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Conserved domains on  [gi|1002279835|ref|XP_015644237|]
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cell division control protein 48 homolog C [Oryza sativa Japonica Group]

Protein Classification

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 ...
169-767 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: 538.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 169 EAKPEsaPPSEGGDRGGKGPTFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANE 248
Cdd:TIGR01243 158 EIREK--PVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 249 TGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigs 328
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMD-------- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 329 gsgdvgsesAEKKPGYVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATS 408
Cdd:TIGR01243 308 ---------GLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTH 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 409 SFVGADLKALVDKAGNLAMKRIIDRRRAQFcqehdenskhdwwrqpwDANEI-----EGLSITMDDFEEATKMVQPSLRR 483
Cdd:TIGR01243 379 GFVGADLAALAKEAAMAALRRFIREGKINF-----------------EAEEIpaevlKELKVTMKDFMEALKMVEPSAIR 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 484 EGFSSIPDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGP 563
Cdd:TIGR01243 442 EVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 564 ELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRG-KEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRID 642
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGaRFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPD 601
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 643 VIDDAALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEERL-- 720
Cdd:TIGR01243 602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTE--GYTGADIEAVCREAAMAALRESIgs 679
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002279835 721 ---EFLENGESSMSSSSAIELPHFERALAKMQPSVSEQQRRHYEALCKKY 767
Cdd:TIGR01243 680 pakEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKEL 729
Nucleolin_bd super family cl25070
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
12-69 1.72e-03

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


The actual alignment was detected with superfamily member pfam16725:

Pssm-ID: 465247  Cd Length: 70  Bit Score: 37.61  E-value: 1.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835  12 RSHSPYFESQ-LRRLITDGGLSSSS-----AEDVAIALRSRFPEFRRHKLDPFTSAVRRALNSI 69
Cdd:pfam16725   1 KKRSGYFSDPrLVPRVEQYLEDNSDstyvdVDAMADELQRQYREYGRRKRNAFRIQVEKAYEII 64
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
169-767 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: 538.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 169 EAKPEsaPPSEGGDRGGKGPTFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANE 248
Cdd:TIGR01243 158 EIREK--PVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 249 TGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigs 328
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMD-------- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 329 gsgdvgsesAEKKPGYVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATS 408
Cdd:TIGR01243 308 ---------GLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTH 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 409 SFVGADLKALVDKAGNLAMKRIIDRRRAQFcqehdenskhdwwrqpwDANEI-----EGLSITMDDFEEATKMVQPSLRR 483
Cdd:TIGR01243 379 GFVGADLAALAKEAAMAALRRFIREGKINF-----------------EAEEIpaevlKELKVTMKDFMEALKMVEPSAIR 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 484 EGFSSIPDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGP 563
Cdd:TIGR01243 442 EVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 564 ELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRG-KEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRID 642
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGaRFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPD 601
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 643 VIDDAALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEERL-- 720
Cdd:TIGR01243 602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTE--GYTGADIEAVCREAAMAALRESIgs 679
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002279835 721 ---EFLENGESSMSSSSAIELPHFERALAKMQPSVSEQQRRHYEALCKKY 767
Cdd:TIGR01243 680 pakEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKEL 729
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
488-754 1.93e-95

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 300.00  E-value: 1.93e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 488 SIPDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLN 567
Cdd:COG1222    71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 568 KYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEG-GWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDD 646
Cdd:COG1222   151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGtSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 647 AALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEERLEfleng 726
Cdd:COG1222   231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRD----- 303
                         250       260
                  ....*....|....*....|....*...
gi 1002279835 727 essmssssAIELPHFERALAKMQPSVSE 754
Cdd:COG1222   304 --------TVTMEDLEKAIEKVKKKTET 323
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
192-373 1.60e-86

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: 270.81  E-value: 1.60e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEE 271
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 272 NIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDEyhqqigsgsgdVGSESAEKKPgyVIVIGAT 351
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDE-----------LNNEKTAGGP--VLVIGAT 147
                         170       180
                  ....*....|....*....|..
gi 1002279835 352 NRPDAVDQALRRPGRFDREISL 373
Cdd:cd19518   148 NRPDSLDPALRRAGRFDREICL 169
ftsH CHL00176
cell division protein; Validated
491-721 1.14e-67

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 235.71  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 491 DVTWDDVGGLDSLRKEFDRyIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYV 570
Cdd:CHL00176  179 GITFRDIAGIEEAKEEFEE-VVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 571 GESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKE-GGWVVER--LLNQLLIELDGAGERKGVFVIGATNRIDVIDDA 647
Cdd:CHL00176  258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiGGGNDEReqTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAA 337
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 648 ALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREecKNLTGADLASMVNEAAMAALEERLE 721
Cdd:CHL00176  338 LLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRT--PGFSGADLANLLNEAAILTARRKKA 409
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
533-662 3.63e-49

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 168.93  E-value: 3.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVV 612
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSES 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002279835 613 ERLLNQLLIELDGAGERKG-VFVIGATNRIDVIDDAALrpGRFGKKHYVPL 662
Cdd:pfam00004  82 RRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
490-769 1.18e-47

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 173.38  E-value: 1.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEeykTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPD---LFPLGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRA-----QTNTPCILFFDEVDALTTKRGKE-GGWVveRLLNQLLIELDG---AGERKGVFVIGATNR 640
Cdd:NF041006  175 LGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALLGVYSSEvGGEV--RVRNQFLKEMDGlqdKSENYHVYVIGATNK 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 641 IDVIDDAALRpgRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEerl 720
Cdd:NF041006  253 PWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTE--GYTASDIRDIVQAAHMRVVK--- 325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279835 721 EFLENGEssmSSSSAIELPHFERALAKMQPSVSEQQRRHYEALCKKYSA 769
Cdd:NF041006  326 EMFEKGL---GEPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKFKA 371
cell_div_CdvC NF041006
cell division protein CdvC;
189-484 1.43e-38

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 147.57  E-value: 1.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEV-----PRwlgvkpvaGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS 263
Cdd:NF041006  101 TFSDIVGLEDVKEALKEAIVYPSKRPDLfplgwPR--------GILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 264 GVSGASEENIRSLFKKAYRTA-----PSIVFIDEIDAIASKRENlQREMERRIVTQLMTCMDeyhqqigsGSGDVGSESa 338
Cdd:NF041006  173 KWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMD--------GLQDKSENY- 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 339 ekkpgYVIVIGATNRPDAVDQALRRpgRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKAL 418
Cdd:NF041006  243 -----HVYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDI 315
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279835 419 VDKAGNLAMKRIIDRrraqfcqehdenskhdwwrqpwdaNEIEGLSITMDDFEEATKMVQPSLRRE 484
Cdd:NF041006  316 VQAAHMRVVKEMFEK------------------------GLGEPRPITMEDFKEVLKIRKPSVNQE 357
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
533-663 6.57e-16

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: 75.49  E-value: 6.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835  533 LLFGPPGCGKTLIAKAVAHEAGANFIHIK-----------------GPELLNKYVGESESEVRKIFIRAQTNTPCILFFD 595
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDVLILD 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279835  596 EVDALTTKRGKEggwvvERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPgRFGKKHYVPLP 663
Cdd:smart00382  86 EITSLLDAEQEA-----LLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
12-69 1.72e-03

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


Pssm-ID: 465247  Cd Length: 70  Bit Score: 37.61  E-value: 1.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835  12 RSHSPYFESQ-LRRLITDGGLSSSS-----AEDVAIALRSRFPEFRRHKLDPFTSAVRRALNSI 69
Cdd:pfam16725   1 KKRSGYFSDPrLVPRVEQYLEDNSDstyvdVDAMADELQRQYREYGRRKRNAFRIQVEKAYEII 64
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
533-553 9.34e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.61  E-value: 9.34e-03
                          10        20
                  ....*....|....*....|.
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEA 553
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAA 114
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
169-767 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: 538.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 169 EAKPEsaPPSEGGDRGGKGPTFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANE 248
Cdd:TIGR01243 158 EIREK--PVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 249 TGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigs 328
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMD-------- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 329 gsgdvgsesAEKKPGYVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATS 408
Cdd:TIGR01243 308 ---------GLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTH 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 409 SFVGADLKALVDKAGNLAMKRIIDRRRAQFcqehdenskhdwwrqpwDANEI-----EGLSITMDDFEEATKMVQPSLRR 483
Cdd:TIGR01243 379 GFVGADLAALAKEAAMAALRRFIREGKINF-----------------EAEEIpaevlKELKVTMKDFMEALKMVEPSAIR 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 484 EGFSSIPDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGP 563
Cdd:TIGR01243 442 EVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 564 ELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRG-KEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRID 642
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGaRFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPD 601
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 643 VIDDAALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEERL-- 720
Cdd:TIGR01243 602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTE--GYTGADIEAVCREAAMAALRESIgs 679
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002279835 721 ---EFLENGESSMSSSSAIELPHFERALAKMQPSVSEQQRRHYEALCKKY 767
Cdd:TIGR01243 680 pakEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKEL 729
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
488-754 1.93e-95

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 300.00  E-value: 1.93e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 488 SIPDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLN 567
Cdd:COG1222    71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 568 KYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEG-GWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDD 646
Cdd:COG1222   151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGtSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 647 AALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEERLEfleng 726
Cdd:COG1222   231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRD----- 303
                         250       260
                  ....*....|....*....|....*...
gi 1002279835 727 essmssssAIELPHFERALAKMQPSVSE 754
Cdd:COG1222   304 --------TVTMEDLEKAIEKVKKKTET 323
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
192-373 1.60e-86

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: 270.81  E-value: 1.60e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEE 271
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 272 NIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDEyhqqigsgsgdVGSESAEKKPgyVIVIGAT 351
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDE-----------LNNEKTAGGP--VLVIGAT 147
                         170       180
                  ....*....|....*....|..
gi 1002279835 352 NRPDAVDQALRRPGRFDREISL 373
Cdd:cd19518   148 NRPDSLDPALRRAGRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
145-485 2.96e-84

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 270.72  E-value: 2.96e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 145 QQLEIEIAAEKPRRLITSDGGAGGEAKPESAPPSEGGDRGGKGP------TFSDLGGMESVIEQLMMEVVVPLCHPEVPR 218
Cdd:COG1222    26 GVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPaespdvTFDDIGGLDEQIEEIREAVELPLKNPELFR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 219 WLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIAS 298
Cdd:COG1222   106 KYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 299 KRENL-QREMERRIVTQLMTCMDEYhqqigsgsgdvgsesaeKKPGYVIVIGATNRPDAVDQALRRPGRFDREISLGVPD 377
Cdd:COG1222   186 RRTDDgTSGEVQRTVNQLLAELDGF-----------------ESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 378 EYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAGnlaMKRIIDRRRaqfcqehdenskhdwwrqpwda 457
Cdd:COG1222   249 EEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG---MFAIREGRD---------------------- 303
                         330       340
                  ....*....|....*....|....*...
gi 1002279835 458 neieglSITMDDFEEATKMVQPSLRREG 485
Cdd:COG1222   304 ------TVTMEDLEKAIEKVKKKTETAT 325
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
500-660 2.20e-81

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: 257.03  E-value: 2.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 500 LDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRK 579
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 580 IFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKKHY 659
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                  .
gi 1002279835 660 V 660
Cdd:cd19530   161 V 161
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
353-749 1.49e-76

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: 252.91  E-value: 1.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 353 RPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAGNLAMKRIID 432
Cdd:COG0464    15 LLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 433 RRRAQFCQEHDENSKHDWWRQPWDANEIEGLSITMDDFEEATKMVQPSLRREGFSSIPDVTWDDVGGLDSLRKEFDRYII 512
Cdd:COG0464    95 GELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 513 RCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCIL 592
Cdd:COG0464   175 LPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 593 FFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAgeRKGVFVIGATNRIDVIDDAALRpgRFGKKHYVPLPGADERVSIL 672
Cdd:COG0464   255 FIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIF 330
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279835 673 RALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEErleflengessmsSSSAIELPHFERALAKMQ 749
Cdd:COG0464   331 RIHLRKRPLDEDVDLEELAEATE--GLSGADIRNVVRRAALQALRL-------------GREPVTTEDLLEALERED 392
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
192-371 2.00e-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: 230.64  E-value: 2.00e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEE 271
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 272 NIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDEYhqqigsgsgdvgsesaeKKPGYVIVIGAT 351
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM-----------------SSRGKVVVIAAT 143
                         170       180
                  ....*....|....*....|
gi 1002279835 352 NRPDAVDQALRRPGRFDREI 371
Cdd:cd19503   144 NRPDAIDPALRRPGRFDREV 163
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
515-660 1.79e-68

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: 222.54  E-value: 1.79e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 515 IKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFF 594
Cdd:cd19511    13 LKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFF 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279835 595 DEVDALTTKRGKE-GGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYV 660
Cdd:cd19511    93 DEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
ftsH CHL00176
cell division protein; Validated
491-721 1.14e-67

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 235.71  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 491 DVTWDDVGGLDSLRKEFDRyIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYV 570
Cdd:CHL00176  179 GITFRDIAGIEEAKEEFEE-VVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 571 GESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKE-GGWVVER--LLNQLLIELDGAGERKGVFVIGATNRIDVIDDA 647
Cdd:CHL00176  258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiGGGNDEReqTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAA 337
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 648 ALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREecKNLTGADLASMVNEAAMAALEERLE 721
Cdd:CHL00176  338 LLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRT--PGFSGADLANLLNEAAILTARRKKA 409
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
490-719 2.70e-65

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 222.40  E-value: 2.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRAQTNTPCILFFDEVDALTTKR---GKEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDD 646
Cdd:PRK03992  206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 647 AALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEER 719
Cdd:PRK03992  286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTE--GASGADLKAICTEAGMFAIRDD 356
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
37-483 4.83e-65

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: 221.71  E-value: 4.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835  37 EDVAIALRSRFPEFRRHKLDPFTSAVRRALNSIPSDSHSDSADDSHASTPSQRRRRRPRHDAHATASSSTSLSDDAAHPP 116
Cdd:COG0464     1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 117 PPPIYDVTKSMLRTQYASQTPKRDTGSNQQLEIEIAAEKPRRLITSDGGAGGEAK--PESAPPSEGGDRGGKGPTFSDLG 194
Cdd:COG0464    81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLvtYEDIGGLEEELLELREAILDDLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 195 GMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIR 274
Cdd:COG0464   161 GLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 275 SLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDEYHQQigsgsgdvgsesaekkpgyVIVIGATNRP 354
Cdd:COG0464   241 EVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD-------------------VVVIAATNRP 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 355 DAVDQALRRpgRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAGNLAMkriidrr 434
Cdd:COG0464   302 DLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL------- 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279835 435 raqfcqehdenskhdwwrqpwdanEIEGLSITMDDFEEATKMVQPSLRR 483
Cdd:COG0464   373 ------------------------RLGREPVTTEDLLEALEREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
469-716 2.60e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 225.56  E-value: 2.60e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 469 DFEEATKMVQPsLRREGFSSIPDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKA 548
Cdd:TIGR01243 153 EATEVEIREKP-VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKA 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 549 VAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAGE 628
Cdd:TIGR01243 232 VANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKG 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 629 RKGVFVIGATNRIDVIDDAALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALArrEECKNLTGADLASMV 708
Cdd:TIGR01243 312 RGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLA--EVTHGFVGADLAALA 389

                  ....*...
gi 1002279835 709 NEAAMAAL 716
Cdd:TIGR01243 390 KEAAMAAL 397
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
192-374 4.72e-63

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: 208.44  E-value: 4.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEE 271
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 272 NIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigsgsgdvgsesAEKKPGYVIVIGAT 351
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMD-----------------GLKQRAHVIVMAAT 143
                         170       180
                  ....*....|....*....|...
gi 1002279835 352 NRPDAVDQALRRPGRFDREISLG 374
Cdd:cd19519   144 NRPNSIDPALRRFGRFDREIDIG 166
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
490-758 1.44e-61

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: 215.23  E-value: 1.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFdRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKE-GGW--VVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDD 646
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlGGGndEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 647 AALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARReeCKNLTGADLASMVNEAAMAALEERLEfleng 726
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARR--TPGFSGADLANLLNEAALLAARKNKT----- 281
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1002279835 727 essmssssAIELPHFERA-------LAKMQPSVSEQQRR 758
Cdd:TIGR01241 282 --------EITMNDIEEAidrviagPEKKSRVISEKEKK 312
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
189-478 4.43e-60

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 208.15  E-value: 4.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGA 268
Cdd:PRK03992  129 TYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGE 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 269 SEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENL----QREMERRIVtQLMTCMDEYhqqigSGSGDVGsesaekkpgy 344
Cdd:PRK03992  209 GARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSgtsgDREVQRTLM-QLLAEMDGF-----DPRGNVK---------- 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 345 viVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAGn 424
Cdd:PRK03992  273 --IIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAG- 349
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 425 laMKRIIDRRRaqfcqehdenskhdwwrqpwdaneieglSITMDDFEEATKMVQ 478
Cdd:PRK03992  350 --MFAIRDDRT----------------------------EVTMEDFLKAIEKVM 373
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
189-429 5.15e-58

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: 201.57  E-value: 5.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGA 268
Cdd:TIGR01242 120 SYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGE 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 269 SEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENL----QREMERRIVtQLMTCMDEYHQQigsgsGDVGsesaekkpgy 344
Cdd:TIGR01242 200 GARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSgtsgDREVQRTLM-QLLAELDGFDPR-----GNVK---------- 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 345 viVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAGN 424
Cdd:TIGR01242 264 --VIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGM 341

                  ....*
gi 1002279835 425 LAMKR 429
Cdd:TIGR01242 342 FAIRE 346
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
515-660 3.05e-57

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: 192.34  E-value: 3.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 515 IKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFF 594
Cdd:cd19528    13 VEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFF 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 595 DEVDALTTKRG---KEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYV 660
Cdd:cd19528    93 DELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
515-660 7.62e-57

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: 191.17  E-value: 7.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 515 IKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFF 594
Cdd:cd19529    13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279835 595 DEVDALTTKRGKEGG-WVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYV 660
Cdd:cd19529    93 DEIDSIAPRRGTTGDsGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
516-656 1.41e-56

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: 190.33  E-value: 1.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 516 KQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFFD 595
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002279835 596 EVDALTTKRGKEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGK 656
Cdd:cd19526    94 EFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
496-654 2.02e-55

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: 187.50  E-value: 2.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESES 575
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 576 EVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRF 654
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRF 159
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
490-745 2.52e-55

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 200.26  E-value: 2.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLD----SLR--KEFdryiircIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGP 563
Cdd:COG0465   137 PKVTFDDVAGVDeakeELQeiVDF-------LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 564 ELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGK-EGGWVVER--LLNQLLIELDGAGERKGVFVIGATNR 640
Cdd:COG0465   210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAgLGGGHDEReqTLNQLLVEMDGFEGNEGVIVIAATNR 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 641 IDVIDDAALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARReecknlT----GADLASMVNEAA-MAA 715
Cdd:COG0465   290 PDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARR------TpgfsGADLANLVNEAAlLAA 363
                         250       260       270
                  ....*....|....*....|....*....|
gi 1002279835 716 LEERleflengessmsssSAIELPHFERAL 745
Cdd:COG0465   364 RRNK--------------KAVTMEDFEEAI 379
ftsH CHL00176
cell division protein; Validated
186-429 4.82e-55

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 200.66  E-value: 4.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 186 KGPTFSDLGGMESVIEQLMmEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGV 265
Cdd:CHL00176  178 TGITFRDIAGIEEAKEEFE-EVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 266 SGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKR------ENLQREmerRIVTQLMTCMDEYHQQIGsgsgdvgsesae 339
Cdd:CHL00176  257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagiggGNDERE---QTLNQLLTEMDGFKGNKG------------ 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 340 kkpgyVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALV 419
Cdd:CHL00176  322 -----VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLL 396
                         250
                  ....*....|
gi 1002279835 420 DKAGNLAMKR 429
Cdd:CHL00176  397 NEAAILTARR 406
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
189-485 9.02e-54

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: 193.66  E-value: 9.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMmEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS---GV 265
Cdd:TIGR01241  53 TFKDVAGIDEAKEELM-EIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfvGV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 266 sGASEenIRSLFKKAYRTAPSIVFIDEIDAIASKR------ENLQREmerRIVTQLMTCMDeyhqqigsgsgdvGSESAE 339
Cdd:TIGR01241 132 -GASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglggGNDERE---QTLNQLLVEMD-------------GFGTNT 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 340 KkpgyVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALV 419
Cdd:TIGR01241 193 G----VIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLL 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279835 420 DKAGNLAMKRiidRRRAqfcqehdenskhdwwrqpwdaneieglsITMDDFEEATKMVQPSLRREG 485
Cdd:TIGR01241 269 NEAALLAARK---NKTE----------------------------ITMNDIEEAIDRVIAGPEKKS 303
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
189-473 2.12e-53

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 194.49  E-value: 2.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMmEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS---GV 265
Cdd:COG0465   140 TFDDVAGVDEAKEELQ-EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfvGV 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 266 sGASEenIRSLFKKAYRTAPSIVFIDEIDAIASKR---------EnlqREmerRIVTQLMTCMDeyhqqigsgsgdvGSE 336
Cdd:COG0465   219 -GASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglggghdE---RE---QTLNQLLVEMD-------------GFE 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 337 SAEKkpgyVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLK 416
Cdd:COG0465   277 GNEG----VIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLA 352
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279835 417 ALVDKAGNLAMkriidRRRAQfcqehdenskhdwwrqpwdaneieglSITMDDFEEA 473
Cdd:COG0465   353 NLVNEAALLAA-----RRNKK--------------------------AVTMEDFEEA 378
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
492-660 2.74e-52

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: 179.35  E-value: 2.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 492 VTWDDVGGLDSLRKEFdRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVG 571
Cdd:cd19501     1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 572 ESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGW---VVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAA 648
Cdd:cd19501    80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGghdEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                         170
                  ....*....|..
gi 1002279835 649 LRPGRFGKKHYV 660
Cdd:cd19501   160 LRPGRFDRQVYV 171
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
493-657 3.31e-52

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: 179.07  E-value: 3.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 493 TWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGE 572
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 573 SESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWV---VERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAAL 649
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGdreVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                  ....*...
gi 1002279835 650 RPGRFGKK 657
Cdd:cd19502   161 RPGRFDRK 168
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
190-449 2.68e-51

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 179.31  E-value: 2.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 190 FSDLGGMESV---IEQLMMEvvvpLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVS 266
Cdd:COG1223     1 LDDVVGQEEAkkkLKLIIKE----LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 267 GASEENIRSLFKKAyRTAPSIVFIDEIDAIASKR--ENLQREMeRRIVTQLMTCMDEYhqqigsgsgdvgsesaekkPGY 344
Cdd:COG1223    77 GETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRgdQNDVGEV-KRVVNALLQELDGL-------------------PSG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 345 VIVIGATNRPDAVDQALRRpgRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAgn 424
Cdd:COG1223   136 SVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA-- 211
                         250       260
                  ....*....|....*....|....*
gi 1002279835 425 lamkriidrRRAQFCQEHDENSKHD 449
Cdd:COG1223   212 ---------LKKAILEDREKVTKED 227
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
490-716 2.57e-50

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 181.50  E-value: 2.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:PTZ00454  140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRAQTNTPCILFFDEVDALTTKR-------GKEggwvVERLLNQLLIELDGAGERKGVFVIGATNRID 642
Cdd:PTZ00454  220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaqtgaDRE----VQRILLELLNQMDGFDQTTNVKVIMATNRAD 295
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 643 VIDDAALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAAL 716
Cdd:PTZ00454  296 TLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPE--KISAADIAAICQEAGMQAV 367
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
205-373 5.75e-50

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: 172.47  E-value: 5.75e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 205 MEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTA 284
Cdd:cd19481     6 REAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 285 PSIVFIDEIDAIASKRENL-QREMERRIVTQLMTCMDEYHQQIGsgsgdvgsesaekkpgyVIVIGATNRPDAVDQALRR 363
Cdd:cd19481    86 PCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSK-----------------VLVIAATNRPDLLDPALLR 148
                         170
                  ....*....|
gi 1002279835 364 PGRFDREISL 373
Cdd:cd19481   149 PGRFDEVIEF 158
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
511-657 9.22e-50

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: 171.70  E-value: 9.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 511 IIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPC 590
Cdd:cd19481     8 AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPC 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279835 591 ILFFDEVDALTTKRGKEGGW-VVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKK 657
Cdd:cd19481    88 ILFIDEIDAIGRKRDSSGESgELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
511-660 1.76e-49

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: 171.16  E-value: 1.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 511 IIRCIKQPEEYKTF---GLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTN 587
Cdd:cd19527     5 ILDTIQLPLEHPELfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDA 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279835 588 TPCILFFDEVDALTTKRGKEG--GWVVERLLNQLLIELDG-AGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYV 660
Cdd:cd19527    85 KPCVIFFDELDSLAPSRGNSGdsGGVMDRVVSQLLAELDGmSSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
199-371 2.23e-49

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: 170.93  E-value: 2.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 199 VIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFK 278
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 279 KAYRTAPSIVFIDEIDAIASKR-ENLQREMERRIVTQLMTCMDeyhqqigsgsgdvGSESAEKkpgyVIVIGATNRPDAV 357
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD-------------GIESLKG----VVVIAATNRPDMI 143
                         170
                  ....*....|....
gi 1002279835 358 DQALRRPGRFDREI 371
Cdd:cd19511   144 DPALLRPGRLDKLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
186-441 3.04e-49

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 179.58  E-value: 3.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 186 KGP--TFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS 263
Cdd:PTZ00361  176 KAPleSYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 264 GVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMER---RIVTQLMTCMDEYHQQigsgsGDVGsesaek 340
Cdd:PTZ00361  256 KYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKeiqRTMLELLNQLDGFDSR-----GDVK------ 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 341 kpgyviVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVD 420
Cdd:PTZ00361  325 ------VIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICT 398
                         250       260
                  ....*....|....*....|.
gi 1002279835 421 KAGNLAMKriidRRRAQFCQE 441
Cdd:PTZ00361  399 EAGLLALR----ERRMKVTQA 415
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
533-662 3.63e-49

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 168.93  E-value: 3.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVV 612
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSES 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002279835 613 ERLLNQLLIELDGAGERKG-VFVIGATNRIDVIDDAALrpGRFGKKHYVPL 662
Cdd:pfam00004  82 RRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
496-654 1.34e-48

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: 168.77  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESES 575
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 576 EVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRF 654
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRF 159
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
489-724 1.80e-48

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: 179.13  E-value: 1.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 489 IPDVTWDDVGGLDSLrkefdryiIRCIK--------QPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGAN---- 556
Cdd:TIGR03689 176 VPDVTYADIGGLGSQ--------IEQIRdavelpflHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARigae 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 557 ------FIHIKGPELLNKYVGESESEVRKIFIRAQ----TNTPCILFFDEVDALTTKRGKEGGWVVER-LLNQLLIELDG 625
Cdd:TIGR03689 248 gggksyFLNIKGPELLNKYVGETERQIRLIFQRARekasEGRPVIVFFDEMDSLFRTRGSGVSSDVETtVVPQLLAEIDG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 626 AGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYVPLPGADERVSIL-RALARNKPISSsvDLGALARREEcknltgADL 704
Cdd:TIGR03689 328 VESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDDLPLPE--DLAAHDGDRE------ATA 399
                         250       260
                  ....*....|....*....|..
gi 1002279835 705 ASMVNEA--AMAALEERLEFLE 724
Cdd:TIGR03689 400 AALIQRVvdALYARSEANRYVE 421
cell_div_CdvC NF041006
cell division protein CdvC;
490-769 1.18e-47

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 173.38  E-value: 1.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEeykTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPD---LFPLGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRA-----QTNTPCILFFDEVDALTTKRGKE-GGWVveRLLNQLLIELDG---AGERKGVFVIGATNR 640
Cdd:NF041006  175 LGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALLGVYSSEvGGEV--RVRNQFLKEMDGlqdKSENYHVYVIGATNK 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 641 IDVIDDAALRpgRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEerl 720
Cdd:NF041006  253 PWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTE--GYTASDIRDIVQAAHMRVVK--- 325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279835 721 EFLENGEssmSSSSAIELPHFERALAKMQPSVSEQQRRHYEALCKKYSA 769
Cdd:NF041006  326 EMFEKGL---GEPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKFKA 371
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
228-371 1.94e-47

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: 164.30  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREM 307
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 308 ERRIVTQLMTCMDEYhqqigsgsgdvgsesaEKKPGYVIVIGATNRPDAVDQALRrpGRFDREI 371
Cdd:pfam00004  81 SRRVVNQLLTELDGF----------------TSSNSKVIVIAATNRPDKLDPALL--GRFDRII 126
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
189-371 3.31e-47

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 165.10  E-value: 3.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMmEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS---GV 265
Cdd:cd19501     2 TFKDVAGCEEAKEELK-EVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfvGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 266 sGASEenIRSLFKKAYRTAPSIVFIDEIDAIASKR------ENLQREmerRIVTQLMTCMDEYhqqiGSGSGdvgsesae 339
Cdd:cd19501    81 -GASR--VRDLFEQAKKNAPCIVFIDEIDAVGRKRgaglggGHDERE---QTLNQLLVEMDGF----ESNTG-------- 142
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1002279835 340 kkpgyVIVIGATNRPDAVDQALRRPGRFDREI 371
Cdd:cd19501   143 -----VIVIAATNRPDVLDPALLRPGRFDRQV 169
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
493-715 1.72e-46

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 175.99  E-value: 1.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 493 TWDDVGGLDSLRKEFDRyIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGE 572
Cdd:PRK10733  150 TFADVAGCDEAKEEVAE-LVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 573 SESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKE-GGWVVER--LLNQLLIELDGAGERKGVFVIGATNRIDVIDDAAL 649
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlGGGHDEReqTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279835 650 RPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARreECKNLTGADLASMVNEAAMAA 715
Cdd:PRK10733  309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIAR--GTPGFSGADLANLVNEAALFA 372
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
494-724 7.49e-46

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 164.29  E-value: 7.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 494 WDDVGGLDSLRKEFDRyIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGES 573
Cdd:COG1223     1 LDDVVGQEEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 574 ESEVRKIFIRAQtNTPCILFFDEVDALTTKRG--KEGGWVVeRLLNQLLIELDgaGERKGVFVIGATNRIDVIDDAALRp 651
Cdd:COG1223    80 ARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGdqNDVGEVK-RVVNALLQELD--GLPSGSVVIAATNHPELLDSALWR- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 652 gRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALArrEECKNLTGADLASMVNEAAMAALEERLEFLE 724
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLA--KKLEGLSGADIEKVLKTALKKAILEDREKVT 224
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
199-371 2.31e-45

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 159.58  E-value: 2.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 199 VIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFK 278
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 279 KAYRTAPSIVFIDEIDAIASKR-ENLQREMERRIVTQLMTCMDeyhqqigsgsgdvGSESAEKkpgyVIVIGATNRPDAV 357
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELD-------------GLEEMNG----VVVIAATNRPDII 143
                         170
                  ....*....|....
gi 1002279835 358 DQALRRPGRFDREI 371
Cdd:cd19529   144 DPALLRAGRFDRLI 157
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
189-371 1.16e-44

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: 158.27  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGA 268
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 269 SEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMER---RIVTQLMTCMDEYHQqigsgSGDVGsesaekkpgyv 345
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDP-----RGNIK----------- 144
                         170       180
                  ....*....|....*....|....*.
gi 1002279835 346 iVIGATNRPDAVDQALRRPGRFDREI 371
Cdd:cd19502   145 -VIMATNRPDILDPALLRPGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
189-429 1.92e-44

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 164.94  E-value: 1.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGA 268
Cdd:PTZ00454  143 TYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 269 SEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQ----REMErRIVTQLMTCMDEYHQQIGsgsgdvgsesaekkpgy 344
Cdd:PTZ00454  223 GPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQtgadREVQ-RILLELLNQMDGFDQTTN----------------- 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 345 VIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKAGN 424
Cdd:PTZ00454  285 VKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGM 364

                  ....*
gi 1002279835 425 LAMKR 429
Cdd:PTZ00454  365 QAVRK 369
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
497-660 1.83e-43

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: 154.43  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 497 VGGLDSLRKEFDRYIIRCIKQPEEYKTfGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESESE 576
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPG-LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 577 VRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAG--ERKGVFVIGATNRIDVIDDAALRpgRF 654
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR--RF 157

                  ....*.
gi 1002279835 655 GKKHYV 660
Cdd:cd19509   158 EKRIYI 163
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
490-719 1.28e-42

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 160.71  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:PTZ00361  178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRAQTNTPCILFFDEVDALTTKR--GKEGGWV-VERLLNQLLIELDGAGERKGVFVIGATNRIDVIDD 646
Cdd:PTZ00361  258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydATSGGEKeIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 647 AALRPGRFGKKHYVPLPGADERVSILRALARNKPISSSVDLGALARREEckNLTGADLASMVNEAAMAALEER 719
Cdd:PTZ00361  338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKD--ELSGADIKAICTEAGLLALRER 408
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
496-654 5.26e-42

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: 150.63  E-value: 5.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESES 575
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 576 EVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDG----AGERKGVFVIGATNRIDVIDDAALRP 651
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDElnneKTAGGPVLVIGATNRPDSLDPALRRA 160

                  ...
gi 1002279835 652 GRF 654
Cdd:cd19518   161 GRF 163
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
189-428 6.03e-42

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 162.90  E-value: 6.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMmEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGA 268
Cdd:PRK10733  150 TFADVAGCDEAKEEVA-ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 269 SEENIRSLFKKAYRTAPSIVFIDEIDAIASKRE------NLQREmerRIVTQLMTCMDEYHqqigsgsgdvGSESaekkp 342
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglgggHDERE---QTLNQMLVEMDGFE----------GNEG----- 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 343 gyVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKALVDKA 422
Cdd:PRK10733  291 --IIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEA 368

                  ....*.
gi 1002279835 423 GNLAMK 428
Cdd:PRK10733  369 ALFAAR 374
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
192-370 1.07e-40

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: 146.89  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETG-----VPFYKISAPEVVSGVS 266
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 267 GASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDEYHQQigsgsgdvgsesaekkpGYVI 346
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNR-----------------GQVV 143
                         170       180
                  ....*....|....*....|....
gi 1002279835 347 VIGATNRPDAVDQALRRPGRFDRE 370
Cdd:cd19517   144 VIGATNRPDALDPALRRPGRFDRE 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
193-371 1.69e-40

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: 145.96  E-value: 1.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 193 LGGMESVIEQLMMEVVVPLCHPEVPRwLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEEN 272
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 273 IRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigsgsGDVGSESaekkpGYVIVIGATN 352
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMD----------GVLNKPE-----DRVLVLGATN 144
                         170
                  ....*....|....*....
gi 1002279835 353 RPDAVDQALRRpgRFDREI 371
Cdd:cd19509   145 RPWELDEAFLR--RFEKRI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
196-369 3.30e-40

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 145.32  E-value: 3.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 196 MESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRS 275
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 276 LFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigsgsgdvGSESAEKkpgyVIVIGATNRPD 355
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMD-------------GLEERSN----VFVIAATNRPD 143
                         170
                  ....*....|....
gi 1002279835 356 AVDQALRRPGRFDR 369
Cdd:cd19530   144 IIDPAMLRPGRLDK 157
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
199-371 8.67e-40

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 144.19  E-value: 8.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 199 VIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFK 278
Cdd:cd19528     1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 279 KAYRTAPSIVFIDEIDAIASKRENLQRE---MERRIVTQLMTCMDEYHQqigsgsgdvgsesaeKKPgyVIVIGATNRPD 355
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNT---------------KKN--VFIIGATNRPD 143
                         170
                  ....*....|....*.
gi 1002279835 356 AVDQALRRPGRFDREI 371
Cdd:cd19528   144 IIDPAILRPGRLDQLI 159
cell_div_CdvC NF041006
cell division protein CdvC;
189-484 1.43e-38

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 147.57  E-value: 1.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEV-----PRwlgvkpvaGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS 263
Cdd:NF041006  101 TFSDIVGLEDVKEALKEAIVYPSKRPDLfplgwPR--------GILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 264 GVSGASEENIRSLFKKAYRTA-----PSIVFIDEIDAIASKRENlQREMERRIVTQLMTCMDeyhqqigsGSGDVGSESa 338
Cdd:NF041006  173 KWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMD--------GLQDKSENY- 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 339 ekkpgYVIVIGATNRPDAVDQALRRpgRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARATSSFVGADLKAL 418
Cdd:NF041006  243 -----HVYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDI 315
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279835 419 VDKAGNLAMKRIIDRrraqfcqehdenskhdwwrqpwdaNEIEGLSITMDDFEEATKMVQPSLRRE 484
Cdd:NF041006  316 VQAAHMRVVKEMFEK------------------------GLGEPRPITMEDFKEVLKIRKPSVNQE 357
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
189-422 2.20e-37

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: 147.16  E-value: 2.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIAN--------ETGVP--FYKISA 258
Cdd:TIGR03689 180 TYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaEGGGKsyFLNIKG 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 259 PEVVSGVSGASEENIRSLFKKAYRTA----PSIVFIDEIDAIASKR-ENLQREMERRIVTQLMTCMDeyhqqigsgsgdv 333
Cdd:TIGR03689 260 PELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRgSGVSSDVETTVVPQLLAEID------------- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 334 GSESAEKkpgyVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILM-MLTRNLRLEGQLdllkiaRATSSFVG 412
Cdd:TIGR03689 327 GVESLDN----VIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAkYLTDDLPLPEDL------AAHDGDRE 396
                         250
                  ....*....|
gi 1002279835 413 ADLKALVDKA 422
Cdd:TIGR03689 397 ATAAALIQRV 406
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
200-371 2.42e-36

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: 134.09  E-value: 2.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 200 IEQLMMEVVV-PLCHPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFK 278
Cdd:cd19526     1 VKKALEETIEwPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 279 KAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigsgsgdvGSESAEKkpgyVIVIGATNRPDAVD 358
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLD-------------GVEGLDG----VYVLAATSRPDLID 143
                         170
                  ....*....|...
gi 1002279835 359 QALRRPGRFDREI 371
Cdd:cd19526   144 PALLRPGRLDKLV 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
490-660 2.36e-35

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: 131.91  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYkTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAG-ERKGVFVIGATNRIDVIDDAA 648
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGnDSQGVLVLGATNIPWQLDSAI 160
                         170
                  ....*....|..
gi 1002279835 649 LRpgRFGKKHYV 660
Cdd:cd19521   161 RR--RFEKRIYI 170
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
199-369 6.03e-35

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: 130.33  E-value: 6.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 199 VIEQLMMEVVVPLCHPEVPRwLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFK 278
Cdd:cd19527     1 VKKEILDTIQLPLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 279 KAYRTAPSIVFIDEIDAIASKRENLQRE--MERRIVTQLMTCMDEYHqqiGSGSGdvgsesaekkpgyVIVIGATNRPDA 356
Cdd:cd19527    80 KARDAKPCVIFFDELDSLAPSRGNSGDSggVMDRVVSQLLAELDGMS---SSGQD-------------VFVIGATNRPDL 143
                         170
                  ....*....|...
gi 1002279835 357 VDQALRRPGRFDR 369
Cdd:cd19527   144 LDPALLRPGRFDK 156
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
497-654 6.16e-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: 131.07  E-value: 6.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 497 VGGLDS-LRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHI-KGPELLNKYVGESE 574
Cdd:cd19504     2 IGGLDKeFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 575 SEVRKIFIRAQTNTPC--------ILFFDEVDALTTKRGKEGG--WVVERLLNQLLIELDGAGERKGVFVIGATNRIDVI 644
Cdd:cd19504    82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGstGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLI 161
                         170
                  ....*....|
gi 1002279835 645 DDAALRPGRF 654
Cdd:cd19504   162 DEALLRPGRL 171
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
496-654 1.57e-34

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: 129.47  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKTFGL-NMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESE 574
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 575 SEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDG--AGERKGVFVIGATNRIDVIDDAALR-- 650
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGlsTDGNCRVIVMGATNRPQDLDEAILRrm 160

                  ....
gi 1002279835 651 PGRF 654
Cdd:cd19520   161 PKRF 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
496-660 2.92e-33

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: 125.73  E-value: 2.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKtfGLNMQA-GFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESE 574
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 575 SEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGA--GERKGVFVIGATNRIDVIDDAALRpg 652
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR-- 156

                  ....*...
gi 1002279835 653 RFGKKHYV 660
Cdd:cd19524   157 RFTKRVYV 164
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
192-367 4.04e-33

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: 125.23  E-value: 4.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGV-KPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASE 270
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 271 ENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqiGSGSGDVGSesaekkpgyVIVIGA 350
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWD------GLSTDGNCR---------VIVMGA 145
                         170
                  ....*....|....*....
gi 1002279835 351 TNRPDAVDQALRR--PGRF 367
Cdd:cd19520   146 TNRPQDLDEAILRrmPKRF 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
190-371 5.50e-33

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 124.97  E-value: 5.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 190 FSDLGGMESVIEQLMMEVVVPLCHPEVPRWlGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGAS 269
Cdd:cd19521     6 WEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGES 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 270 EENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqiGSGSGDVGsesaekkpgyVIVIG 349
Cdd:cd19521    85 EKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMN------GVGNDSQG----------VLVLG 148
                         170       180
                  ....*....|....*....|..
gi 1002279835 350 ATNRPDAVDQALRRpgRFDREI 371
Cdd:cd19521   149 ATNIPWQLDSAIRR--RFEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
490-660 8.96e-33

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: 125.10  E-value: 8.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYKtfGLNMQ-AGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNK 568
Cdd:cd19525    17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFT--GLRGPpKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 569 YVGESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGA--GERKGVFVIGATNRIDVIDD 646
Cdd:cd19525    95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDE 174
                         170
                  ....*....|....
gi 1002279835 647 AALRpgRFGKKHYV 660
Cdd:cd19525   175 AARR--RLVKRLYI 186
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
496-659 1.53e-32

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: 123.77  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGAN-----FIHIKGPELLNKYV 570
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGgqkvsFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 571 GESESEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALR 650
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                  ....*....
gi 1002279835 651 PGRFGKKHY 659
Cdd:cd19517   161 PGRFDREFY 169
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
192-371 7.13e-32

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: 122.02  E-value: 7.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVprWLGVK-PVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASE 270
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEF--FKGIRrPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 271 ENIRSLFKKAYRTAPSIVFIDEIDAIASKR-ENLQREMERRIVTQLMTCMDeyhqqiGSGSGDVGSESAEkkpgYVIVIG 349
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMD------GVGGASENDDPSK----MVMVLA 148
                         170       180
                  ....*....|....*....|..
gi 1002279835 350 ATNRPDAVDQALRRpgRFDREI 371
Cdd:cd19522   149 ATNFPWDIDEALRR--RLEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
190-371 4.77e-29

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 114.31  E-value: 4.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 190 FSDLGGMESVIEQLMMEVVVPLCHPEVprWLGVK-PVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGA 268
Cdd:cd19525    21 WADIAGLEFAKKTIKEIVVWPMLRPDI--FTGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 269 SEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDeyhqqigsgsgDVGSESAEKkpgyVIVI 348
Cdd:cd19525    99 GEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLD-----------GATTSSEDR----ILVV 163
                         170       180
                  ....*....|....*....|...
gi 1002279835 349 GATNRPDAVDQALRRpgRFDREI 371
Cdd:cd19525   164 GATNRPQEIDEAARR--RLVKRL 184
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
192-371 1.32e-28

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: 112.25  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVprWLGVK-PVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASE 270
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPEL--FTGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 271 ENIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQREMERRIVTQLMTCMDEYHqqigSGSGDVgsesaekkpgyVIVIGA 350
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQ----SNGDDR-----------VLVMGA 143
                         170       180
                  ....*....|....*....|.
gi 1002279835 351 TNRPDAVDQALRRpgRFDREI 371
Cdd:cd19524   144 TNRPQELDDAVLR--RFTKRV 162
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
496-660 5.00e-27

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 108.15  E-value: 5.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKtfGLNMQ-AGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESE 574
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 575 SEVRKIFIRAQTNTPCILFFDEVDALTTKRGKEGGW-VVERLLNQLLIELDGAG-------ERKGVFVIGATNRIDVIDD 646
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHeASRRVKSELLVQMDGVGgasenddPSKMVMVLAATNFPWDIDE 158
                         170
                  ....*....|....
gi 1002279835 647 AALRpgRFGKKHYV 660
Cdd:cd19522   159 ALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
214-373 1.27e-25

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 104.11  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 214 PEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKI-SAPEVVSGVSGASEENIRSLFKKA---YRTAPS--- 286
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAeeeQRRLGAnsg 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 287 --IVFIDEIDAIASKRENLQRE--MERRIVTQLMTCMDeyhqqigsgsgdvGSESAEKkpgyVIVIGATNRPDAVDQALR 362
Cdd:cd19504   104 lhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKID-------------GVEQLNN----ILVIGMTNRKDLIDEALL 166
                         170
                  ....*....|.
gi 1002279835 363 RPGRFDREISL 373
Cdd:cd19504   167 RPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
530-662 2.12e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 102.61  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 530 AGFLLFGPPGCGKTLIAKAVAHEA---GANFIHIKGPELLNKYVGESE---SEVRKIFIRAQTNTPCILFFDEVDALttk 603
Cdd:cd00009    20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELfghFLVRLLFELAEKAKPGVLFIDEIDSL--- 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 604 rgkeGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYVPL 662
Cdd:cd00009    97 ----SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
490-722 1.01e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 108.57  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 490 PDVTWDDVGGLDSLRKEFDRYIIRCIKQPEEYktfGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKY 569
Cdd:CHL00195  223 VNEKISDIGGLDNLKDWLKKRSTSFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 570 VGESESEVRKIFIRAQTNTPCILFFDEVD-ALTTKRGKEGGWVVERLLNQLLIELdgAGERKGVFVIGATNRIDVIDDAA 648
Cdd:CHL00195  300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWL--SEKKSPVFVVATANNIDLLPLEI 377
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279835 649 LRPGRFGKKHYVPLPGADERVSILRA-LARNKPIS-SSVDLGALArrEECKNLTGADLASMVNEAAMAALEERLEF 722
Cdd:CHL00195  378 LRKGRFDEIFFLDLPSLEEREKIFKIhLQKFRPKSwKKYDIKKLS--KLSNKFSGAEIEQSIIEAMYIAFYEKREF 451
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
223-374 1.31e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 100.30  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 223 KPVAGLLLHGPPGCGKTTLAHAIANET---GVPFYKISAPEVVSGVSGASEEN---IRSLFKKAYRTAPSIVFIDEIDAi 296
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDS- 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279835 297 askrenlqreMERRIVTQLMTCMDEYHQQIGSGSGdvgsesaekkpgyVIVIGATNRPDAVDQALRRPGRFDREISLG 374
Cdd:cd00009    96 ----------LSRGAQNALLRVLETLNDLRIDREN-------------VRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
496-660 7.11e-23

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 95.90  E-value: 7.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYktfGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESES 575
Cdd:cd19507     1 DVGGLDNLKDWLKKRKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 576 EVRKIFIRAQTNTPCILFFDEVD-ALTTKRGKEGGWVVERLLNQLLIELDgagERKG-VFVIGATNRIDVIDDAALRPGR 653
Cdd:cd19507    78 RLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ---EKKKpVFVVATANNVQSLPPELLRKGR 154

                  ....*..
gi 1002279835 654 FGKKHYV 660
Cdd:cd19507   155 FDEIFFV 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
496-660 2.11e-20

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 88.79  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 496 DVGGLDSLRKEFDRYIIRCIKQPEEYKTFgLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLNKYVGESES 575
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 576 EVRKIFIRAQTNTPCILFFDEVDALTTKRgKEGGWVVERLLNQLLIELDG---AGErKGVFVIGATNRIDVIDDAALRpg 652
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGvlgSGE-DGVLVVCTTSKPEEIDESLRR-- 155

                  ....*...
gi 1002279835 653 RFGKKHYV 660
Cdd:cd19523   156 YFSKRLLV 163
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
221-369 1.15e-17

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 80.88  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 221 GVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEID-AIASK 299
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 300 RENLQREMERRIVTQLMTCMDEyhqqigsgsgdvgsesaEKKPgyVIVIGATNRPDAVDQALRRPGRFDR 369
Cdd:cd19507   107 DSKGDSGTSSRVLGTFLTWLQE-----------------KKKP--VFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
192-363 3.02e-17

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: 79.54  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 192 DLGGMESVIEQLMMEVVVPLCHPEVPRWLGVKPVAgLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEE 271
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRS-ILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 272 NIRSLFKKAYRTAPSIVFIDEIDAIASKRENlQREMERRIVTQLMTCMDEyhqqiGSGSGDVGsesaekkpgyVIVIGAT 351
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDD-EASPVGRLQVELLAQLDG-----VLGSGEDG----------VLVVCTT 143
                         170
                  ....*....|..
gi 1002279835 352 NRPDAVDQALRR 363
Cdd:cd19523   144 SKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
533-663 6.57e-16

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: 75.49  E-value: 6.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835  533 LLFGPPGCGKTLIAKAVAHEAGANFIHIK-----------------GPELLNKYVGESESEVRKIFIRAQTNTPCILFFD 595
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDVLILD 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279835  596 EVDALTTKRGKEggwvvERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPgRFGKKHYVPLP 663
Cdd:smart00382  86 EITSLLDAEQEA-----LLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
227-371 1.81e-15

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: 74.31  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSgvsgaSEENIRSLFkkayRTAP--SIVFIDEIDAIASKRE--- 301
Cdd:cd19510    25 GYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLL----NTAPkqSIILLEDIDAAFESREhnk 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 302 ---NLQREMERRIVTQLMTCMDeyhqqigsgsgdvGSESAEKKpgyvIVIGATNRPDAVDQALRRPGRFDREI 371
Cdd:cd19510    96 knpSAYGGLSRVTFSGLLNALD-------------GVASSEER----IVFMTTNHIERLDPALIRPGRVDMKI 151
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
228-293 3.10e-15

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 78.59  E-value: 3.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISApeVVSGVsgaseENIRSLFKKAYRTAPS----IVFIDEI 293
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSA--VTSGV-----KDLREVIEEARQRRSAgrrtILFIDEI 101
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
228-377 3.14e-15

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 73.56  E-value: 3.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835  228 LLLHGPPGCGKTTLAHAIANETGVPFYKI-----------------SAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFI 290
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPDVLIL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835  291 DEIDAIASKRENLQREMERRIVTQLMtcmdeyhqqigsgsgdvgsesaEKKPGYVIVIGATNRPDAVDQALRRPgRFDRE 370
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEELRLLLL----------------------LKSEKNLTVILTTNDEKDLGPALLRR-RFDRR 141

                   ....*..
gi 1002279835  371 ISLGVPD 377
Cdd:smart00382 142 IVLLLIL 148
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
228-293 5.73e-15

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 77.79  E-value: 5.73e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISApeVVSGVSgaseeNIRSLFKKAYRTA----PSIVFIDEI 293
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA--VTSGVK-----DIREVIEEARERRaygrRTILFVDEI 114
ycf46 CHL00195
Ycf46; Provisional
227-416 6.33e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 75.06  E-value: 6.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVFIDEIDAIASKRENlqre 306
Cdd:CHL00195  261 GLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSES---- 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 307 merrivtqlmtcmdeyhqqigsgSGDVGSES----------AEKK-PgyVIVIGATNRPDAVDQALRRPGRFDREISLGV 375
Cdd:CHL00195  337 -----------------------KGDSGTTNrvlatfitwlSEKKsP--VFVVATANNIDLLPLEILRKGRFDEIFFLDL 391
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1002279835 376 PDEYARKKILMMLTRNLRLEG--QLDLLKIARATSSFVGADLK 416
Cdd:CHL00195  392 PSLEEREKIFKIHLQKFRPKSwkKYDIKKLSKLSNKFSGAEIE 434
PRK04195 PRK04195
replication factor C large subunit; Provisional
189-296 9.48e-12

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 68.02  E-value: 9.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 189 TFSDLGGMESVIEQLMmevvvplchPEVPRWLGVKPVAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAP-----EVVS 263
Cdd:PRK04195   12 TLSDVVGNEKAKEQLR---------EWIESWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIE 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002279835 264 GVSGASEENiRSLFKKAYRtapsIVFIDEIDAI 296
Cdd:PRK04195   83 RVAGEAATS-GSLFGARRK----LILLDEVDGI 110
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
515-660 5.15e-11

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: 61.60  E-value: 5.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 515 IKQPEEYKTFGLNMQAGFLLFGPPGCGKTLIAKAVAHEAGANFIhikgpeLLNKYVGESESEVRKIFIRaqtNTP--CIL 592
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSEVVLTDDRLNHLLN---TAPkqSII 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 593 FFDEVDA--LTTKRGKEGGWVVERL----LNQLLIELDGAGERKGVFVIGATNRIDVIDDAALRPGRFGKKHYV 660
Cdd:cd19510    80 LLEDIDAafESREHNKKNPSAYGGLsrvtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
228-367 4.76e-10

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: 61.55  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGAseeNIRSLFKKAyrtapSIVFIDEIDAIASKRENLqrem 307
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPGDLA---AILTNLEEG-----DVLFIDEIHRLSPAVEEL---- 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 308 errivtqLMTCMDEYHQQIGSGSGDvGSESAEKKPGYVIVIGATNRPDAVDQALRrpGRF 367
Cdd:TIGR00635 101 -------LYPAMEDFRLDIVIGKGP-SARSVRLDLPPFTLVGATTRAGMLTSPLR--DRF 150
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
533-647 2.69e-09

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 57.46  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHE---------AGANFIHIKGPELLNKYVGESESEVRKIF--IRAQTNTPCILFF---DEVD 598
Cdd:cd19508    56 LLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFqkIQELIDDKDALVFvliDEVE 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 599 ALTTKR-----GKEGGWVVeRLLNQLLIELDGAGERKGVFVIGATNRIDVIDDA 647
Cdd:cd19508   136 SLAAARsasssGTEPSDAI-RVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
532-597 5.79e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.94  E-value: 5.79e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 532 FLLFGPPGCGKTLIAKAVAHEAGANFIHIKGpellnkyVGESESEVRKIFIRAQTNT----PCILFFDEV 597
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSA-------VTSGVKDLREVIEEARQRRsagrRTILFIDEI 101
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
189-259 5.88e-09

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: 55.58  E-value: 5.88e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 189 TFSDLGGMESVIEQLmmEVVV--------PLCHpevprwlgvkpvagLLLHGPPGCGKTTLAHAIANETGVPFYKISAP 259
Cdd:pfam05496   5 TLDEYIGQEKVKENL--KIFIeaakqrgeALDH--------------VLLYGPPGLGKTTLANIIANEMGVNIRITSGP 67
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
228-293 6.66e-09

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 58.22  E-value: 6.66e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPE---------VVSGVsgasEENirslfkkayrtapSIVFIDEI 293
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAlekpgdlaaILTNL----EEG-------------DVLFIDEI 111
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
228-259 2.01e-08

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 56.63  E-value: 2.01e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAP 259
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
PRK13341 PRK13341
AAA family ATPase;
225-293 3.25e-08

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 56.99  E-value: 3.25e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279835 225 VAGLLLHGPPGCGKTTLAHAIANETGVPFYKISApeVVSGVSgaseeNIRSLFKKAY--------RTapsIVFIDEI 293
Cdd:PRK13341   52 VGSLILYGPPGVGKTTLARIIANHTRAHFSSLNA--VLAGVK-----DLRAEVDRAKerlerhgkRT---ILFIDEV 118
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
533-676 3.85e-08

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 56.78  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHE-AG------ANFIHIKGPELLNKYVGESESEVRKIFIRAQTNtpcILFFDEVDALTTKRG 605
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGlgvlrkPLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY 392
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 606 KEGGWVVERLLNQLLIELDGAGERKGVFVIGATNRIDVIDDA--ALRpGRFGKKHYVPLPGADERVSILRALA 676
Cdd:TIGR03922 393 GQKDPFGLEAIDTLLARMENDRDRLVVIGAGYRKDLDKFLEVneGLR-SRFTRVIEFPSYSPDELVEIARRMA 464
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
228-361 3.91e-08

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 54.37  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGV---------PFYKISAPEVVSGVSGASEENIRSLFKKAY-----RTAPSIVFIDEI 293
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIQeliddKDALVFVLIDEV 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002279835 294 DAIASKRENLQREMER----RIVTQLMTCMDeyhqQIgsgsgdvgsesaeKKPGYVIVIGATNRPDAVDQAL 361
Cdd:cd19508   135 ESLAAARSASSSGTEPsdaiRVVNAVLTQID----RI-------------KRYHNNVILLTSNLLEKIDVAF 189
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
532-600 4.01e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 56.22  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 532 FLLFGPPGCGKTLIAKAVAHEAGANFIHIKGpellnkyVGESESEVRKIFIRAQTN----TPCILFFDEV--------DA 599
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERraygRRTILFVDEIhrfnkaqqDA 124

                  .
gi 1002279835 600 L 600
Cdd:COG2256   125 L 125
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
533-647 4.17e-08

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: 52.91  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPEL--LNKyvgESESEVRKIFIRAQT-NTPCILFFDEVDALTTKRGKEGg 609
Cdd:cd19512    26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEK- 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1002279835 610 wVVERL---LNQLLIELdGAGERKGVFVIgATNRIDVIDDA 647
Cdd:cd19512   102 -ISEDLraaLNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWA 139
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
227-367 2.68e-07

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: 50.37  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 227 GLLLHGPPGCGKTTL----AHAIANETG--VPFYKISAPEVVSG---VSGASEENIRSLFKKAYRTApSIVFIDEIDAIA 297
Cdd:pfam07728   1 GVLLVGPPGTGKTELaerlAAALSNRPVfyVQLTRDTTEEDLFGrrnIDPGGASWVDGPLVRAAREG-EIAVLDEINRAN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835 298 SKrenlqremerrIVTQLMTCMDEYHQQIGSGSGDVGsesaeKKPGYVIVIGATNRPDA----VDQALRRpgRF 367
Cdd:pfam07728  80 PD-----------VLNSLLSLLDERRLLLPDGGELVK-----AAPDGFRLIATMNPLDRglneLSPALRS--RF 135
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
228-306 3.97e-07

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 52.50  E-value: 3.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYK-----ISAPEVVSGVSGASEENIRSLFKKAYRTApSIVFIDEIDAIASKrEN 302
Cdd:COG0593    37 LFLYGGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDFINAIRNNTIEEFKEKYRSV-DVLLIDDIQFLAGK-EA 114

                  ....
gi 1002279835 303 LQRE 306
Cdd:COG0593   115 TQEE 118
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
228-307 5.66e-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: 50.46  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPEV--VSGVSGASEENIRSLFKkayrtapSIVFIDEIDAIASK------ 299
Cdd:cd19498    49 ILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVE-------GIVFIDEIDKIAKRggssgp 121
                          90
                  ....*....|.
gi 1002279835 300 ---RENLQREM 307
Cdd:cd19498   122 dvsREGVQRDL 132
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
228-298 6.74e-07

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 50.25  E-value: 6.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISapevVSGVSGASEenIR---------------SLFKKAYRTAPSIVfIDE 292
Cdd:cd19500    40 LCLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAE--IRghrrtyvgampgriiQALKKAGTNNPVFL-LDE 112

                  ....*.
gi 1002279835 293 IDAIAS 298
Cdd:cd19500   113 IDKIGS 118
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
398-432 8.02e-07

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: 46.38  E-value: 8.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002279835 398 LDLLKIARATSSFVGADLKALVDKAGNLAMKRIID 432
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLE 36
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
684-724 9.76e-07

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: 45.99  E-value: 9.76e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1002279835 684 SVDLGALARReeCKNLTGADLASMVNEAAMAALEERLEFLE 724
Cdd:pfam17862   1 DVDLEELAER--TEGFSGADLEALCREAALAALRRGLEAVT 39
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
227-296 1.45e-06

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 50.74  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIANE-----------------------TGVPFYKISaPEVVSGVSGAseENIRSLFKKAYRT 283
Cdd:COG0470    20 ALLLHGPPGIGKTTLALALARDllcenpeggkacgqchsrlmaagNHPDLLELN-PEEKSDQIGI--DQIRELGEFLSLT 96
                          90
                  ....*....|....*..
gi 1002279835 284 APS----IVFIDEIDAI 296
Cdd:COG0470    97 PLEggrkVVIIDEADAM 113
rfc PRK00440
replication factor C small subunit; Reviewed
228-309 1.65e-06

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 50.64  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVvsgvsGASEEN----IRSLFKKAYRTAPS------IVFIDEIDAIA 297
Cdd:PRK00440   41 LLFAGPPGTGKTTAALALARELYGEDWRENFLEL-----NASDERgidvIRNKIKEFARTAPVggapfkIIFLDEADNLT 115
                          90
                  ....*....|...
gi 1002279835 298 SKREN-LQREMER 309
Cdd:PRK00440  116 SDAQQaLRRTMEM 128
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
223-298 2.77e-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: 47.96  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 223 KPVAGLLLHGPPGCGKTTLAHAIANETGV---PFYKISAPE-----VVSGVSGASEENIR-----SLFKKAYRTAPSIVF 289
Cdd:pfam07724   1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEymeehSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVL 80

                  ....*....
gi 1002279835 290 IDEIDAIAS 298
Cdd:pfam07724  81 IDEIEKAHP 89
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
225-292 6.69e-06

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: 46.75  E-value: 6.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 225 VAGLLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVSGVSGAS--EENIRSLFKKAYRTAPSIVFIDE 292
Cdd:cd19506    26 VKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
533-692 1.08e-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: 47.85  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKG-PELL-------NKYVGESESEV---RKIFiraqTNtpcILFFDEVDALT 601
Cdd:COG0714    35 LLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDQQTGEFEfrpGPLF----AN---VLLADEINRAP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 602 tkrgkeggwvvERLLNQLLIELDgagER------------KGVFVIGATNRIDVID-----DAALRpgRFGKKHYVPLPG 664
Cdd:COG0714   108 -----------PKTQSALLEAME---ERqvtipggtyklpEPFLVIATQNPIEQEGtyplpEAQLD--RFLLKLYIGYPD 171
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002279835 665 ADERVSILRALARN-----KPISSSVDLGALAR 692
Cdd:COG0714   172 AEEEREILRRHTGRhlaevEPVLSPEELLALQE 204
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
228-313 1.16e-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: 47.85  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKI-----SAPEVVSGVSGASEENIRSLFKKayrtAP---SIVFIDEIDAIASK 299
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdLLPSDILGTYIYDQQTGEFEFRP----GPlfaNVLLADEINRAPPK 109
                          90
                  ....*....|....*
gi 1002279835 300 REN-LQREMERRIVT 313
Cdd:COG0714   110 TQSaLLEAMEERQVT 124
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
227-274 1.34e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 48.07  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIANETG--VPFYKISAPEVVSGVSGASE---ENIR 274
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTEaltQAFR 104
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
227-263 4.02e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 46.89  E-value: 4.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIANETG--VPFYKISAPEVVS 263
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGedTPFVAISGSEIYS 104
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
531-654 5.81e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 43.44  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 531 GFLLFGPPGCGKTLIAKAVAHE-AGANFIHIkgpeLLNKYVGESE------------SEVRKIFIRAQTNtPCILFFDEV 597
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYV----QLTRDTTEEDlfgrrnidpggaSWVDGPLVRAARE-GEIAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279835 598 DALTTKrgkeggwVVERLLNQL----LIELDGAGERK----GVFVIGATNRIDVID---DAALRpGRF 654
Cdd:pfam07728  76 NRANPD-------VLNSLLSLLderrLLLPDGGELVKaapdGFRLIATMNPLDRGLnelSPALR-SRF 135
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
228-316 7.82e-05

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: 42.88  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIAN---ETGVPFYKISAPEVVsgvsgaseenIRSLFKKAYRTAPSIVFIDEIDAIASKRENLQ 304
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEqalLSDEPVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70
                          90
                  ....*....|..
gi 1002279835 305 REMERRIVTQLM 316
Cdd:cd01120    71 SSELLEDLAKLL 82
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
228-368 1.11e-04

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: 43.28  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVVS-GVSGASEenIRSLFKKAYRTAPS-IVFIDEIDAIASKRENlqr 305
Cdd:cd19512    25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPmGREGVTA--IHKVFDWANTSRRGlLLFVDEADAFLRKRST--- 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279835 306 emeRRIVTQLMTCMDEYHQQIGsgsgdvgsesaEKKPGYVIVIgATNRPDAVDQALRrpGRFD 368
Cdd:cd19512   100 ---EKISEDLRAALNAFLYRTG-----------EQSNKFMLVL-ASNQPEQFDWAIN--DRID 145
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
232-310 1.49e-04

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


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 42.47  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 232 GPPGCGKTTLAHAIANETGVPFY---KISAPEVVSGVSgaseenirslfkkayrtapSIVFIDEIDAIASKRenlQREME 308
Cdd:cd02020     6 GPAGSGKSTVAKLLAKKLGLPYLdtgGIRTEEVGKLAS-------------------EVAAIPEVRKALDER---QRELA 63

                  ..
gi 1002279835 309 RR 310
Cdd:cd02020    64 KK 65
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
224-477 2.37e-04

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: 44.45  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 224 PVAG----LLLHGPPGCGKTTLAHAIANE---TGVpfykISAPEVVSgVS---------GASEENIRSLFKKAYrtaPSI 287
Cdd:TIGR03922 307 PVAQtsnhMLFAGPPGTGKTTIARVVAKIycgLGV----LRKPLVRE-VSradligqyiGESEAKTNEIIDSAL---GGV 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 288 VFIDEIDAIASKRENLQREMERRIVTQLMTCMDEYHQQIgsgsgdvgsesaekkpgyvIVIGATNRPD-----AVDQALR 362
Cdd:TIGR03922 379 LFLDEAYTLVETGYGQKDPFGLEAIDTLLARMENDRDRL-------------------VVIGAGYRKDldkflEVNEGLR 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 363 RpgRFDREISLG--VPDEYARKKILMMLTRNLRLEGQ-----LDLL-KIARATSSFVGADLKALVDKAGNLAMKR-IIDR 433
Cdd:TIGR03922 440 S--RFTRVIEFPsySPDELVEIARRMATERDSVLDDAaadalLEAAtTLAQDTTPDANGDLRRGLDIAGNGRFVRnVVER 517
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002279835 434 RRaqfcQEHDENSKHDWWRQPWDANEIegLSITMDDFEEATKMV 477
Cdd:TIGR03922 518 AE----EERDFRLDHSDRLDAVTVDDL--MEITADDVARAVASL 555
PRK08116 PRK08116
hypothetical protein; Validated
227-282 2.84e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 43.47  E-value: 2.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIAN---ETGVPFYKISAPEVVSgvsgaseeNIRSLFKKAYR 282
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANeliEKGVPVIFVNFPQLLN--------RIKSTYKSSGK 166
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
533-565 5.23e-04

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: 41.33  E-value: 5.23e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPEL 565
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
PRK08116 PRK08116
hypothetical protein; Validated
531-617 5.46e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.70  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 531 GFLLFGPPGCGKTLIAKAVAHEAGANFIHIKG---PELLNK---YVGESESEVRKIFIRAQTNTPCILffdeVDALTTKR 604
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANELIEKGVPVIFvnfPQLLNRiksTYKSSGKEDENEIIRSLVNADLLI----LDDLGAER 191
                          90
                  ....*....|...
gi 1002279835 605 GKEggWVVERLLN 617
Cdd:PRK08116  192 DTE--WAREKVYN 202
PLN03025 PLN03025
replication factor C subunit; Provisional
228-308 5.49e-04

replication factor C subunit; Provisional


Pssm-ID: 178596 [Multi-domain]  Cd Length: 319  Bit Score: 42.79  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKISAPEVvsgvsGASEE-------NIRSLFKKAYRTAPS----IVFIDEIDAI 296
Cdd:PLN03025   37 LILSGPPGTGKTTSILALAHELLGPNYKEAVLEL-----NASDDrgidvvrNKIKMFAQKKVTLPPgrhkIVILDEADSM 111
                          90
                  ....*....|...
gi 1002279835 297 AS-KRENLQREME 308
Cdd:PLN03025  112 TSgAQQALRRTME 124
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
533-611 7.35e-04

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 41.21  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPELLN-KYVG-ESESEVRKIfiraqtnTPCILFFDEVDALTTKRGKEGGW 610
Cdd:cd19498    50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDL-------VEGIVFIDEIDKIAKRGGSSGPD 122

                  .
gi 1002279835 611 V 611
Cdd:cd19498   123 V 123
PRK04182 PRK04182
cytidylate kinase; Provisional
232-303 9.19e-04

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 40.94  E-value: 9.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 232 GPPGCGKTTLAHAIANETGVPFykISAPEVVSGVsgASEENIrSL--FKKAYRTAPSivfID-EIDA----IASKRENL 303
Cdd:PRK04182    7 GPPGSGKTTVARLLAEKLGLKH--VSAGEIFREL--AKERGM-SLeeFNKYAEEDPE---IDkEIDRrqleIAEKEDNV 77
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
533-673 9.94e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.14  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGAN---------FIHI--KGP--------ELLNK--------YVGESESEVRKIFIRA- 584
Cdd:COG1474    55 LIYGPTGTGKTAVAKYVLEELEEEaeergvdvrVVYVncRQAstryrvlsRILEElgsgedipSTGLSTDELFDRLYEAl 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 585 -QTNTPCILFFDEVDALTTKRGKEggwvverLLNQLLiELDGAGERKGVFVIGATNRIDVID--DAALRpGRFGKKHyVP 661
Cdd:COG1474   135 dERDGVLVVVLDEIDYLVDDEGDD-------LLYQLL-RANEELEGARVGVIGISNDLEFLEnlDPRVK-SSLGEEE-IV 204
                         170
                  ....*....|....
gi 1002279835 662 LP--GADERVSILR 673
Cdd:COG1474   205 FPpyDADELRDILE 218
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
533-565 1.18e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPEL 565
Cdd:PRK00080   55 LLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
532-598 1.36e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.24  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 532 FLLFGPPGCGKTLIAKAVA---HEAGANFIHIKGPELLNK------------YVGESES-----EVRKifiraqtNTPCI 591
Cdd:cd19499    44 FLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGgqlteAVRR-------KPYSV 116

                  ....*..
gi 1002279835 592 LFFDEVD 598
Cdd:cd19499   117 VLLDEIE 123
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
532-598 1.40e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 40.26  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 532 FLLFGPPGCGKTLIAKAVAHEAG---ANFIHIKGPELLNK------------YVGESESEVRKIFIRaqTNTPCILFFDE 596
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMEEhsvsrligappgYVGYEEGGQLTEAVR--RKPYSIVLIDE 83

                  ..
gi 1002279835 597 VD 598
Cdd:pfam07724  84 IE 85
AAA_28 pfam13521
AAA domain;
230-310 1.68e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.94  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 230 LHGPPGCGKTTLAHAIANETGVPFYkisapevvsgvsgasEENIRSLFKKAYRTA-PSIVFIDEIDAIASKRENLQREME 308
Cdd:pfam13521   4 ITGGPSTGKTTLAEALAARFGYPVV---------------PEAAREILEELGADGgDALPWVEDLLAFARGVLEAQLEDE 68

                  ..
gi 1002279835 309 RR 310
Cdd:pfam13521  69 AA 70
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
532-650 1.68e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 39.92  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 532 FLLFGPPGCGKTLIAKAVA--HEAGANFIHIKGPELLNK----------YVGE-SESEVRKIFI-RAQTNTPCILFFDEV 597
Cdd:cd00267    28 VALVGPNGSGKSTLLRAIAglLKPTSGEILIDGKDIAKLpleelrrrigYVPQlSGGQRQRVALaRALLLNPDLLLLDEP 107
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279835 598 ----DALTTKRgkeggwvVERLLNQLLieldgageRKGVFVIGATNRIDVIDDAALR 650
Cdd:cd00267   108 tsglDPASRER-------LLELLRELA--------EEGRTVIIVTHDPELAELAADR 149
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
12-69 1.72e-03

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


Pssm-ID: 465247  Cd Length: 70  Bit Score: 37.61  E-value: 1.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002279835  12 RSHSPYFESQ-LRRLITDGGLSSSS-----AEDVAIALRSRFPEFRRHKLDPFTSAVRRALNSI 69
Cdd:pfam16725   1 KKRSGYFSDPrLVPRVEQYLEDNSDstyvdVDAMADELQRQYREYGRRKRNAFRIQVEKAYEII 64
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
533-565 1.81e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.13  E-value: 1.81e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGPEL 565
Cdd:TIGR00635  34 LLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
228-257 1.87e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 41.93  E-value: 1.87e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETGVPFYKIS 257
Cdd:COG0466   355 LCLVGPPGVGKTSLGKSIARALGRKFVRIS 384
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
227-327 1.99e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.53  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 227 GLLLHGPPGCGKTTLAHAIANE---TGVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTAPSIVfIDEIDAIASKREN- 302
Cdd:COG1484   101 NLILLGPPGTGKTHLAIALGHEacrAGYRVRFTTAPDLVNELKEARADGRLERLLKRLAKVDLLI-LDELGYLPLDAEGa 179
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002279835 303 ------LQREMERR---IVTQLmtCMDEYHQQIG 327
Cdd:COG1484   180 ellfelISDRYERRstiITSNL--PFSEWGEVFG 211
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
527-601 2.03e-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: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 527 NMQAGFLLF-GPPGCGKTLIAKAVAHEAGANFIHIKgpellnkyVG--ESESEVR------------KI---FIRAQTNT 588
Cdd:cd19500    34 SMKGPILCLvGPPGVGKTSLGKSIARALGRKFVRIS--------LGgvRDEAEIRghrrtyvgampgRIiqaLKKAGTNN 105
                          90
                  ....*....|...
gi 1002279835 589 PCILfFDEVDALT 601
Cdd:cd19500   106 PVFL-LDEIDKIG 117
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
228-348 2.05e-03

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


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 38.72  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANEtgvpFYKISAPEVVSG----VSGASEENIRSLFKKAYRTAPSIVFIDEIdaiaSKRENL 303
Cdd:pfam13173   5 LVITGPRQVGKTTLLLQLIKE----LLPPENILYINLddprLLKLADFELLELFLELLYPGKTYLFLDEI----QRVPDW 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279835 304 QREMeRRIVtqlmtcmDEYHQ-QI---GSGSGDVGSESAEKKPGYVIVI 348
Cdd:pfam13173  77 ELAL-KRLY-------DDGPNgRViltGSSALLLSKEIAESLAGRVVVI 117
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
228-248 2.31e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 2.31e-03
                          10        20
                  ....*....|....*....|.
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANE 248
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
533-563 2.41e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 40.83  E-value: 2.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEAGANFIHIKGP 563
Cdd:COG2255    58 LLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
AAA_22 pfam13401
AAA domain;
228-315 2.75e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIAN---ETGVPFYKISAPEVVS------------GVSGASEENIRSLFK------KAYRTAPS 286
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPSGTSpkdllrallralGLPLSGRLSKEELLAalqqllLALAVAVV 87
                          90       100
                  ....*....|....*....|....*....
gi 1002279835 287 IVfIDEIDaiaskreNLQREMERRIVTQL 315
Cdd:pfam13401  88 LI-IDEAQ-------HLSLEALEELRDLL 108
Bac_DnaA pfam00308
Bacterial dnaA protein;
228-306 3.09e-03

Bacterial dnaA protein;


Pssm-ID: 278724 [Multi-domain]  Cd Length: 219  Bit Score: 40.00  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANET-----GVPFYKISAPEVVSGVSGASEENIRSLFKKAYRTApSIVFIDEIDAIASKrEN 302
Cdd:pfam00308  37 LFIYGGVGLGKTHLLHAIGNYAlqnapNLRVVYLTAEEFLNDFVDAIRDNKTNQFKEKYRNV-DVLLIDDIQFLAGK-EG 114

                  ....
gi 1002279835 303 LQRE 306
Cdd:pfam00308 115 TQEE 118
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
228-250 4.14e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.74  E-value: 4.14e-03
                          10        20
                  ....*....|....*....|...
gi 1002279835 228 LLLHGPPGCGKTTLAHAIANETG 250
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLG 24
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
232-254 4.21e-03

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 38.57  E-value: 4.21e-03
                          10        20
                  ....*....|....*....|...
gi 1002279835 232 GPPGCGKTTLAHAIANETGVPFY 254
Cdd:COG0703     5 GMMGAGKSTVGRLLAKRLGLPFV 27
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
214-253 5.21e-03

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.


Pssm-ID: 463892 [Multi-domain]  Cd Length: 193  Bit Score: 38.90  E-value: 5.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002279835 214 PEVPRWL--GVKPVAGL-LLHGPPGCGKTTL----AHAIAneTGVPF 253
Cdd:pfam13481  19 PPPRRWLikGLLPAGGLgLLAGAPGTGKTTLaldlAAAVA--TGKPW 63
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
531-574 6.40e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.57  E-value: 6.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1002279835 531 GFLLFGPPGCGKTLIAKAVAHEAGAN--FIHIKGPELLNKYVGESE 574
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTE 111
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
330-596 6.80e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 39.75  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 330 SGDVGSESAEKKPGYVIVIGATNRPDAVDQALRRPGRFDREISLGVPDEYARKKILMMLTRNLRLEGQLDLLKIARatss 409
Cdd:COG1401    22 SEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEA---- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 410 FVGADLKALVDKAGNLAMKRIIDRRRAQFCQEHDENSKHDWWRQPWDA-NEIEGLSITMDDFEEATKMVQPSLRREGFSS 488
Cdd:COG1401    98 AVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEeRAALETEVLEALEAELEELLAAPEDLSADAL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 489 IPDVTWDDVGGLDSLRKEFDRYI-IRCIKQPEEYKTFGLNMQAG--FLLFGPPGCGKTLIAKAVAHEAGA----NFIHI- 560
Cdd:COG1401   178 AAELSAAEELYSEDLESEDDYLKdLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYLARRLAEALGGedngRIEFVq 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002279835 561 -----KGPELLNKYV-GESESEVR---KIFIRA------QTNTPCILFFDE 596
Cdd:COG1401   258 fhpswSYEDFLLGYRpSLDEGKYEptpGIFLRFclkaekNPDKPYVLIIDE 308
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
533-647 7.54e-03

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: 37.87  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 533 LLFGPPGCGKTLIAKAVAH---EAGANFIHIKGPELLnKYVGESESEVRKIFIRA----QTNTPCILFFDEVDALTTKRG 605
Cdd:pfam13191  28 LLTGEAGTGKTTLLRELLRaleRDGGYFLRGKCDENL-PYSPLLEALTREGLLRQlldeLESSLLEAWRAALLEALAPVP 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002279835 606 KEGGWVVERLLNQLLIELDGAGERKGVFVIgatnridVIDDA 647
Cdd:pfam13191 107 ELPGDLAERLLDLLLRLLDLLARGERPLVL-------VLDDL 141
clpC CHL00095
Clp protease ATP binding subunit
534-675 7.57e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 39.65  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279835 534 LFGPPGCGKTLIAKAVAH----EAGANFIHIKGPELLN--------KYVGESESEVRKIFIRAQTNTPCILFFDEVDALT 601
Cdd:CHL00095  205 LIGEPGVGKTAIAEGLAQrivnRDVPDILEDKLVITLDiglllagtKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLI 284
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279835 602 TKRGKEGGWVVERLLNQLLieldgagERKGVFVIGATNrIDVID-----DAALRPgRFgKKHYVPLPGADERVSILRAL 675
Cdd:CHL00095  285 GAGAAEGAIDAANILKPAL-------ARGELQCIGATT-LDEYRkhiekDPALER-RF-QPVYVGEPSVEETIEILFGL 353
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
232-254 7.66e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 37.80  E-value: 7.66e-03
                          10        20
                  ....*....|....*....|...
gi 1002279835 232 GPPGCGKTTLAHAIANETGVPFY 254
Cdd:COG3265     8 GVSGSGKSTVGQALAERLGWPFI 30
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
533-553 9.34e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.61  E-value: 9.34e-03
                          10        20
                  ....*....|....*....|.
gi 1002279835 533 LLFGPPGCGKTLIAKAVAHEA 553
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAA 114
 
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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