRLDIRIVIP 150
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
484-651 3.30e-31

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: 119.56  E-value: 3.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 484 GGLENVKRELQETVQYPvehpekfekfgmsPSKGVLFYGPPGCGKTLLAKAIANEC---QANFISIKGPELLTMWFGESE 560
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 561 AN---VREIFDKARQSAPCVLFFDELDSIatqrgnsvgdAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPAL 637
Cdd:cd00009  68 FGhflVRLLFELAEKAKPGVLFIDEIDSL----------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                       170
                ....*....|....
gi 15231775 638 LRPGRLDQLIYIPL 651
Cdd:cd00009 138 ALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
482-649 9.83e-31

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 118.24  E-value: 9.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQEtvQYPVEHPEKFeKFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19507   1 DVGGLDNLKDWLKK--RKAAFSKQAS-AYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSiATQRGNSVGDaGGAADRVLNQLLTEMDgmNAKKTVFIIGATNRPDIIDPALLRPG 641
Cdd:cd19507  78 RLRQMIQTAEAIAPCVLWIDEIEK-GFSNADSKGD-SGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153

                ....*...
gi 15231775 642 RLDQLIYI 649
Cdd:cd19507 154 RFDEIFFV 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
209-364 2.72e-29

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: 114.21  E-value: 2.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVRKQMAQIRELVELPLRHPQLFKSIgVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESES 288
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 289 NLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVErRIVSQLLTLMDGLKSRA--HVIVMGATNRPNSIDPALRRF 364
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRRY 156
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
209-369 2.82e-25

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: 102.83  E-value: 2.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 209 DVGGVR--KQMAQIRElvelPLRHPQLFKSiGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGES 286
Cdd:cd19507   1 DVGGLDnlKDWLKKRK----AAFSKQASAY-GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 287 ESNLRKAFEEAEKNAPSIIFIDEIDS-IAPKREKTHGEVERRIVSQLLTLMDGLKSRahVIVMGATNRPNSIDPALRRFG 365
Cdd:cd19507  76 ESRLRQMIQTAEAIAPCVLWIDEIEKgFSNADSKGDSGTSSRVLGTFLTWLQEKKKP--VFVVATANNVQSLPPELLRKG 153

                ....
gi 15231775 366 RFDR 369
Cdd:cd19507 154 RFDE 157
CDC48_N pfam02359
Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel ...
30-112 8.11e-25

Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases pfam00004 is a substrate 185-residue recognition domain.


Pssm-ID: 426738  Cd Length: 85  Bit Score: 98.81  E-value: 8.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775    30 RLVVDEAINDD--NSVVSLHPDTMEKLQLFRGDTILIKGKKRkdTVCIALADETCDEPK--IRMNKVVRSNLRVRLGDVI 105
Cdd:pfam02359   1 RLRVAEAPDRDvgRGIARLNPEDMEELGLFPGDVVEIKGKRK--TVAIVWSAYPEDEGPgiIRMDGVTRKNAGVSIGDTV 78

                  ....*..
gi 15231775   106 SVHQCPD 112
Cdd:pfam02359  79 TVRPAEV 85
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
482-639 1.85e-23

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: 97.65  E-value: 1.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 482 DIGGLENVKRELQETVQYPVEHPEKFEKFgMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 561
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 562 NVREIFDKARQSAPCVLFFDELDSIATQRgnsvGDAGGAADRVLNQLLTEMDGM--NAKKTVFIIGATNRPDIIDPALLR 639
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQ----DDEASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
31-110 1.35e-22

Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain.


Pssm-ID: 215012 [Multi-domain]  Cd Length: 82  Bit Score: 92.29  E-value: 1.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775     31 LVVDEAINDD---NSVVSLHPDTMEKLQLFRGDTILIKGKKRkdTVCIALADETCDEPK-IRMNKVVRSNLRVRLGDVIS 106
Cdd:smart01073   1 LRVAEAPSDEdvgRGIARLSPEDMDELGLFPGDYVLITGKRR--TVAIVWPAYPEDPGGiIRIDGVQRKNAGVSIGDTVT 78

                   ....
gi 15231775    107 VHQC 110
Cdd:smart01073  79 VRKA 82
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
514-653 5.98e-21

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: 90.13  E-value: 5.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775    514 PSKGVLFYGPPGCGKTLLAKAIANECQAN---FISIKGPELL--------------TMWFGESEANVREIFDKARQSAPC 576
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775    577 VLFFDELDSIAtqrgnsvgDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPgRLDQLIYIPLPD 653
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
241-377 2.32e-20

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: 88.20  E-value: 2.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775    241 PPKGILLYGPPGSGKTLIARAVANE---TGAFFFCINGPEIMS--------------KLAGESESNLRKAFEEAEKNAPS 303
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231775    304 IIFIDEIDSIAPKREKthgevERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFgRFDREIDIGVPD 377
Cdd:smart00382  81 VLILDEITSLLDAEQE-----ALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
ycf46 CHL00195
Ycf46; Provisional
238-430 8.03e-17

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 84.30  E-value: 8.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  238 GVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPSIIFIDEID-SIAPK 316
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  317 REKTHGEVERRIVSQLLTLMDGLKSRahVIVMGATNRPNSIDPALRRFGRFDREIDIGVPDEIGRLEVLRIHTKNM--KL 394
Cdd:CHL00195 335 ESKGDSGTTNRVLATFITWLSEKKSP--VFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKS 412
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15231775  395 AEDVDLERVSKDTHGYVGADLAALCTEAALQCIREK 430
Cdd:CHL00195 413 WKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEK 448
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
516-649 4.62e-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: 70.46  E-value: 4.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 516 KGVLFYGPPGCGKTLLAKAIANECQANF--ISIKGPELltmwfgeSEANVREIFDKARQSApcVLFFDELDS--IATQRG 591
Cdd:cd19510  24 RGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVL-------TDDRLNHLLNTAPKQS--IILLEDIDAafESREHN 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231775 592 NSVGDAGGAADRV-LNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLRPGRLDQLIYI 649
Cdd:cd19510  95 KKNPSAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
518-649 6.70e-14

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: 71.32  E-value: 6.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 518 VLFYGPPGCGKTLLAKAIANEC---------QANFISIKGPELLTMWFGESEANVREIFDK------ARQSAPCVLfFDE 582
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLsirlssryrYGQLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVL-IDE 133
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 583 LDSIATQRGN-SVGDAGGAADRVLNQLLTEMDGMNAKKTVFIIGATNRPDIIDPALLrpGRLDQLIYI 649
Cdd:cd19508 134 VESLAAARSAsSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
220-371 2.00e-13

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 68.53  E-value: 2.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 220 IRELVELPLRHPQLFKSIGVKPPKGILLYGPPGSGKTLIARAVANETGAFFFCINgpeimskLAGESESNLRKafEEAEK 299
Cdd:cd19510   1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN-------LSEVVLTDDRL--NHLLN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 300 NAP--SIIFIDEIDSIAPKREKT------HGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREI 371
Cdd:cd19510  72 TAPkqSIILLEDIDAAFESREHNkknpsaYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
397-440 2.58e-13

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: 64.48  E-value: 2.58e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15231775   397 DVDLERVSKDTHGYVGADLAALCTEAALQCIREKMDVIDLDDEE 440
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
245-361 1.66e-12

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 67.09  E-value: 1.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 245 ILLYGPPGSGKTLIARAVANE-----TGAFFFC----INGPEIMSKLAGESESNLRKAFEEAE-----KNAPSIIFIDEI 310
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKlsirlSSRYRYGqlieINSHSLFSKWFSESGKLVTKMFQKIQeliddKDALVFVLIDEV 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15231775 311 DSIAPKREKTHGEVER----RIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPAL 361
Cdd:cd19508 135 ESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
245-310 5.13e-12

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 68.93  E-value: 5.13e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAFFFCINGpeIMSKLAgesesNLRKAFEEAEKNA----PSIIFIDEI 310
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA--VTSGVK-----DIREVIEEARERRaygrRTILFVDEI 114
CDC48_2 smart01072
Cell division protein 48 (CDC48) domain 2; This domain has a double psi-beta barrel fold and ...
136-196 5.46e-12

Cell division protein 48 (CDC48) domain 2; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the C-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain.


Pssm-ID: 215011  Cd Length: 64  Bit Score: 61.46  E-value: 5.46e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231775    136 FDAYLKPYFLEayRPVRKGDLFLVRGGMRSIEFKVIETDPAEYCVVAPDTEIFCEGEPIKR 196
Cdd:smart01072   6 FAEYVKRKLLG--RPVTKGDTIVVPFLGKALPFVVVSTEPSGPVIVTDDTEIEILEKPVEE 64
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
245-310 5.91e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 68.57  E-value: 5.91e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPeimskLAGESEsnLRKAFEEAEKNAPS----IIFIDEI 310
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGVKD--LREVIEEARQRRSAgrrtILFIDEI 101
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
243-368 1.75e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 62.93  E-value: 1.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 243 KGILLYGPPGSGKTLIARAVANETGAFFFCINGPEImSKLAGESESNLRKAFEEAEK-NAPSIIFIDEIDSIAPKREKTH 321
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEK 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15231775 322 GEVERRIVSQLLTLMDGLKSRAHVIVMgATNRPNSIDPALRrfGRFD 368
Cdd:cd19512 102 ISEDLRAALNAFLYRTGEQSNKFMLVL-ASNQPEQFDWAIN--DRID 145
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
509-649 3.65e-11

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 62.39  E-value: 3.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 509 KFGMSPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWF--------------GESEANVREIFDKARQSA 574
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPdfgnddwidgmlilKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 575 PCVLFFD---ELDsIATQRGNSVGDAGGAADRVLNQLLTEMDGMNAKKTVfIIGATNRPDIIDPALLRPGRLDQLIYI 649
Cdd:cd19505  86 PCIIWIPnihELN-VNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNIL-VIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
220-358 3.41e-10

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: 59.46  E-value: 3.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 220 IRELVELPLRHPQLFKSIGVKPP--KGILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSKLAGES--ESNLRKAFE 295
Cdd:cd19506   2 VRQLLTLYGILPLGSQAVHEKAPlvKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLK 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231775 296 EAEKNAPSIIFIDEIDSIAPKR-EKTHGEVE-RRIVSQLLTLMDGLKSRAHVIVMGATNRPNSID 358
Cdd:cd19506  82 VARQLQPSVIWIGDAEKTFYKKvPKTEKQLDpKRLKKDLPKILKSLKPEDRVLIVGTTSRPFEAD 146
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
513-647 4.28e-10

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 58.69  E-value: 4.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 513 SPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWfGESEANVREIFDKARQSAP-CVLFFDELDSIATQRG 591
Cdd:cd19512  20 GLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRgLLLFVDEADAFLRKRS 98
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775 592 -NSVGDAGGAAdrvLNQLLTEMdGMNAKKTVFIIgATNRPDIIDPALlrPGRLDQLI 647
Cdd:cd19512  99 tEKISEDLRAA---LNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 148
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
518-582 1.07e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 61.61  E-value: 1.07e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231775 518 VLFYGPPGCGKTLLAKAIANECQANFISIKGpelltmwfgeSEANV---REIFDKARQSA----PCVLFFDE 582
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA----------VTSGVkdiREVIEEARERRaygrRTILFVDE 113
CDC48_2 pfam02933
Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and ...
138-195 1.32e-09

Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the C-terminus. The VAT-N domain found in AAA ATPases pfam00004 is a substrate 185-residue recognition domain.


Pssm-ID: 427063  Cd Length: 64  Bit Score: 54.55  E-value: 1.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775   138 AYLKPYFLEayRPVRKGDLFLVRGGMRSIEFKVIETDPAEYCVVAPDTEIFCEGEPIK 195
Cdd:pfam02933   8 AYVKRNLEG--RPVSKGDTIVVEFLGGAIPLVVVSTEPSGPVVVTETTEIEIGEKPVQ 63
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
197-403 1.67e-09

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: 61.01  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   197 EDEERLDE-VGyddVGGVRKQMAQIRELVELPLRHPQLfksiGVKPP---KGILLYGPPGSGKTLIARAVANetgafFFC 272
Cdd:TIGR03922 270 EAEAELAEqIG---LERVKRQVAALKSSTAMALARAER----GLPVAqtsNHMLFAGPPGTGKTTIARVVAK-----IYC 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   273 ----INGPEIM----SKLAGESESNLRKAFEEA-EKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRA 343
Cdd:TIGR03922 338 glgvLRKPLVRevsrADLIGQYIGESEAKTNEIiDSALGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARMENDRDRL 417
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231775   344 HVIVMG---ATNRPNSIDPALRRfgRFDREIDIG--VPDEIGRLEVlRIHTKNMKLAEDVDLERV 403
Cdd:TIGR03922 418 VVIGAGyrkDLDKFLEVNEGLRS--RFTRVIEFPsySPDELVEIAR-RMATERDSVLDDAAADAL 479
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
518-582 2.30e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.48  E-value: 2.30e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231775  518 VLFYGPPGCGKTLLAKAIANECQANFISIKGPElltmwfgESEANVREIFDKARQSA----PCVLFFDE 582
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRsagrRTILFIDE 100
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
673-713 3.04e-09

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 52.93  E-value: 3.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15231775   673 DVDLRALAKYTQGFSGADITEICQRSCKYAIRENIE----KDIEK 713
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEavtqEDLEE 45
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
485-632 7.44e-09

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: 59.09  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   485 GLENVKRE---LQETVQYPVEHPEKfekfGMS---PSKGVLFYGPPGCGKTLLAKAIANE-C------QANFISIKGPEL 551
Cdd:TIGR03922 280 GLERVKRQvaaLKSSTAMALARAER----GLPvaqTSNHMLFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADL 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   552 LTMWFGESEANVREIFDKARQSapcVLFFDELDSIaTQRGNSVGDAGGAAdrVLNQLLTEMDgmNAKKTVFIIGATNRPD 631
Cdd:TIGR03922 356 IGQYIGESEAKTNEIIDSALGG---VLFLDEAYTL-VETGYGQKDPFGLE--AIDTLLARME--NDRDRLVVIGAGYRKD 427

                  .
gi 15231775   632 I 632
Cdd:TIGR03922 428 L 428
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
244-367 6.04e-08

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: 52.29  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   244 GILLYGPPGSGKTLIARAVANET-GAFFFCINGP------------EIMSKLAGESESNLRKAFEEAEknapsIIFIDEI 310
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTrdtteedlfgrrNIDPGGASWVDGPLVRAAREGE-----IAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231775   311 DSIAPK-REKTHGEVERRIvsqlLTLMDG----LKSRAHVIVMGATNRP----NSIDPALRRfgRF 367
Cdd:pfam07728  76 NRANPDvLNSLLSLLDERR----LLLPDGgelvKAAPDGFRLIATMNPLdrglNELSPALRS--RF 135
PRK13341 PRK13341
AAA family ATPase;
246-310 7.16e-08

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 56.22  E-value: 7.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  246 LLYGPPGSGKTLIARAVANETGAFFFCINgpeimSKLAGESEsnLRKAFEEAEK-----NAPSIIFIDEI 310
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLN-----AVLAGVKD--LRAEVDRAKErlerhGKRTILFIDEV 118
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
242-338 2.18e-07

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: 51.61  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 242 PKGILLYGPPGSGKTLIARAVANETGAFFFCINGPEI--MSKLAGESESNLRKAFEeaeknapSIIFIDEIDSIAPKREK 319
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118
                        90       100
                ....*....|....*....|
gi 15231775 320 THGEVERRIVSQ-LLTLMDG 338
Cdd:cd19498 119 SGPDVSREGVQRdLLPIVEG 138
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
238-373 2.38e-07

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 51.22  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 238 GVKPPKGILLYGPPGSGKTLIARAVANET--------------GAFFFCINGPEIMSKLAGESESNLRKAFEEAEKNAPS 303
Cdd:cd19505   8 GLSPSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPC 87
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231775 304 IIFIDEIDSIAPKREKTHGEVERRI-VSQLLTLMDGLKSRAHV---IVMGATNRPNSIDPALRRFGRFDREIDI 373
Cdd:cd19505  88 IIWIPNIHELNVNRSTQNLEEDPKLlLGLLLNYLSRDFEKSSTrniLVIASTHIPQKVDPALIAPNRLDTCINI 161
44 PHA02544
clamp loader, small subunit; Provisional
226-384 5.24e-07

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 52.30  E-value: 5.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  226 LPLRHPQLFKSIgVKP---PKGILLYGPPGSGKTLIARAVANETGAFFFCINGpeimSKLAGESESNLRKAFEEA--EKN 300
Cdd:PHA02544  25 LPAADKETFKSI-VKKgriPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNG----SDCRIDFVRNRLTRFASTvsLTG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  301 APSIIFIDEIDsiapkREKTHgEVERrivsQLLTLMDGLKSRAHVIVmgATNRPNSIDPALRrfGRFdREIDIGVPDEIG 380
Cdd:PHA02544 100 GGKVIIIDEFD-----RLGLA-DAQR----HLRSFMEAYSKNCSFII--TANNKNGIIEPLR--SRC-RVIDFGVPTKEE 164

                 ....
gi 15231775  381 RLEV 384
Cdd:PHA02544 165 QIEM 168
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
245-365 6.78e-07

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 52.06  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSK--LAGeSESNLrkafeeaEKNapSIIFIDEIDSIAPKREkthg 322
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKPgdLAA-ILTNL-------EEG--DVLFIDEIHRLSPVVE---- 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775  323 EV------ERRIvsqllTLMDGLKSRAHVIVM--------GATNRPNSIDPALR-RFG 365
Cdd:PRK00080 120 EIlypameDFRL-----DIMIGKGPAARSIRLdlppftliGATTRAGLLTSPLRdRFG 172
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
518-551 7.26e-07

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: 49.81  E-value: 7.26e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 15231775   518 VLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 551
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
245-382 1.13e-06

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: 51.15  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPEIM--SKLAGeSESNLRKAfeeaeknapSIIFIDEIDSIAPKREkthg 322
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEkpGDLAA-ILTNLEEG---------DVLFIDEIHRLSPAVE---- 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775   323 EVerrivsqLLTLMD----------GLKSR------AHVIVMGATNRPNSIDPALR-RFGrFDREIDIGVPDEIGRL 382
Cdd:TIGR00635  99 EL-------LYPAMEdfrldivigkGPSARsvrldlPPFTLVGATTRAGMLTSPLRdRFG-IILRLEFYTVEELAEI 167
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
518-551 1.53e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.90  E-value: 1.53e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15231775  518 VLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 551
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
245-365 2.05e-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: 48.27  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPEIMSK--LAGeSESNLRKAfeeaeknapSIIFIDEIDSIAPKREkthg 322
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERPgdLAA-ILTNLEPG---------DVLFIDEIHRLNRAVE---- 101
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231775   323 EV------ERRIVsqlLTLMDGLKSRAHVI------VMGATNRPNSIDPALR-RFG 365
Cdd:pfam05496 102 EIlypameDFRLD---IVIGKGPSARSIRLdlppftLVGATTRAGLLTSPLRdRFG 154
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
479-551 3.77e-06

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: 49.61  E-value: 3.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231775   479 SWEDIGGLENVKRELQETVQYPVEHPEKFEKfgmspskgVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 551
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEALDH--------LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
242-315 8.97e-06

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: 46.80  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   242 PKG-ILLYGPPGSGKTLIARAVANETGAF---FFCINGPEIM-----SKLAGESESNLRKA-----FEEAEKNAPSIIFI 307
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELLFGDeraLIRIDMSEYMeehsvSRLIGAPPGYVGYEeggqlTEAVRRKPYSIVLI 81

                  ....*...
gi 15231775   308 DEIDSIAP 315
Cdd:pfam07724  82 DEIEKAHP 89
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
518-549 1.12e-05

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 48.15  E-value: 1.12e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 15231775 518 VLFYGPPGCGKTLLAKAIANECQANFISIKGP 549
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
240-368 1.17e-05

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: 46.40  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 240 KPPKGILLYGPPGSGKTLIARAVA---NETGAFFFCINGPEIMSKlagESESNLRKA-------------FEEAEKNAPS 303
Cdd:cd19499  39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEK---HSVSRLIGAppgyvgyteggqlTEAVRRKPYS 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231775 304 IIFIDEIdsiapkrEKTHGEVeRRIVSQLL---TLMDGLKSRAH----VIVMGAtnrpNSIDPALrrFGRFD 368
Cdd:cd19499 116 VVLLDEI-------EKAHPDV-QNLLLQVLddgRLTDSHGRTVDfkntIIIMTS----NHFRPEF--LNRID 173
PRK04195 PRK04195
replication factor C large subunit; Provisional
240-379 1.82e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.99  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  240 KPPKGILLYGPPGSGKTLIARAVANETGAFFFCINGP-----EIMSKLAGESeSNLRKAFEEAEKnapsIIFIDEIDSIa 314
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIERVAGEA-ATSGSLFGARRK----LILLDEVDGI- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  315 pkrektHGEVERRIVSQLLTLmdgLKSRAHVIVMGATN---------------------RPNSIDPALRRFGRfdREiDI 373
Cdd:PRK04195 111 ------HGNEDRGGARAILEL---IKKAKQPIILTANDpydpslrelrnaclmiefkrlSTRSIVPVLKRICR--KE-GI 178

                 ....*.
gi 15231775  374 GVPDEI 379
Cdd:PRK04195 179 ECDDEA 184
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
245-389 1.82e-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: 47.47  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAFFFCING-PEIM-SKLAGESESNLRKAFEEAEKNaP---SIIFIDEIDSiAPkrEK 319
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpSDILGTYIYDQQTGEFEFRPG-PlfaNVLLADEINR-AP--PK 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 320 THgeverrivSQLLTLM-------DG----LKSRAHVIvmgATNrpNSID--------PALRRfgRFDREIDIGVPDEIG 380
Cdd:COG0714 110 TQ--------SALLEAMeerqvtiPGgtykLPEPFLVI---ATQ--NPIEqegtyplpEAQLD--RFLLKLYIGYPDAEE 174

                ....*....
gi 15231775 381 RLEVLRIHT 389
Cdd:COG0714 175 EREILRRHT 183
PRK04195 PRK04195
replication factor C large subunit; Provisional
481-538 1.96e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.99  E-value: 1.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775  481 EDIGGLENVKRELQETVqypvehpEKFEKfgMSPSKGVLFYGPPGCGKTLLAKAIANE 538
Cdd:PRK04195  14 SDVVGNEKAKEQLREWI-------ESWLK--GKPKKALLLYGPPGVGKTSLAHALAND 62
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
243-293 2.34e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.66  E-value: 2.34e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231775 243 KGILLYGPPGSGKTLIARAVANETGAF--FFCINGPEIMSKLAGESE---SNLRKA 293
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALRKA 120
PRK13341 PRK13341
AAA family ATPase;
519-665 3.61e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 47.36  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775  519 LFYGPPGCGKTLLAKAIANECQANFISIKgpellTMWFGESEanVREIFDKARQSAP-----CVLFFDELdsiatQRGNS 593
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLN-----AVLAGVKD--LRAEVDRAKERLErhgkrTILFIDEV-----HRFNK 123
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775  594 vgdaggaadrvlNQ---LLTEMDgmnaKKTVFIIGAT--NRPDIIDPALLRPGRLDQLiyIPLpDEESRYQIFKSCL 665
Cdd:PRK13341 124 ------------AQqdaLLPWVE----NGTITLIGATteNPYFEVNKALVSRSRLFRL--KSL-SDEDLHQLLKRAL 181
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
218-371 6.32e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 45.99  E-value: 6.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 218 AQIRELVELpLRhPQLFKSigvkPPKGILLYGPPGSGKTLIARAV-------ANETGAFFFC--INGPE------IMSKL 282
Cdd:COG1474  33 EEIEELASA-LR-PALRGE----RPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVvyVNCRQastryrVLSRI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 283 A------------GESESNLRKAFEEA--EKNAPSIIFIDEIDSIapkrEKTHGEverRIVSQLLTLMDGLKSrAHVIVM 348
Cdd:COG1474 107 LeelgsgedipstGLSTDELFDRLYEAldERDGVLVVVLDEIDYL----VDDEGD---DLLYQLLRANEELEG-ARVGVI 178
                       170       180
                ....*....|....*....|....*..
gi 15231775 349 GATNRPN---SIDPALR-RFGrfDREI 371
Cdd:COG1474 179 GISNDLEfleNLDPRVKsSLG--EEEI 203
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
516-543 7.37e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.16  E-value: 7.37e-05
                        10        20
                ....*....|....*....|....*....
gi 15231775 516 KGVLFYGPPGCGKTLLAKAIANE-CQANF 543
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEaCRAGY 128
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
486-685 1.01e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 44.97  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 486 LENVKRELQETVQYPVEHPekfekfgmspskGVLFYGPPGCGKTLLAKAIANE--CQAN-------------FISIKGPE 550
Cdd:COG0470   1 QEEAWEQLLAAAESGRLPH------------ALLLHGPPGIGKTTLALALARDllCENPeggkacgqchsrlMAAGNHPD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 551 LLTMwfgESEAN--------VREIFDKARQSAPC----VLFFDELDSIATqrgnsvgdaggAADRVLNQLLTEMdgmnAK 618
Cdd:COG0470  69 LLEL---NPEEKsdqigidqIRELGEFLSLTPLEggrkVVIIDEADAMNE-----------AAANALLKTLEEP----PK 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231775 619 KTVFIIgATNRPDIIDPALL-RPgrldQLIYIPLPDEESryqiFKSCLRKSPVAKDvDLRALAKYTQG 685
Cdd:COG0470 131 NTPFIL-IANDPSRLLPTIRsRC----QVIRFRPPSEEE----ALAWLREEGVDED-ALEAILRLAGG 188
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
518-587 1.06e-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: 43.72  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   518 VLFYGPPGCGKTLLAKAIANE---CQANFISIKGPELL-----TMWFGESEANVR-----EIFDKARQSAPCVLFFDELD 584
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMeehsvSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85

                  ...
gi 15231775   585 SIA 587
Cdd:pfam07724  86 KAH 88
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
243-293 1.13e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 1.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231775   243 KGILLYGPPGSGKTLIARAVANETGAF--FFCINGPEIMSKLAGESES---NLRKA 293
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEAltqAFRKA 106
AAA_22 pfam13401
AAA domain;
245-349 1.86e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   245 ILLYGPPGSGKTLIARAVAN---ETGAFFFCINGP------EIMSKLAGE---------SESNLRKAFEEA--EKNAPSI 304
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPsgtspkDLLRALLRAlglplsgrlSKEELLAALQQLllALAVAVV 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15231775   305 IFIDEIDSIAPKrekthgeverrIVSQLLTLMDGLKSRAHVIVMG 349
Cdd:pfam13401  88 LIIDEAQHLSLE-----------ALEELRDLLNLSSKLLQLILVG 121
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
245-310 2.23e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 44.30  E-value: 2.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAFFFCINGPEImSK---LAGeSESNLrkafeeaEKNapSIIFIDEI 310
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI-EKpgdLAA-ILTNL-------EEG--DVLFIDEI 114
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
214-348 2.45e-04

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: 42.49  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   214 RKQMAQIRELVElPLRHPQlfksigvkpPKGILLYGPPGSGKTLIARAV---ANETGAFFFCINGPEIMSKLA---GESE 287
Cdd:pfam13191   6 EEELEQLLDALD-RVRSGR---------PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPlleALTR 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231775   288 SNLRKAFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVM 348
Cdd:pfam13191  76 EGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
PRK08116 PRK08116
hypothetical protein; Validated
515-538 6.62e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.32  E-value: 6.62e-04
                         10        20
                 ....*....|....*....|....
gi 15231775  515 SKGVLFYGPPGCGKTLLAKAIANE 538
Cdd:PRK08116 114 NVGLLLWGSVGTGKTYLAACIANE 137
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
518-639 7.92e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 43.25  E-value: 7.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 518 VLFYGPPGCGKTLLAKAIANECQANFISIKGP-----------------ELLTMWFGESEANVREIFDKARQSAPCVLFF 580
Cdd:COG5635 183 LLILGEPGSGKTTLLRYLALELAERYLDAEDPipilielrdlaeeasleDLLAEALEKRGGEPEDALERLLRNGRLLLLL 262
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231775 581 DELDSIATQRGNsvgdaggaaDRVLNQLLTEMDgmNAKKTVFIIgaTNRPDIIDPALLR 639
Cdd:COG5635 263 DGLDEVPDEADR---------DEVLNQLRRFLE--RYPKARVII--TSRPEGYDSSELE 308
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
516-561 7.94e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 42.65  E-value: 7.94e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15231775 516 KGVLFYGPPGCGKTLLAKAIANECQAN--FISIKGPELLTMWFGESEA 561
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEF 112
PRK08116 PRK08116
hypothetical protein; Validated
244-310 8.50e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.93  E-value: 8.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231775  244 GILLYGPPGSGKTLIARAVAN---ETGAFFFCINGPEIMSKLAgeSESNLRKAFEEAE-----KNAPSIIfIDEI 310
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANeliEKGVPVIFVNFPQLLNRIK--STYKSSGKEDENEiirslVNADLLI-LDDL 187
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
201-353 9.21e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 41.69  E-value: 9.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 201 RLDEVGYDDVGGVRKqmAQIRELVELPlrhpqlFksigVKPPKGILLYGPPGSGKTLIARAVANE------TGAFFFCin 274
Cdd:COG1484  70 TLEDFDFDAQPGLDR--RQILELATLD------F----IERGENLILLGPPGTGKTHLAIALGHEacragyRVRFTTA-- 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 275 gPEIMSKLA-GESESNLRKAFEEAEKnaPSIIFIDEIDSIAPKREKTH--GEV-----ERR---IVSQL----------- 332
Cdd:COG1484 136 -PDLVNELKeARADGRLERLLKRLAK--VDLLILDELGYLPLDAEGAEllFELisdryERRstiITSNLpfsewgevfgd 212
                       170       180
                ....*....|....*....|....*
gi 15231775 333 --LT--LMDGLKSRAHVIVMGATNR 353
Cdd:COG1484 213 ptLAtaILDRLVHHAHIIELKGESY 237
PRK06835 PRK06835
DNA replication protein DnaC; Validated
487-538 1.27e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 41.81  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15231775  487 ENVKRELQETVQYPVEHPEKFEKFGMSPSKGVLFYGPPGCGKTLLAKAIANE 538
Cdd:PRK06835 155 DDEPLSPRKNMEKILEKCKNFIENFDKNNENLLFYGNTGTGKTFLSNCIAKE 206
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
518-538 1.33e-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: 38.74  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|.
gi 15231775   518 VLFYGPPGCGKTLLAKAIANE 538
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
245-358 1.94e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 39.02  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAF---FFCINGPEIMsklagesesnLRKAFEEAEKNAPSIIFIDEIDSIAPKREkth 321
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSdepVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQ--- 67
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15231775 322 GEVERRIVSQLLTLMDGLKsRAHVIVMGATNRPNSID 358
Cdd:cd01120  68 GDRSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
245-314 2.17e-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: 39.85  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAFFFCINgpeimskLAG-ESESNLR---------------KAFEEAEKNAPsIIFID 308
Cdd:cd19500  40 LCLVGPPGVGKTSLGKSIARALGRKFVRIS-------LGGvRDEAEIRghrrtyvgampgriiQALKKAGTNNP-VFLLD 111

                ....*.
gi 15231775 309 EIDSIA 314
Cdd:cd19500 112 EIDKIG 117
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
518-543 2.85e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 2.85e-03
                         10        20
                 ....*....|....*....|....*..
gi 15231775  518 VLFYGPPGCGKTLLAKAIANE-CQANF 543
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAaCRQGY 119
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
245-285 3.27e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.13  E-value: 3.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAFFFCINgpEIMSKLAGE 285
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRSD--VVRKRLFGA 40
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
241-343 3.49e-03

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 40.69  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   241 PPKGILLYGPPGSGKTLIARAVANE-------TGAFFF-----C--INGP-EIMSKLA---GESESN-----------LR 291
Cdd:TIGR02928  39 RPSNVFIYGKTGTGKTAVTKYVMKEleeaaedRDVRVVtvyvnCqiLDTLyQVLVELAnqlRGSGEEvpttglstsevFR 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231775   292 KAFEEAEKNAPSIIFI-DEIDSIAPK---------REKTHGEVER-RI----VSQLLTLMDGLKSRA 343
Cdd:TIGR02928 119 RLYKELNERGDSLIIVlDEIDYLVGDdddllyqlsRARSNGDLDNaKVgvigISNDLKFRENLDPRV 185
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
249-328 3.78e-03

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 39.42  E-value: 3.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 249 GPPGSGKTLIARAVANETGafFFCINGpEIMSKLAGESESNLrKAFEEAEKNAPSIIFIDEidsiaPKREKTHGEVERRI 328
Cdd:COG1102   7 REPGSGGTTIAKRLAEKLG--LPLYDG-EILREAAKERGLSE-EEFEKLDEKAPSLLYRDT-----AEEDEIDRALDKVI 77
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
293-542 4.09e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.52  E-value: 4.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 293 AFEEAEKNAPSIIFIDEIDSIAPKREKTHGEVERRIVSQLLTLMDGLKSRAHVIVMGATNRPNSIDPALRRFGRFDREID 372
Cdd:COG1401   3 RPVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 373 IGvpdEIGRLEVLRIHTKNMKLAEDVDLERVSKDTHGYVGADLAALCTEAAlqcIREKMDVIDLDDEEIDAEILNSmAVS 452
Cdd:COG1401  83 LE---KVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALE---ALERARLLLELADLEERAALET-EVL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 453 NDHFQTALGNSNPSALRETVVEVPNVSWEDIGGLENVKRELQETVQYPVEH-PEKFEKF--GMSPSKGVLFYGPPGCGKT 529
Cdd:COG1401 156 EALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKfEETLEAFlaALKTKKNVILAGPPGTGKT 235
                       250
                ....*....|...
gi 15231775 530 LLAKAIANECQAN 542
Cdd:COG1401 236 YLARRLAEALGGE 248
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
518-535 4.63e-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: 39.06  E-value: 4.63e-03
                          10
                  ....*....|....*...
gi 15231775   518 VLFYGPPGCGKTLLAKAI 535
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRL 42
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
518-537 4.87e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 39.60  E-value: 4.87e-03
                          10        20
                  ....*....|....*....|
gi 15231775   518 VLFYGPPGCGKTLLAKAIAN 537
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIAH 135
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
291-326 5.08e-03

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 40.06  E-value: 5.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15231775  291 RKAFEEAEKNApsIIFIDEIDSIAPKREKTHGEVER 326
Cdd:PRK05201 241 QEAIERVEQNG--IVFIDEIDKIAARGGSSGPDVSR 274
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
245-398 6.36e-03

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.40  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 245 ILLYGPPGSGKTLIARAVANETGAFF-----FCINGPEIMSKLAGESESNLRKAFEEAEKNApSIIFIDEIDSIAPKrEK 319
Cdd:COG0593  37 LFLYGGVGLGKTHLLHAIGNEALENNpgarvVYLTAEEFTNDFINAIRNNTIEEFKEKYRSV-DVLLIDDIQFLAGK-EA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775 320 THGEverrivsqLLTLMDGLKSRAHVIVMGATNRPNSI---DPALR-RFgrfdrE----IDIGVPDEIGRLEVLR--IHT 389
Cdd:COG0593 115 TQEE--------FFHTFNALREAGKQIVLTSDRPPKELpglEERLRsRL-----EwglvVDIQPPDLETRIAILRkkAAD 181

                ....*....
gi 15231775 390 KNMKLAEDV 398
Cdd:COG0593 182 RGLELPDEV 190
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
245-329 7.40e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 38.17  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231775   245 ILLYGPPGSGKTLIARAVANETGAFFfcINGPEIMSKLAGESESNLRKAFEEAEKNapsiifiDEIDSIAPKREKTHGEV 324
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKL--ISAGDIFRELAAKMGLDLIEFLNYAEEN-------PEIDKKIDRRIHEIALK 73

                  ....*
gi 15231775   325 ERRIV 329
Cdd:TIGR02173  74 EKNVV 78
 
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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