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Conserved domains on  [gi|1002279290|ref|XP_015643962|]
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spastin [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 216-379 2.25e-99

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: 295.61  E-value: 2.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKL 295
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 296 VRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDDLVIVIGATNKPQELDDAVLRRLVK 375
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1002279290 376 RIYV 379
Cdd:cd19524   161 RVYV 164
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 55-463 3.70e-66

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


:

Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 218.24  E-value: 3.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290  55 EEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAkwQTQVEERLRVLGQRSGAAAPV 134
Cdd:COG0464     2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLL--LLLSGALAALLLLALLLLALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 135 PKKVVTNNPVNRNDRAASTSFHRPTSQPSPTFNRGGQASSHQKSSSGGAKPVQRAGANYDDKLVemiNTTIVDRSPAVKW 214
Cdd:COG0464    80 ALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG---LEEELLELREAIL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 215 EDVAGLDKAKQALMEMVILPTKRRDLFT--GLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEA 292
Cdd:COG0464   157 DDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 293 EKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNpddlVIVIGATNKPQELDDAVLRR 372
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLLDPALLRR 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 373 LVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSGSDLRALCEEAAMMPIRELGPqniltikanqlrP 452
Cdd:COG0464   312 FDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE------------P 378

                         410
                  ....*....|.
gi 1002279290 453 LKYEDFKKAMT 463
Cdd:COG0464   379 VTTEDLLEALE 389
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 445-485 6.54e-04

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


The actual alignment was detected with superfamily member pfam09336:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 37.86  E-value: 6.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002279290 445 IKANQL--RPLKYEDFKKAMTVIRPSLQKSKWDELEKWNEEFG 485
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 216-379 2.25e-99

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: 295.61  E-value: 2.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKL 295
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 296 VRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDDLVIVIGATNKPQELDDAVLRRLVK 375
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1002279290 376 RIYV 379
Cdd:cd19524   161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 195-473 1.05e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 258.78  E-value: 1.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 195 DKLVEMINTTIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFT--GLRRPaRGLLLFGPPGNGKTMLAKAVASES 272
Cdd:COG1222    58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 273 EATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARL-ANENDASRRLKSEFLIQFDGVTSNPDd 351
Cdd:COG1222   137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLAELDGFESRGD- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 352 lVIVIGATNKPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKgqSFKLSSH-DLERLAADTEGYSGSDLRALCEE 428
Cdd:COG1222   216 -VLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLR--DMPLADDvDLDKLAKLTEGFSGADLKAIVTE 292

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002279290 429 AAMMPIRElgpqniltiKANQLRPlkyEDFKKAMTVIRPSLQKSK 473
Cdd:COG1222   293 AGMFAIRE---------GRDTVTM---EDLEKAIEKVKKKTETAT 325
cell_div_CdvC NF041006
cell division protein CdvC;
185-484 6.50e-77

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 245.41  E-value: 6.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 185 PVQRAGANYDDKLVEMInttIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTgLRRPaRGLLLFGPPGNGKTML 264
Cdd:NF041006   76 PAEPAGPDVEKESDEEL---VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP-LGWP-RGILLYGPPGCGKTML 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 265 AKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMVA-----VDRQPSVIFMDEIDSVMsARLANENDASRRLKSEFL 339
Cdd:NF041006  151 AAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALL-GVYSSEVGGEVRVRNQFL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 340 IQFDGVTSNPDDL-VIVIGATNKPQELDDAVLRRLVKRIYVPLPDPNVRRLLLKTQLKGqsFKLSSH-DLERLAADTEGY 417
Cdd:NF041006  230 KEMDGLQDKSENYhVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSK--IKLENDvDLDELAEMTEGY 307

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279290 418 SGSDLRALCEEAAMMPIRELGPQNIltikaNQLRPLKYEDFKKAMTVIRPSLQKSKWDELEKWNEEF 484
Cdd:NF041006  308 TASDIRDIVQAAHMRVVKEMFEKGL-----GEPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 55-463 3.70e-66

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 218.24  E-value: 3.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290  55 EEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAkwQTQVEERLRVLGQRSGAAAPV 134
Cdd:COG0464     2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLL--LLLSGALAALLLLALLLLALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 135 PKKVVTNNPVNRNDRAASTSFHRPTSQPSPTFNRGGQASSHQKSSSGGAKPVQRAGANYDDKLVemiNTTIVDRSPAVKW 214
Cdd:COG0464    80 ALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG---LEEELLELREAIL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 215 EDVAGLDKAKQALMEMVILPTKRRDLFT--GLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEA 292
Cdd:COG0464   157 DDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 293 EKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNpddlVIVIGATNKPQELDDAVLRR 372
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLLDPALLRR 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 373 LVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSGSDLRALCEEAAMMPIRELGPqniltikanqlrP 452
Cdd:COG0464   312 FDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE------------P 378

                         410
                  ....*....|.
gi 1002279290 453 LKYEDFKKAMT 463
Cdd:COG0464   379 VTTEDLLEALE 389
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 210-485 4.04e-62

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: 215.54  E-value: 4.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 210 PAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKW 288
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGiRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 289 VGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDA-SRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDD 367
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSN--VVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 368 AVLR--RLVKRIYVPLPDPNVRRLLLKTQLKgqSFKLSSH-DLERLAADTEGYSGSDLRALCEEAAMMPIREL----GPQ 440
Cdd:TIGR01243 606 ALLRpgRFDRLILVPPPDEEARKEIFKIHTR--SMPLAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRESigspAKE 683

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002279290 441 NILTIKANQLRPLKY--EDFKKAMTVIRPSLQKSKWDELEKWNEEFG 485
Cdd:TIGR01243 684 KLEVGEEEFLKDLKVemRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 206-461 3.64e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 205.07  E-value: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 206 VDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFT--GLRrPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASS 283
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIE-PPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 284 LTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASR---RLKSEFLIQFDGVtsNPDDLVIVIGATN 360
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGF--DPRGNVKIIAATN 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 361 KPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSGSDLRALCEEAAMMPIRELG 438
Cdd:PRK03992  279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLA-DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDR 357

                         250       260
                  ....*....|....*....|...
gi 1002279290 439 PQniltikanqlrpLKYEDFKKA 461
Cdd:PRK03992  358 TE------------VTMEDFLKA 368
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 251-381 2.35e-50

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 167.77  E-value: 2.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 251 LLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDA 330
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002279290 331 SRRLKSEFLIQFDGVTSNPDDlVIVIGATNKPQELDDAVLRRLVKRIYVPL 381
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSK-VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 46-124 2.46e-30

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 112.76  E-value: 2.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279290  46 LRGYFELAKEEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAKWQTQVEERLRVL 124
Cdd:cd02679     1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVPSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 247-383 1.51e-13

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 68.17  E-value: 1.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290  247 PARGLLLFGPPGNGKTMLAKAVASESEATFFNV-----------------SASSLTSKWVGEAEKLVRTLFMVAVDRQPS 309
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002279290  310 VIFMDEIDSVMSARLANENDASRRLKSEFLIQfdgvtsnPDDLVIVIGATNKPQELDDAVLRRLV-KRIYVPLPD 383
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALLRRRFdRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
47-121 2.50e-12

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 62.33  E-value: 2.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002279290   47 RGYFELAKEEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAKWQTQVEERL 121
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLERL 76
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 406-436 3.87e-10

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 54.85  E-value: 3.87e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1002279290 406 DLERLAADTEGYSGSDLRALCEEAAMMPIRE 436
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRR 33
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 445-485 6.54e-04

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 37.86  E-value: 6.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002279290 445 IKANQL--RPLKYEDFKKAMTVIRPSLQKSKWDELEKWNEEFG 485
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 216-379 2.25e-99

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: 295.61  E-value: 2.25e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKL 295
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 296 VRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDDLVIVIGATNKPQELDDAVLRRLVK 375
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1002279290 376 RIYV 379
Cdd:cd19524   161 RVYV 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 194-379 2.87e-87

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: 265.70  E-value: 2.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 194 DDKLVEMINTTIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESE 273
Cdd:cd19525     1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 274 ATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDDLV 353
Cdd:cd19525    81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                         170       180
                  ....*....|....*....|....*.
gi 1002279290 354 IVIGATNKPQELDDAVLRRLVKRIYV 379
Cdd:cd19525   161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 217-379 1.45e-86

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: 262.67  E-value: 1.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 217 VAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLV 296
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 297 RTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDDLVIVIGATNKPQELDDAVLRRLVKR 376
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                  ...
gi 1002279290 377 IYV 379
Cdd:cd19509   161 IYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 195-473 1.05e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 258.78  E-value: 1.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 195 DKLVEMINTTIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFT--GLRRPaRGLLLFGPPGNGKTMLAKAVASES 272
Cdd:COG1222    58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 273 EATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARL-ANENDASRRLKSEFLIQFDGVTSNPDd 351
Cdd:COG1222   137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLAELDGFESRGD- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 352 lVIVIGATNKPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKgqSFKLSSH-DLERLAADTEGYSGSDLRALCEE 428
Cdd:COG1222   216 -VLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLR--DMPLADDvDLDKLAKLTEGFSGADLKAIVTE 292

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002279290 429 AAMMPIRElgpqniltiKANQLRPlkyEDFKKAMTVIRPSLQKSK 473
Cdd:COG1222   293 AGMFAIRE---------GRDTVTM---EDLEKAIEKVKKKTETAT 325
cell_div_CdvC NF041006
cell division protein CdvC;
185-484 6.50e-77

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 245.41  E-value: 6.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 185 PVQRAGANYDDKLVEMInttIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTgLRRPaRGLLLFGPPGNGKTML 264
Cdd:NF041006   76 PAEPAGPDVEKESDEEL---VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP-LGWP-RGILLYGPPGCGKTML 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 265 AKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMVA-----VDRQPSVIFMDEIDSVMsARLANENDASRRLKSEFL 339
Cdd:NF041006  151 AAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALL-GVYSSEVGGEVRVRNQFL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 340 IQFDGVTSNPDDL-VIVIGATNKPQELDDAVLRRLVKRIYVPLPDPNVRRLLLKTQLKGqsFKLSSH-DLERLAADTEGY 417
Cdd:NF041006  230 KEMDGLQDKSENYhVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSK--IKLENDvDLDELAEMTEGY 307

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002279290 418 SGSDLRALCEEAAMMPIRELGPQNIltikaNQLRPLKYEDFKKAMTVIRPSLQKSKWDELEKWNEEF 484
Cdd:NF041006  308 TASDIRDIVQAAHMRVVKEMFEKGL-----GEPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 210-379 4.73e-72

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 225.90  E-value: 4.73e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 210 PAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWV 289
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVtSNPDDLVIVIGATNKPQELDDAV 369
Cdd:cd19521    82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGV-GNDSQGVLVLGATNIPWQLDSAI 160

                         170
                  ....*....|
gi 1002279290 370 LRRLVKRIYV 379
Cdd:cd19521   161 RRRFEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 55-463 3.70e-66

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 218.24  E-value: 3.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290  55 EEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAkwQTQVEERLRVLGQRSGAAAPV 134
Cdd:COG0464     2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLL--LLLSGALAALLLLALLLLALL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 135 PKKVVTNNPVNRNDRAASTSFHRPTSQPSPTFNRGGQASSHQKSSSGGAKPVQRAGANYDDKLVemiNTTIVDRSPAVKW 214
Cdd:COG0464    80 ALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG---LEEELLELREAIL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 215 EDVAGLDKAKQALMEMVILPTKRRDLFT--GLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEA 292
Cdd:COG0464   157 DDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 293 EKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNpddlVIVIGATNKPQELDDAVLRR 372
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLLDPALLRR 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 373 LVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSGSDLRALCEEAAMMPIRELGPqniltikanqlrP 452
Cdd:COG0464   312 FDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE------------P 378

                         410
                  ....*....|.
gi 1002279290 453 LKYEDFKKAMT 463
Cdd:COG0464   379 VTTEDLLEALE 389
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 216-379 1.68e-63

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: 203.43  E-value: 1.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLF--TGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAE 293
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 294 KLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDDLVIVIGATNKPQELDDAVLRRL 373
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                  ....*.
gi 1002279290 374 VKRIYV 379
Cdd:cd19520   161 PKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 216-379 4.08e-63

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: 202.52  E-value: 4.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKL 295
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 296 VRTLFMVAVDRQPSVIFMDEIDSVMSAR-LANENDASRRLKSEFLIQFDGVT-----SNPDDLVIVIGATNKPQELDDAV 369
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGgasenDDPSKMVMVLAATNFPWDIDEAL 160

                         170
                  ....*....|
gi 1002279290 370 LRRLVKRIYV 379
Cdd:cd19522   161 RRRLEKRIYI 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 210-485 4.04e-62

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: 215.54  E-value: 4.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 210 PAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKW 288
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGiRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 289 VGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDA-SRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDD 367
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSN--VVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 368 AVLR--RLVKRIYVPLPDPNVRRLLLKTQLKgqSFKLSSH-DLERLAADTEGYSGSDLRALCEEAAMMPIREL----GPQ 440
Cdd:TIGR01243 606 ALLRpgRFDRLILVPPPDEEARKEIFKIHTR--SMPLAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRESigspAKE 683

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002279290 441 NILTIKANQLRPLKY--EDFKKAMTVIRPSLQKSKWDELEKWNEEFG 485
Cdd:TIGR01243 684 KLEVGEEEFLKDLKVemRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 206-461 3.64e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 205.07  E-value: 3.64e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 206 VDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFT--GLRrPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASS 283
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIE-PPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 284 LTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASR---RLKSEFLIQFDGVtsNPDDLVIVIGATN 360
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGF--DPRGNVKIIAATN 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 361 KPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSGSDLRALCEEAAMMPIRELG 438
Cdd:PRK03992  279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLA-DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDR 357

                         250       260
                  ....*....|....*....|...
gi 1002279290 439 PQniltikanqlrpLKYEDFKKA 461
Cdd:PRK03992  358 TE------------VTMEDFLKA 368
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 183-477 5.06e-53

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 190.50  E-value: 5.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 183 AKPVQRAGANYDDKLVEMINTTIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGK 261
Cdd:TIGR01243 146 AGFVYVTEATEVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGK 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 262 TMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQ 341
Cdd:TIGR01243 226 TLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTL 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 342 FDGVTSNPDdlVIVIGATNKPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSG 419
Cdd:TIGR01243 306 MDGLKGRGR--VIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLA-EDVDLDKLAEVTHGFVG 382

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279290 420 SDLRALCEEAAMMPIRELGPQNILTIKANQ-----LRPLKY--EDFKKAMTVIRPSLQKS--------KWDEL 477
Cdd:TIGR01243 383 ADLAALAKEAAMAALRRFIREGKINFEAEEipaevLKELKVtmKDFMEALKMVEPSAIREvlvevpnvRWSDI 455
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 216-379 7.55e-51

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: 170.45  E-value: 7.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKL 295
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 296 VRTLFMVAVDRQPSVIFMDEIDSVMSARLaNENDASRRLKSEFLIQFDGVTSNPDDLVIVIGATNKPQELDDAVLRRLVK 375
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQD-DEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                  ....
gi 1002279290 376 RIYV 379
Cdd:cd19523   160 RLLV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 251-381 2.35e-50

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 167.77  E-value: 2.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 251 LLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDA 330
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002279290 331 SRRLKSEFLIQFDGVTSNPDDlVIVIGATNKPQELDDAVLRRLVKRIYVPL 381
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSK-VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 195-435 1.68e-47

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 168.79  E-value: 1.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 195 DKLVEMINttiVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESE 273
Cdd:PTZ00454  128 DSSIQLLQ---MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTT 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 274 ATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASR---RLKSEFLIQFDGVTSNPD 350
Cdd:PTZ00454  205 ATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 351 dlVIVIGATNKPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLkgQSFKLSSH-DLERLAADTEGYSGSDLRALCE 427
Cdd:PTZ00454  285 --VKVIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTIT--SKMNLSEEvDLEDFVSRPEKISAADIAAICQ 360


                  ....*...
gi 1002279290 428 EAAMMPIR 435
Cdd:PTZ00454  361 EAGMQAVR 368
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 223-379 2.46e-47

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: 160.91  E-value: 2.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 223 AKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFM 301
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLGiRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 302 VAVDRQPSVIFMDEIDSVMSARLAN-ENDASRRLKSEFLIQFDGVtsNPDDLVIVIGATNKPQELDDAVLR--RLVKRIY 378
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGI--ESLKGVVVIAATNRPDMIDPALLRpgRLDKLIY 158


                  .
gi 1002279290 379 V 379
Cdd:cd19511   159 V 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 194-436 4.91e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 166.10  E-value: 4.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 194 DDKLVEMINTTIVDRSPAVKWEDVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASES 272
Cdd:PTZ00361  162 LDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGiKPPKGVILYGPPGTGKTLLAKAVANET 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 273 EATFFNVSASSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASR---RLKSEFLIQFDGVTSNP 349
Cdd:PTZ00361  242 SATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKeiqRTMLELLNQLDGFDSRG 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 350 DdlVIVIGATNKPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLktQLKGQSFKLSSH-DLERLAADTEGYSGSDLRALC 426
Cdd:PTZ00361  322 D--VKVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIF--EIHTSKMTLAEDvDLEEFIMAKDELSGADIKAIC 397

                         250
                  ....*....|
gi 1002279290 427 EEAAMMPIRE 436
Cdd:PTZ00361  398 TEAGLLALRE 407
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 216-372 8.15e-46

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: 157.07  E-value: 8.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEK 294
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGlKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279290 295 LVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAvLRR 372
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGK--VVVIAATNRPDAIDPA-LRR 155
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
214-460 4.04e-45

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 158.12  E-value: 4.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 214 WEDVAGLDKAKQALmEMVILPTKRRDLftgLRR----PARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWV 289
Cdd:COG1223     1 LDDVVGQEEAKKKL-KLIIKELRRREN---LRKfglwPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKLVRTLFMvAVDRQPSVIFMDEIDSVMSAR-LANENDASRRLKSEFLIQFDGVTSNpddlVIVIGATNKPQELDDA 368
Cdd:COG1223    77 GETARNLRKLFD-FARRAPCVIFFDEFDAIAKDRgDQNDVGEVKRVVNALLQELDGLPSG----SVVIAATNHPELLDSA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 369 VLRRLVKRIYVPLPDPNVRRLLLktQLKGQSFKLS-SHDLERLAADTEGYSGSDLRALCEEAAMMPI---RELGPQNILT 444
Cdd:COG1223   152 LWRRFDEVIEFPLPDKEERKEIL--ELNLKKFPLPfELDLKKLAKKLEGLSGADIEKVLKTALKKAIledREKVTKEDLE 229

                         250
                  ....*....|....*.
gi 1002279290 445 IKANQLRPLKYEDFKK 460
Cdd:COG1223   230 EALKQRKERKKEPKKE 245
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 214-379 3.68e-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: 152.88  E-value: 3.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 214 WEDVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEA 292
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 293 EKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASR---RLKSEFLIQFDGVtsNPDDLVIVIGATNKPQELDDAV 369
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGF--DPRGNIKVIMATNRPDILDPAL 159

                         170
                  ....*....|..
gi 1002279290 370 LR--RLVKRIYV 379
Cdd:cd19502   160 LRpgRFDRKIEF 171
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 223-379 1.97e-43

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: 150.51  E-value: 1.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 223 AKQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMV 302
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 303 AVDRQPSVIFMDEIDSVMSARLAN-ENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAVLR--RLVKRIYV 379
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSK--VLVIAATNRPDLLDPALLRpgRFDEVIEF 158
ftsH CHL00176
cell division protein; Validated
 211-436 2.92e-42

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 159.06  E-value: 2.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 211 AVKWEDVAGLDKAKQALMEMV-ILPTKRRDLFTGLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWV 289
Cdd:CHL00176  179 GITFRDIAGIEEAKEEFEEVVsFLKKPERFTAVGAKIP-KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLAN---ENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELD 366
Cdd:CHL00176  258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKG--VIVIAATNRVDILD 335

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002279290 367 DAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKGQSFKLSShDLERLAADTEGYSGSDLRALCEEAAMMPIRE 436
Cdd:CHL00176  336 AALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDV-SLELIARRTPGFSGADLANLLNEAAILTARR 406
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 223-379 8.70e-42

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: 146.49  E-value: 8.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 223 AKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFM 301
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGiRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 302 VAVDRQPSVIFMDEIDSVMSAR-LANENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAVLR--RLVKRIY 378
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLIY 158


                  .
gi 1002279290 379 V 379
Cdd:cd19529   159 I 159
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 212-379 4.41e-40

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: 142.37  E-value: 4.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 212 VKWEDVAGLDKAKQALMEMV-ILptKRRDLFTGL-RRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWV 289
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVeFL--KNPEKFTKLgAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANE---NDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELD 366
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFESNTG--VIVIAATNRPDVLD 156

                         170
                  ....*....|....*
gi 1002279290 367 DAVLR--RLVKRIYV 379
Cdd:cd19501   157 PALLRpgRFDRQVYV 171
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 224-379 5.46e-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: 141.49  E-value: 5.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 224 KQALMEMVILPTKRRDLFT--GLRrPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFM 301
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLkfGMT-PSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 302 VAVDRQPSVIFMDEIDSVMSAR---LANENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAVLR--RLVKR 376
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARggnIGDAGGAADRVINQILTEMDGMNTKKN--VFIIGATNRPDIIDPAILRpgRLDQL 158


                  ...
gi 1002279290 377 IYV 379
Cdd:cd19528   159 IYI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 216-372 1.30e-38

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 138.31  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLF--TGLRrPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAE 293
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 294 KLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDD--LVIVIGATNKPQELDDAvLR 371
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAggPVLVIGATNRPDSLDPA-LR 158


                  .
gi 1002279290 372 R 372
Cdd:cd19518   159 R 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 216-372 4.92e-38

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: 136.41  E-value: 4.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEK 294
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279290 295 LVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAvLRR 372
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAH--VIVMAATNRPNSIDPA-LRR 155
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 220-379 7.08e-37

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: 133.38  E-value: 7.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 220 LDKAKQALMEMVILPTKRRDLFT--GLRRPArGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVR 297
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKalGIDLPT-GVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 298 TLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAVLR--RLVK 375
Cdd:cd19530    80 QVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSN--VFVIAATNRPDIIDPAMLRpgRLDK 157


                  ....
gi 1002279290 376 RIYV 379
Cdd:cd19530   158 TLYV 161
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
205-430 1.40e-35

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 139.40  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 205 IVDRSPAVKWEDVAGLDKAKQALMEMV-IL--PTKRRDLftGLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSA 281
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIVdFLkdPEKFTRL--GAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 282 SSLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSAR---LANENDasrrlksE-------FLIQFDGVTSNpdD 351
Cdd:COG0465   209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGHD-------EreqtlnqLLVEMDGFEGN--E 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 352 LVIVIGATNKPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKGQsfKLSSH-DLERLAADTEGYSGSDLRALCEE 428
Cdd:COG0465   280 GVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKK--PLAPDvDLEVIARRTPGFSGADLANLVNE 357


                  ..
gi 1002279290 429 AA 430
Cdd:COG0465   358 AA 359
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 224-379 2.81e-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: 128.78  E-value: 2.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 224 KQALMEMVILPTKRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFMVA 303
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 304 VDRQPSVIFMDEIDSVMSARlANENDAS---RRLKSEFLIQFDGVTSNPDDlVIVIGATNKPQELDDAVLR--RLVKRIY 378
Cdd:cd19527    82 RDAKPCVIFFDELDSLAPSR-GNSGDSGgvmDRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLY 159


                  .
gi 1002279290 379 V 379
Cdd:cd19527   160 L 160
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
216-435 3.64e-34

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 135.93  E-value: 3.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVIL---PTKRRDLftGLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEA 292
Cdd:PRK10733  153 DVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 293 EKLVRTLFMVAVDRQPSVIFMDEIDSVMSAR---LANENDASRRLKSEFLIQFDGVTSNpdDLVIVIGATNKPQELDDAV 369
Cdd:PRK10733  230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRgagLGGGHDEREQTLNQMLVEMDGFEGN--EGIIVIAATNRPDVLDPAL 307

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002279290 370 LR--RLVKRIYVPLPDPNVRRLLLKTQLKGQSFKlSSHDLERLAADTEGYSGSDLRALCEEAAMMPIR 435
Cdd:PRK10733  308 LRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 223-378 3.11e-32

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: 120.61  E-value: 3.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 223 AKQALMEMVILPTKRRDLFTGLRRPAR-GLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEAEKLVRTLFM 301
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279290 302 VAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNpdDLVIVIGATNKPQELDDAVLR--RLVKRIY 378
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGL--DGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 216-372 3.01e-31

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: 118.38  E-value: 3.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMEMVILPTKRRDLFTGLR-RPARGLLLFGPPGNGKTMLAKAVASE-----SEATFFNVSASSLTSKWV 289
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAEcskggQKVSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDGVTSNPDdlVIVIGATNKPQELDDAv 369
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPA- 157


                  ...
gi 1002279290 370 LRR 372
Cdd:cd19517   158 LRR 160
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 46-124 2.46e-30

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 112.76  E-value: 2.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279290  46 LRGYFELAKEEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAKWQTQVEERLRVL 124
Cdd:cd02679     1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVPSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 236-381 3.12e-23

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: 95.68  E-value: 3.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 236 KRRDLFTGLRRPARGLLLFGPPGNGKTMLAKAVA---SESEATFFNVSASSLTSKWVGEAEK---LVRTLFMVAVDRQPS 309
Cdd:cd00009     7 IEALREALELPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPG 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002279290 310 VIFMDEIDSVmsarlanendaSRRLKSEFLIQFDGVTSNPD--DLVIVIGATNKP--QELDDAVLRRLVKRIYVPL 381
Cdd:cd00009    87 VLFIDEIDSL-----------SRGAQNALLRVLETLNDLRIdrENVRVIGATNRPllGDLDRALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 249-371 1.04e-15

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: 74.83  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 249 RGLLLFGPPGNGKTMLAKAVaseseATFFN------VSASSLTSKWVGEAEKLVRTLFMVAVDRQPS--------VIFMD 314
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQI-----GKMLNarepkiVNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFD 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002279290 315 EIDSVMSARLANENDAS--RRLKSEFLIQFDGVtsnpDDL--VIVIGATNKPQELDDAVLR 371
Cdd:cd19504   111 EIDAICKQRGSMAGSTGvhDTVVNQLLSKIDGV----EQLnnILVIGMTNRKDLIDEALLR 167
ycf46 CHL00195
Ycf46; Provisional
 209-480 3.34e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 77.75  E-value: 3.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 209 SPAVKWEDVAGLDKAKQALmemvilpTKRRDLFT------GLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSAS 282
Cdd:CHL00195  222 SVNEKISDIGGLDNLKDWL-------KKRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVG 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 283 SLTSKWVGEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMSaRLANENDA--SRRLKSEFLIQFDGVTSNpddlVIVIGATN 360
Cdd:CHL00195  294 KLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFS-NSESKGDSgtTNRVLATFITWLSEKKSP----VFVVATAN 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 361 KPQELDDAVLR--RLVKRIYVPLPDPNVRRLLLKTQLKG---QSFKlsSHDLERLAADTEGYSGSDLRALCEEA---AMM 432
Cdd:CHL00195  369 NIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKfrpKSWK--KYDIKKLSKLSNKFSGAEIEQSIIEAmyiAFY 446

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002279290 433 PIRELGPQNILtIKANQLRPLKYedfkkamtvirpsLQKSKWDELEKW 480
Cdd:CHL00195  447 EKREFTTDDIL-LALKQFIPLAQ-------------TEKEQIEALQNW 480
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 247-383 1.51e-13

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 68.17  E-value: 1.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290  247 PARGLLLFGPPGNGKTMLAKAVASESEATFFNV-----------------SASSLTSKWVGEAEKLVRTLFMVAVDRQPS 309
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002279290  310 VIFMDEIDSVMSARLANENDASRRLKSEFLIQfdgvtsnPDDLVIVIGATNKPQELDDAVLRRLV-KRIYVPLPD 383
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALLRRRFdRRIVLLLIL 148
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 249-377 6.04e-13

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: 66.40  E-value: 6.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 249 RGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWVGEA--EKLVRTLFMVAVDRQPSVIFMDEIDSVMSARLAN 326
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002279290 327 ENDAS--RRLKSEFLIQFDGVtsNPDDLVIVIGATNKPQELDDAVLRRLVKRI 377
Cdd:cd19506   107 TEKQLdpKRLKKDLPKILKSL--KPEDRVLIVGTTSRPFEADLKSFCKVYNKI 157
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 249-379 7.29e-13

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 67.47  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 249 RGLLLFGPPGNGKTMLAKAVASE---------SEATFFNVSASSLTSKWVGEAEKLVRTLF-----MVAVDRQPSVIFMD 314
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqeLIDDKDALVFVLID 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279290 315 EIDSVMSARLA----NENDASRRLKSEFLIQFDGVTSNPDDLVIVigATNKPQELDDAVLRRLVKRIYV 379
Cdd:cd19508   133 EVESLAAARSAsssgTEPSDAIRVVNAVLTQIDRIKRYHNNVILL--TSNLLEKIDVAFVDRADIKQYI 199
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
47-121 2.50e-12

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 62.33  E-value: 2.50e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002279290   47 RGYFELAKEEIDKAVRAEEWGLPDDAAAHYRNALRVMLEAKAARVPDAVSSSERGQVRVYQEKIAKWQTQVEERL 121
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLERL 76
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 216-372 6.74e-12

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: 63.54  E-value: 6.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 216 DVAGLDKAKQALMemvilptKRRDLFT------GLRRPaRGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSKWV 289
Cdd:cd19507     1 DVGGLDNLKDWLK-------KRKAAFSkqasayGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKLVRTLFMVAVDRQPSVIFMDEIDSVMS-ARLANENDASRRLKSEFLIQFDGVTSNpddlVIVIGATNKPQELDDA 368
Cdd:cd19507    73 GESESRLRQMIQTAEAIAPCVLWIDEIEKGFSnADSKGDSGTSSRVLGTFLTWLQEKKKP----VFVVATANNVQSLPPE 148


                  ....
gi 1002279290 369 VLRR 372
Cdd:cd19507   149 LLRK 152
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 227-379 7.09e-12

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: 63.14  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 227 LMEMVILPTKRRDLFTGLRRP-ARGLLLFGPPGNGKTMLAKAVASESEATF--FNVSASSLTSKwvgeaeklvRTLFMVA 303
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPyRRGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVLTDD---------RLNHLLN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 304 VDRQPSVIFMDEIDSVMSARLANE------NDASRRLKSEFLIQFDGVTSNpdDLVIVIGATNKPQELDDAVLR--RLVK 375
Cdd:cd19510    72 TAPKQSIILLEDIDAAFESREHNKknpsayGGLSRVTFSGLLNALDGVASS--EERIVFMTTNHIERLDPALIRpgRVDM 149


                  ....
gi 1002279290 376 RIYV 379
Cdd:cd19510   150 KIYM 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 406-436 3.87e-10

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 54.85  E-value: 3.87e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1002279290 406 DLERLAADTEGYSGSDLRALCEEAAMMPIRE 436
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRR 33
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 251-435 5.81e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 61.25  E-value: 5.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 251 LLLFGPPGNGKTMLAKAVASESEATFFNVSASslTSKwVGEAEKLVRTLFMVAVDRQPSVIFMDEIdsvmsarlanenda 330
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAV--TSG-VKDLREVIEEARQRRSAGRRTILFIDEI-------------- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 331 sRRL-KS--EFLIQF--DGvtsnpddLVIVIGAT--NkPQ-ELDDAVLRRLvkRIYV--PLPDPNVRRLLLK--TQLKGQ 398
Cdd:PRK13342  102 -HRFnKAqqDALLPHveDG-------TITLIGATteN-PSfEVNPALLSRA--QVFElkPLSEEDIEQLLKRalEDKERG 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002279290 399 SFKLSSHDLERLAAdtegYSGSDLRA---LCEEAAMMPIR 435
Cdd:PRK13342  171 LVELDDEALDALAR----LANGDARRalnLLELAALGVDS 206
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 251-425 1.55e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.52  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 251 LLLFGPPGNGKTMLAKAVASESEATFFNVSASslTSKwVGEAEKLVRTLFMVAVDRQPSVIFMDEIDsvmsaRLaneN-- 328
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSAV--TSG-VKDIREVIEEARERRAYGRRTILFVDEIH-----RF---Nka 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 329 --DAsrrlkseFLiqfdgvtsnP---DDLVIVIGAT--NKPQELDDAVLRRLvkRIYV--PLPDPNVRRLL------LKT 393
Cdd:COG2256   121 qqDA-------LL---------PhveDGTITLIGATteNPSFEVNSALLSRC--RVFVlkPLSEEDLEQLLeraladDER 182

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1002279290 394 QLKGQSFKLSSHDLERLAAdtegYSGSDLRAL 425
Cdd:COG2256   183 GLGGYKLELDDEALEALAR----LADGDARRA 210
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 217-332 7.66e-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: 49.30  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 217 VAGLDKAKQALMEMVILPTKRRDLFTGLRRPA--RGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTS-KWVG-EA 292
Cdd:cd19498    13 IIGQDEAKRAVAIALRNRWRRMQLPEELRDEVtpKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDV 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002279290 293 EKLVRTLFmvavdrqPSVIFMDEIDSVMSARLANENDASR 332
Cdd:cd19498    93 ESIIRDLV-------EGIVFIDEIDKIAKRGGSSGPDVSR 125
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 245-373 1.01e-06

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: 48.29  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 245 RRPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSkwVG-EAEKLVRTLFMVA-VDRQPSVIFMDEIDSVMSA 322
Cdd:cd19512    19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRK 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002279290 323 RLANE-NDASRRLKSEFLIQfDGVTSNpdDLVIVIgATNKPQELDDAVLRRL 373
Cdd:cd19512    97 RSTEKiSEDLRAALNAFLYR-TGEQSN--KFMLVL-ASNQPEQFDWAINDRI 144
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 252-317 1.75e-05

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: 45.26  E-value: 1.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279290 252 LLFGPPGNGKTMLAKAVASE---SEATFFNVSASSLT-----SKWVGEAEKLVR----TLFMVAVDRQP-SVIFMDEID 317
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMeehsvSRLIGAPPGYVGyeegGQLTEAVRRKPySIVLIDEIE 85
PRK04195 PRK04195
replication factor C large subunit; Provisional
 215-483 4.61e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 45.68  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 215 EDVAGLDKAKQALMEMVILPTKRRdlftglrrPARGLLLFGPPGNGKTMLAKAVASESEATFFNVSAS-----SLTSKWV 289
Cdd:PRK04195   14 SDVVGNEKAKEQLREWIESWLKGK--------PKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIERVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 290 GEAEKlVRTLFmvAVDRQpsVIFMDEIDSvMSARlaneNDA------SRRLKSefliqfdgvTSNPddlvIVIGAtNKPQ 363
Cdd:PRK04195   86 GEAAT-SGSLF--GARRK--LILLDEVDG-IHGN----EDRggaraiLELIKK---------AKQP----IILTA-NDPY 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 364 ELDDAVLRRLVKRI-YVPLPDPNVRRLLLKTqLKGQSFKLSSHDLERLAADTEGysgsDLRA----LceEAAMMPIRELG 438
Cdd:PRK04195  142 DPSLRELRNACLMIeFKRLSTRSIVPVLKRI-CRKEGIECDDEALKEIAERSGG----DLRSaindL--QAIAEGYGKLT 214

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002279290 439 PQNI--LTIKANQLRP-------LKYEDFKKAMTVIRpSLQKSkWDELEKWNEE 483
Cdd:PRK04195  215 LEDVktLGRRDREESIfdaldavFKARNADQALEASY-DVDED-PDDLIEWIDE 266
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 219-380 5.22e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 45.61  E-value: 5.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 219 GLDKAKQALMEMvilptkRRDLFTGLRRPARGL---------LLFGPPGNGKTMLAKAVASE-------SEATFFNVSAS 282
Cdd:TIGR03922 280 GLERVKRQVAAL------KSSTAMALARAERGLpvaqtsnhmLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRA 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 283 SLTSKWVGEAEKLVRTLFMVAVDRqpsVIFMDEIDSVMSARLANENDASRRLKSEFLIQFDgvtSNPDDLVIVIG----A 358
Cdd:TIGR03922 354 DLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME---NDRDRLVVIGAgyrkD 427

                         170       180
                  ....*....|....*....|..
gi 1002279290 359 TNKPQELDDAVLRRLVKRIYVP 380
Cdd:TIGR03922 428 LDKFLEVNEGLRSRFTRVIEFP 449
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 217-317 1.26e-04

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.55  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 217 VAGLDKAKQALMEMVILPTkrrdlfTGLRRPARG---LLLFGPPGNGKTMLAKAVA-----SESEATFFNVSA------- 281
Cdd:cd19499    13 VVGQDEAVKAVSDAIRRAR------AGLSDPNRPigsFLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEymekhsv 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002279290 282 SSLTSKWVGEAEKLVRTLFMVAVDRQP-SVIFMDEID 317
Cdd:cd19499    87 SRLIGAPPGYVGYTEGGQLTEAVRRKPySVVLLDEIE 123
44 PHA02544
clamp loader, small subunit; Provisional
 231-336 2.52e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.05  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 231 VILPTKRRDLFTGLRRPAR--GLLLFGP-PGNGKTMLAKAVASESEATFFNVSASSLTSKWV-GEAEKLVRTlfmVAVDR 306
Cdd:PHA02544   23 CILPAADKETFKSIVKKGRipNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFVrNRLTRFAST---VSLTG 99

                          90       100       110
                  ....*....|....*....|....*....|
gi 1002279290 307 QPSVIFMDEIDSVMSArlanenDASRRLKS 336
Cdd:PHA02544  100 GGKVIIIDEFDRLGLA------DAQRHLRS 123
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 225-460 4.61e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 42.08  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 225 QALMEMVILPTKR--RDLFTGLRrpARG-LLLFGPPGNGKTMLAKAVASESEATFFNVS------ASSLTSKWVGEAEKl 295
Cdd:COG0714     7 RAEIGKVYVGQEEliELVLIALL--AGGhLLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILGTYIYDQQT- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 296 vRTLFMVavdRQP---SVIFMDEIDsvmsaRlanendASRRLKS-------EFLIQFDGVTSNPDDLVIVIgATNKPQE- 364
Cdd:COG0714    84 -GEFEFR---PGPlfaNVLLADEIN-----R------APPKTQSalleameERQVTIPGGTYKLPEPFLVI-ATQNPIEq 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 365 -----LDDAVLRRLVKRIYVPLPDPNVRRLLLKtqlkgqsfklsSHDLERLAADTEGYSGSDLRALCEEAAMMPIRELGP 439
Cdd:COG0714   148 egtypLPEAQLDRFLLKLYIGYPDAEEEREILR-----------RHTGRHLAEVEPVLSPEELLALQELVRQVHVSEAVL 216

                         250       260
                  ....*....|....*....|.
gi 1002279290 440 QNILTIkANQLRPLkyEDFKK 460
Cdd:COG0714   217 DYIVDL-VRATREH--PDLRK 234
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
249-299 4.64e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 42.65  E-value: 4.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002279290 249 RGLLLFGPPGNGKTMLAKAVASE--SEATFFNVSASSLTSKWVGEAEKLVRTL 299
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEFLMQAL 117
PRK08116 PRK08116
hypothetical protein; Validated
 241-271 6.11e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.54  E-value: 6.11e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1002279290 241 FTGLRRPARGLLLFGPPGNGKTMLAKAVASE 271
Cdd:PRK08116  107 FEEMKKENVGLLLWGSVGTGKTYLAACIANE 137
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 445-485 6.54e-04

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 37.86  E-value: 6.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002279290 445 IKANQL--RPLKYEDFKKAMTVIRPSLQKSKWDELEKWNEEFG 485
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 215-317 1.30e-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: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 215 EDVAGLDKAKQALMEMvilptkrrdLFTGLRRPA-RG--LLLFGPPGNGKTMLAKAVASESEATFFNVSASSLTSkwvgE 291
Cdd:cd19500    10 ADHYGLEDVKERILEY---------LAVRKLKGSmKGpiLCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRD----E 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002279290 292 AE--------------KLVRTLFMVAVdRQPsVIFMDEID 317
Cdd:cd19500    77 AEirghrrtyvgampgRIIQALKKAGT-NNP-VFLLDEID 114
PRK09862 PRK09862
ATP-dependent protease;
251-288 1.76e-03

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 40.73  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279290 251 LLLFGPPGNGKTMLAKAV-----------ASESEATFFNVSASSLTSKW 288
Cdd:PRK09862  213 LLLIGPPGTGKTMLASRIngllpdlsneeALESAAILSLVNAESVQKQW 261
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 250-373 2.24e-03

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 38.43  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002279290 250 GLLLFGPPGNGKTMLAKAVASE-SEATFFNV------SASSLTSKWV--GEAEKLVRTLFMVAVdRQPSVIFMDEIDSVM 320
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVqltrdtTEEDLFGRRNidPGGASWVDGPLVRAA-REGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002279290 321 SA------RLANENdasRRLksefLIQFDGVTSNPDDLVIVIGATNKP----QELDDAVLRRL 373
Cdd:pfam07728  80 PDvlnsllSLLDER---RLL----LPDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 213-271 2.27e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 2.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002279290 213 KWEDVAGLDKAKQALmEMVILPTKRRDlftglrRPARGLLLFGPPGNGKTMLAKAVASE 271
Cdd:pfam05496   5 TLDEYIGQEKVKENL-KIFIEAAKQRG------EALDHVLLYGPPGLGKTTLANIIANE 56
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 251-270 2.90e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.06  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|
gi 1002279290 251 LLLFGPPGNGKTMLAKAVAS 270
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
252-317 3.96e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 39.37  E-value: 3.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002279290 252 LLFGPPGNGKTMLAKAVASESEATFFNVSASSLT-SKWVGE-AEKLVRTLFMVA---VDR-QPSVIFMDEID 317
Cdd:PRK05342  112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEdVENILLKLLQAAdydVEKaQRGIVYIDEID 183
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 249-295 4.22e-03

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: 39.21  E-value: 4.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002279290 249 RGLLLFGPPGNGKTMLAKAVASE-SEATFFN-VSASSLTSKWVGEAEKL 295
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElGEDTPFTsISGSEVYSLEMKKTEAL 99
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 251-270 7.84e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 38.87  E-value: 7.84e-03
                          10        20
                  ....*....|....*....|
gi 1002279290 251 LLLFGPPGNGKTMLAKAVAS 270
Cdd:COG0606   214 LLMIGPPGSGKTMLARRLPG 233
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
251-271 8.73e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.19  E-value: 8.73e-03
                          10        20
                  ....*....|....*....|.
gi 1002279290 251 LLLFGPPGNGKTMLAKAVASE 271
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANE 74
 
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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