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Conserved domains on  [gi|568939006|ref|XP_006504892|]
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katanin p60 ATPase-containing subunit A-like 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 207-376 2.46e-132

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: 380.10  E-value: 2.46e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 287 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 568939006 367 RRRLEKRIYI 376
Cdd:cd19522  161 RRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 52-452 2.62e-76

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


:

Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 244.82  E-value: 2.62e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  52 WQQVRQELLEEYEQVKSIVSTLESFKMDKPPDFPVSCRDEPFRDPAVWPPPVPAEHRAPPQIRRPNREVRPLRKDVGAGA 131
Cdd:COG0464    6 ALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 132 RGLVGRAHQISKSDKPASRDKDYRARGRDDKARKNVQDGASDSEIPKFDGAGYDKDLVEALERDIVsrnPSIHWDDIADL 211
Cdd:COG0464   86 LSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLEL---REAILDDLGGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 212 EEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRL 289
Cdd:COG0464  163 EEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLRE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 290 LFEMARFYAPTTIFIDEIDSICSRRGTSDEHeASRRVKSELLIQMDGVggaleNDDpskmVMVLAATNFPWDIDEALRRR 369
Cdd:COG0464  242 VFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVVIAATNRPDLLDPALLRR 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 370 LEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRRRINGLSPEEI-RALSKE 448
Cdd:COG0464  312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLlEALERE 391


                 ....
gi 568939006 449 ELQM 452
Cdd:COG0464  392 DIFL 395
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 4-72 2.99e-37

N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar proteins; This model represents the N-terminal domain (NTD) of katanin p60 ATPase-containing subunit A1 (also called p60 katanin 1 or katanin p60 subunit A1), which is organized into an antiparallel three-helix bundle and is responsible for tubulin binding. Katanin p60 subunit A1 plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. It is a microtubule-severing protein (MTSP) that maintains the density of spindle microtubules at the poles in mitotic cells. MSTPs are a group of microtubule-associated proteins essential for multiple microtubule-related processes, including mitosis and meiosis. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles allows depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. Katanin p60 has been implicated in several malignancies; it is aberrantly expressed in prostate cancer patients with bone metastasis where upregulation of katanin P60 inhibits cell proliferation but enhances cell migration. It promotes cell migration in breast cancer where high ketanin p60 expression in tumor tissue is correlated with lymph node metastasis and poor overall survival. Katanin p60 may also be a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer. Katanin is a heterodimer with an AAA catalytic subunit katanin P60 and a non-AAA subunit katanin P80. In ASPM (known as Asp in fly and ASPM-1 in worm), a microcephaly-associated protein family that regulates spindle architecture, the N-terminal domain of katanin p60 subunit (kp60-NTD) and C-terminal domain of katanin p80 subunit form a heterodimer, which then binds conserved motifs in ASPM, thus forming a complex that controls microtubule disassembly at spindle poles; misregulation of this process can lead to microcephaly. p60 katanin-like 1 has been shown to be predominantly enriched within oocytes and ovaries, and essential for oocyte meiosis and maturation. The N-terminal domain of mouse katanin p60 (kp60-NTD) also binds to tubulin; structure studies of kp60-NTD reveal a striking similarity to the microtubule interacting and trafficking (MIT) domains, although their sequence similarities are low.


:

Pssm-ID: 439297  Cd Length: 69  Bit Score: 131.16  E-value: 2.99e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939006   4 AEICENAKKGREYALLGNYDSSMVYYQGVIQQIQRHCQSLRDPATKAKWQQVRQELLEEYEQVKSIVST 72
Cdd:cd21748    1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 448-486 4.76e-07

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: 46.72  E-value: 4.76e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568939006  448 EELQMP-VTRGDLELALKKIAKSVSAADLEKYEKWMVEFG 486
Cdd:pfam09336  22 DKLLEPpVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 207-376 2.46e-132

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: 380.10  E-value: 2.46e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 287 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 568939006 367 RRRLEKRIYI 376
Cdd:cd19522  161 RRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 201-447 1.72e-92

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 284.21  E-value: 1.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 201 PSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSK 278
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 279 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVggalendDPSKMVMVLAATNF 358
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNR 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 359 PWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRRRING 436
Cdd:COG1222  225 PDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                        250
                 ....*....|..
gi 568939006 437 LSPEEIR-ALSK 447
Cdd:COG1222  305 VTMEDLEkAIEK 316
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 186-488 9.76e-78

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: 257.53  E-value: 9.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  186 KDLVEALE-------RDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLA 256
Cdd:TIGR01243 426 KDFMEALKmvepsaiREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  257 KAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDG 336
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  337 VggalendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYS 414
Cdd:TIGR01243 585 I-------QELSNVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939006  415 GADITNICRDASLMAMRRRINGLSPEEIRALSKEELQ-MPVTRGDLELALKKIAKSVSAADLEKYEKWMVEFGSA 488
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRL 732
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 52-452 2.62e-76

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 244.82  E-value: 2.62e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  52 WQQVRQELLEEYEQVKSIVSTLESFKMDKPPDFPVSCRDEPFRDPAVWPPPVPAEHRAPPQIRRPNREVRPLRKDVGAGA 131
Cdd:COG0464    6 ALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 132 RGLVGRAHQISKSDKPASRDKDYRARGRDDKARKNVQDGASDSEIPKFDGAGYDKDLVEALERDIVsrnPSIHWDDIADL 211
Cdd:COG0464   86 LSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLEL---REAILDDLGGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 212 EEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRL 289
Cdd:COG0464  163 EEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLRE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 290 LFEMARFYAPTTIFIDEIDSICSRRGTSDEHeASRRVKSELLIQMDGVggaleNDDpskmVMVLAATNFPWDIDEALRRR 369
Cdd:COG0464  242 VFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVVIAATNRPDLLDPALLRR 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 370 LEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRRRINGLSPEEI-RALSKE 448
Cdd:COG0464  312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLlEALERE 391


                 ....
gi 568939006 449 ELQM 452
Cdd:COG0464  392 DIFL 395
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 201-468 1.27e-71

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 232.42  E-value: 1.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 201 PSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSK 278
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 279 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSDEHEASRRVkSELLIQMDGVggalendDPSKMVMVLAA 355
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-------DPRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 356 TNFPwDI-DEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRR 432
Cdd:PRK03992 277 TNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568939006 433 RinglspeeiralsKEElqmpVTRGDLELALKKIAK 468
Cdd:PRK03992 356 D-------------RTE----VTMEDFLKAIEKVMG 374
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 242-378 8.35e-54

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 177.02  E-value: 8.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGtSDEHE 321
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG-SGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939006  322 ASRRVKSELLIQMDGVggalenDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPL 378
Cdd:pfam00004  80 ESRRVVNQLLTELDGF------TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 4-72 2.99e-37

N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar proteins; This model represents the N-terminal domain (NTD) of katanin p60 ATPase-containing subunit A1 (also called p60 katanin 1 or katanin p60 subunit A1), which is organized into an antiparallel three-helix bundle and is responsible for tubulin binding. Katanin p60 subunit A1 plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. It is a microtubule-severing protein (MTSP) that maintains the density of spindle microtubules at the poles in mitotic cells. MSTPs are a group of microtubule-associated proteins essential for multiple microtubule-related processes, including mitosis and meiosis. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles allows depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. Katanin p60 has been implicated in several malignancies; it is aberrantly expressed in prostate cancer patients with bone metastasis where upregulation of katanin P60 inhibits cell proliferation but enhances cell migration. It promotes cell migration in breast cancer where high ketanin p60 expression in tumor tissue is correlated with lymph node metastasis and poor overall survival. Katanin p60 may also be a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer. Katanin is a heterodimer with an AAA catalytic subunit katanin P60 and a non-AAA subunit katanin P80. In ASPM (known as Asp in fly and ASPM-1 in worm), a microcephaly-associated protein family that regulates spindle architecture, the N-terminal domain of katanin p60 subunit (kp60-NTD) and C-terminal domain of katanin p80 subunit form a heterodimer, which then binds conserved motifs in ASPM, thus forming a complex that controls microtubule disassembly at spindle poles; misregulation of this process can lead to microcephaly. p60 katanin-like 1 has been shown to be predominantly enriched within oocytes and ovaries, and essential for oocyte meiosis and maturation. The N-terminal domain of mouse katanin p60 (kp60-NTD) also binds to tubulin; structure studies of kp60-NTD reveal a striking similarity to the microtubule interacting and trafficking (MIT) domains, although their sequence similarities are low.


Pssm-ID: 439297  Cd Length: 69  Bit Score: 131.16  E-value: 2.99e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939006   4 AEICENAKKGREYALLGNYDSSMVYYQGVIQQIQRHCQSLRDPATKAKWQQVRQELLEEYEQVKSIVST 72
Cdd:cd21748    1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 238-380 3.60e-17

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: 78.18  E-value: 3.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006   238 PWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYAPT 300
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006   301 TIFIDEIDSICsrrgtsdeheasrRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 379
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147


                   .
gi 568939006   380 T 380
Cdd:smart00382 148 L 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 400-444 5.72e-13

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 62.94  E-value: 5.72e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568939006  400 DVHLEDIADKTEGYSGADITNICRDASLMAMRRRINGLSPEEIRA 444
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 448-486 4.76e-07

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: 46.72  E-value: 4.76e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568939006  448 EELQMP-VTRGDLELALKKIAKSVSAADLEKYEKWMVEFG 486
Cdd:pfam09336  22 DKLLEPpVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 242-307 1.99e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 38.63  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939006 242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYAPTTIFIDEI 307
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINVNLElsrrllELPEKQR--ALRAPRLLDEIAEKSSGDVVLLDNI 88
 
Name Accession Description Interval E-value
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 207-376 2.46e-132

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: 380.10  E-value: 2.46e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 287 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 568939006 367 RRRLEKRIYI 376
Cdd:cd19522  161 RRRLEKRIYI 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 208-376 4.57e-95

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: 284.63  E-value: 4.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 208 IADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLV 287
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 288 RLLFEMARFYAPTTIFIDEIDSICSRRGtSDEHEASRRVKSELLIQMDGVGgalenDDPSKMVMVLAATNFPWDIDEALR 367
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERG-SGEHEASRRVKTEFLVQMDGVL-----NKPEDRVLVLGATNRPWELDEAFL 154


                 ....*....
gi 568939006 368 RRLEKRIYI 376
Cdd:cd19509  155 RRFEKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 201-447 1.72e-92

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 284.21  E-value: 1.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 201 PSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSK 278
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 279 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVggalendDPSKMVMVLAATNF 358
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNR 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 359 PWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRRRING 436
Cdd:COG1222  225 PDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                        250
                 ....*....|..
gi 568939006 437 LSPEEIR-ALSK 447
Cdd:COG1222  305 VTMEDLEkAIEK 316
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 201-376 1.03e-78

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: 242.85  E-value: 1.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 201 PSIHWDDIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYR 280
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 281 GESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGtSDEHEASRRVKSELLIQMDGVGgaleNDDPSkmVMVLAATNFPW 360
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRG-EGESEASRRIKTELLVQMNGVG----NDSQG--VLVLGATNIPW 154

                        170
                 ....*....|....*.
gi 568939006 361 DIDEALRRRLEKRIYI 376
Cdd:cd19521  155 QLDSAIRRRFEKRIYI 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 186-488 9.76e-78

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: 257.53  E-value: 9.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  186 KDLVEALE-------RDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLA 256
Cdd:TIGR01243 426 KDFMEALKmvepsaiREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  257 KAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDG 336
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  337 VggalendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYS 414
Cdd:TIGR01243 585 I-------QELSNVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939006  415 GADITNICRDASLMAMRRRINGLSPEEIRALSKEELQ-MPVTRGDLELALKKIAKSVSAADLEKYEKWMVEFGSA 488
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRL 732
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 185-376 1.78e-76

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: 237.96  E-value: 1.78e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 185 DKDLVEALERDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECG 264
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 265 TTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSdEHEASRRVKSELLIQMDGVggaleND 344
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-EHESSRRIKTEFLVQLDGA-----TT 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568939006 345 DPSKMVMVLAATNFPWDIDEALRRRLEKRIYI 376
Cdd:cd19525  155 SSEDRILVVGATNRPQEIDEAARRRLVKRLYI 186
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 52-452 2.62e-76

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 244.82  E-value: 2.62e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  52 WQQVRQELLEEYEQVKSIVSTLESFKMDKPPDFPVSCRDEPFRDPAVWPPPVPAEHRAPPQIRRPNREVRPLRKDVGAGA 131
Cdd:COG0464    6 ALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 132 RGLVGRAHQISKSDKPASRDKDYRARGRDDKARKNVQDGASDSEIPKFDGAGYDKDLVEALERDIVsrnPSIHWDDIADL 211
Cdd:COG0464   86 LSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLEL---REAILDDLGGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 212 EEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRL 289
Cdd:COG0464  163 EEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLRE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 290 LFEMARFYAPTTIFIDEIDSICSRRGTSDEHeASRRVKSELLIQMDGVggaleNDDpskmVMVLAATNFPWDIDEALRRR 369
Cdd:COG0464  242 VFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVVIAATNRPDLLDPALLRR 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 370 LEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRRRINGLSPEEI-RALSKE 448
Cdd:COG0464  312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLlEALERE 391


                 ....
gi 568939006 449 ELQM 452
Cdd:COG0464  392 DIFL 395
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 201-468 1.27e-71

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 232.42  E-value: 1.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 201 PSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSK 278
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 279 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSDEHEASRRVkSELLIQMDGVggalendDPSKMVMVLAA 355
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-------DPRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 356 TNFPwDI-DEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRR 432
Cdd:PRK03992 277 TNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 568939006 433 RinglspeeiralsKEElqmpVTRGDLELALKKIAK 468
Cdd:PRK03992 356 D-------------RTE----VTMEDFLKAIEKVMG 374
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 207-376 6.97e-64

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: 204.31  E-value: 6.97e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 287 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSdEHEASRRVKSELLIQMDGVGGalendDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEG-EHEASRRLKTEFLIEFDGVQS-----NGDDRVLVMGATNRPQELDDAV 154

                        170
                 ....*....|
gi 568939006 367 RRRLEKRIYI 376
Cdd:cd19524  155 LRRFTKRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 190-469 6.06e-61

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 212.46  E-value: 6.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  190 EALERDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTF 267
Cdd:TIGR01243 162 KPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAGAYF 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  268 FNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRgtsDE--HEASRRVKSELLIQMDGVGGalendd 345
Cdd:TIGR01243 241 ISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR---EEvtGEVEKRVVAQLLTLMDGLKG------ 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  346 pSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICR 423
Cdd:TIGR01243 312 -RGRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAK 390

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 568939006  424 DASLMAMRRRIN----GLSPEEIRALSKEELQmpVTRGDLELALKKIAKS 469
Cdd:TIGR01243 391 EAAMAALRRFIRegkiNFEAEEIPAEVLKELK--VTMKDFMEALKMVEPS 438
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 242-378 8.35e-54

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 177.02  E-value: 8.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGtSDEHE 321
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG-SGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939006  322 ASRRVKSELLIQMDGVggalenDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPL 378
Cdd:pfam00004  80 ESRRVVNQLLTELDGF------TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 207-376 1.29e-53

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: 177.62  E-value: 1.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIR--RPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 285 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDeHEASRRVKSELLIQMDGvggaLENDDPSKmVMVLAATNFPWDIDE 364
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTD-HEATAMMKAEFMSLWDG----LSTDGNCR-VIVMGATNRPQDLDE 154

                        170
                 ....*....|..
gi 568939006 365 ALRRRLEKRIYI 376
Cdd:cd19520  155 AILRRMPKRFHI 166
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 214-376 1.47e-53

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: 177.48  E-value: 1.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 214 AKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLF 291
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 292 EMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGgalenddPSKMVMVLAATNFPWDIDEALRR--R 369
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIE-------SLKGVVVIAATNRPDMIDPALLRpgR 152


                 ....*..
gi 568939006 370 LEKRIYI 376
Cdd:cd19511  153 LDKLIYV 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 207-376 1.09e-52

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: 175.17  E-value: 1.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 285 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGtSDEHEASRRVKSELLIQMDGVggalendDPSKMVMVLAATNFPWDIDE 364
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKRE-EDQREVERRVVAQLLTLMDGM-------SSRGKVVVIAATNRPDAIDP 151

                        170
                 ....*....|....
gi 568939006 365 ALRR--RLEKRIYI 376
Cdd:cd19503  152 ALRRpgRFDREVEI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
205-477 1.35e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.77  E-value: 1.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 205 WDDIADLEEAKKLLREAVvlpmwmpDFFKGIRRP-----W--KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTS 277
Cdd:COG1223    1 LDDVVGQEEAKKKLKLII-------KELRRRENLrkfglWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 278 KYRGESEKLVRLLFEMARfYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGvggalendDPSKmVMVLAATN 357
Cdd:COG1223   74 SYLGETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDG--------LPSG-SVVIAATN 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 358 FPWDIDEALRRRLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDaslmAMRRRIngL 437
Cdd:COG1223  144 HPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKT----ALKKAI--L 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568939006 438 SPEEIralskeelqmpVTRGDLELALKKIAKSVSAADLEK 477
Cdd:COG1223  218 EDREK-----------VTKEDLEEALKQRKERKKEPKKEG 246
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
206-466 2.21e-51

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 183.31  E-value: 2.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 206 DDIADLEEAKKLLREAVvlpmwmpDFFK--------GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTS 277
Cdd:COG0465  142 DDVAGVDEAKEELQEIV-------DFLKdpekftrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVE 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 278 KY------RgeseklVRLLFEMARFYAPTTIFIDEIDSICSRRGTS-----DEHEasrRVKSELLIQMDGVggalendDP 346
Cdd:COG0465  214 MFvgvgasR------VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghDERE---QTLNQLLVEMDGF-------EG 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 347 SKMVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICR 423
Cdd:COG0465  278 NEGVIVIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVN 356

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568939006 424 DASLMAMRRRinglspeeiralsKEElqmpVTRGDLELALKKI 466
Cdd:COG0465  357 EAALLAARRN-------------KKA----VTMEDFEEAIDRV 382
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 214-376 1.94e-50

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 169.00  E-value: 1.94e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 214 AKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEM 293
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 294 ARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVggalENDDPskmVMVLAATNFPWDIDEALRR--RLE 371
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGV----NSRSK---VLVIAATNRPDLLDPALLRpgRFD 153


                 ....*
gi 568939006 372 KRIYI 376
Cdd:cd19481  154 EVIEF 158
ftsH CHL00176
cell division protein; Validated
 203-442 6.34e-50

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 180.63  E-value: 6.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 203 IHWDDIADLEEAKKLLREAVVLpMWMPDFFKGI-RRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRG 281
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 282 ESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGT-----SDEHEasrRVKSELLIQMDGVGGalenddpSKMVMVLAAT 356
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigggNDERE---QTLNQLLTEMDGFKG-------NKGVIVIAAT 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 357 NFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMRRRI 434
Cdd:CHL00176 329 NRVDILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKK 408


                 ....*...
gi 568939006 435 NGLSPEEI 442
Cdd:CHL00176 409 ATITMKEI 416
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 197-432 9.20e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 172.26  E-value: 9.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 197 VSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSST 274
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEqiGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 275 LTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSDEHEAsRRVKSELLIQMDGVggalendDPSKMVM 351
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGADREV-QRILLELLNQMDGF-------DQTTNVK 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 352 VLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMA 429
Cdd:PTZ00454 287 VIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQA 366


                 ...
gi 568939006 430 MRR 432
Cdd:PTZ00454 367 VRK 369
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 197-433 6.05e-48

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.11  E-value: 6.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 197 VSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSST 274
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 275 LTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSDEHEASRRVKSELLIQMDGVggalendDPSKMVMV 352
Cdd:PTZ00361 253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGF-------DSRGDVKV 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 353 LAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAM 430
Cdd:PTZ00361 326 IMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405


                 ...
gi 568939006 431 RRR 433
Cdd:PTZ00361 406 RER 408
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 205-374 9.32e-48

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: 162.51  E-value: 9.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 205 WDDIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGE 282
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 283 SEKLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSDEHEASRRVkSELLIQMDGVggalendDPSKMVMVLAATNFP 359
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTM-LELLNQLDGF-------DPRGNIKVIMATNRP 152

                        170
                 ....*....|....*..
gi 568939006 360 WDIDEALRR--RLEKRI 374
Cdd:cd19502  153 DILDPALLRpgRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 214-376 9.50e-46

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: 156.89  E-value: 9.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 214 AKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLF 291
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 292 EMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVggalendDPSKMVMVLAATNFPWDIDEALRR--R 369
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-------EEMNGVVVIAATNRPDIIDPALLRagR 152


                 ....*..
gi 568939006 370 LEKRIYI 376
Cdd:cd19529  153 FDRLIYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
207-434 1.33e-43

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 162.90  E-value: 1.33e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLpMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 285 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SDEHEASRRVKSELLIQMDGVGGalenddpSKMVMVLAATNFPWDI 362
Cdd:PRK10733 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEG-------NEGIIVIAATNRPDVL 303

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939006 363 DEALRR--RLEKRIYIPLPTAKGRAELLKISLREVELDPDVHLEDIADKTEGYSGADITNICRDASLMAMR--RRI 434
Cdd:PRK10733 304 DPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARgnKRV 379
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 207-377 4.10e-42

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: 147.58  E-value: 4.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKaiGIKPP-RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 285 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSdEHEASRRVKSELLIQMDGVGGalenddpSKMVMVLAATNFPWDIDE 364
Cdd:cd19519   80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT-HGEVERRIVSQLLTLMDGLKQ-------RAHVIVMAATNRPNSIDP 151

                        170
                 ....*....|....*
gi 568939006 365 ALRR--RLEKRIYIP 377
Cdd:cd19519  152 ALRRfgRFDREIDIG 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 215-376 2.83e-41

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 144.96  E-value: 2.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 215 KKLLREAVVLPMWMPD-FFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEM 293
Cdd:cd19528    2 KRELQELVQYPVEHPDkFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 294 ARFYAPTTIFIDEIDSICSRRGTS--DEHEASRRVKSELLIQMDGVggalendDPSKMVMVLAATNFPWDIDEALRR--R 369
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNigDAGGAADRVINQILTEMDGM-------NTKKNVFIIGATNRPDIIDPAILRpgR 154


                 ....*..
gi 568939006 370 LEKRIYI 376
Cdd:cd19528  155 LDQLIYI 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 207-376 6.82e-41

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: 144.26  E-value: 6.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 287 VRLLFEMARFYAPTTIFIDEIDSICSRRgtSDEHEASRRVKSELLIQMDGVGGAlenddPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQ--DDEASPVGRLQVELLAQLDGVLGS-----GEDGVLVVCTTSKPEEIDESL 153

                        170
                 ....*....|
gi 568939006 367 RRRLEKRIYI 376
Cdd:cd19523  154 RRYFSKRLLV 163
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 203-376 5.51e-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: 141.99  E-value: 5.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 203 IHWDDIADLEEAKKLLREAVvlpmwmpDFFK--------GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSST 274
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVV-------EFLKnpekftklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 275 LTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SDEHEASRRVKSELLIQMDGVGGalenddpSKMVMV 352
Cdd:cd19501   73 FVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglGGGHDEREQTLNQLLVEMDGFES-------NTGVIV 145

                        170       180
                 ....*....|....*....|....*.
gi 568939006 353 LAATNFPWDIDEALRR--RLEKRIYI 376
Cdd:cd19501  146 IAATNRPDVLDPALLRpgRFDRQVYV 171
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 211-376 9.11e-38

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: 135.69  E-value: 9.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 211 LEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVR 288
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 289 LLFEMARFYAPTTIFIDEIDSICSRRGTSdEHEASRRVKSELLIQMDGVGGALEnddpskmVMVLAATNFPWDIDEALRR 368
Cdd:cd19530   80 QVFQRARASAPCVIFFDEVDALVPKRGDG-GSWASERVVNQLLTEMDGLEERSN-------VFVIAATNRPDIIDPAMLR 151

                        170
                 ....*....|
gi 568939006 369 --RLEKRIYI 376
Cdd:cd19530  152 pgRLDKTLYV 161
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 4-72 2.99e-37

N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar proteins; This model represents the N-terminal domain (NTD) of katanin p60 ATPase-containing subunit A1 (also called p60 katanin 1 or katanin p60 subunit A1), which is organized into an antiparallel three-helix bundle and is responsible for tubulin binding. Katanin p60 subunit A1 plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. It is a microtubule-severing protein (MTSP) that maintains the density of spindle microtubules at the poles in mitotic cells. MSTPs are a group of microtubule-associated proteins essential for multiple microtubule-related processes, including mitosis and meiosis. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles allows depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. Katanin p60 has been implicated in several malignancies; it is aberrantly expressed in prostate cancer patients with bone metastasis where upregulation of katanin P60 inhibits cell proliferation but enhances cell migration. It promotes cell migration in breast cancer where high ketanin p60 expression in tumor tissue is correlated with lymph node metastasis and poor overall survival. Katanin p60 may also be a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer. Katanin is a heterodimer with an AAA catalytic subunit katanin P60 and a non-AAA subunit katanin P80. In ASPM (known as Asp in fly and ASPM-1 in worm), a microcephaly-associated protein family that regulates spindle architecture, the N-terminal domain of katanin p60 subunit (kp60-NTD) and C-terminal domain of katanin p80 subunit form a heterodimer, which then binds conserved motifs in ASPM, thus forming a complex that controls microtubule disassembly at spindle poles; misregulation of this process can lead to microcephaly. p60 katanin-like 1 has been shown to be predominantly enriched within oocytes and ovaries, and essential for oocyte meiosis and maturation. The N-terminal domain of mouse katanin p60 (kp60-NTD) also binds to tubulin; structure studies of kp60-NTD reveal a striking similarity to the microtubule interacting and trafficking (MIT) domains, although their sequence similarities are low.


Pssm-ID: 439297  Cd Length: 69  Bit Score: 131.16  E-value: 2.99e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939006   4 AEICENAKKGREYALLGNYDSSMVYYQGVIQQIQRHCQSLRDPATKAKWQQVRQELLEEYEQVKSIVST 72
Cdd:cd21748    1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 214-375 1.62e-35

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: 129.47  E-value: 1.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 214 AKKLLREAVVLPMWMPDFFKGIR-RPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFE 292
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPlRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 293 MARFYAPTTIFIDEIDSICSRRGtSDEHEASRRVKSELLIQMDGVGGAlenddpsKMVMVLAATNFPWDIDEALRR--RL 370
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRG-HDSTGVTDRVVNQLLTQLDGVEGL-------DGVYVLAATSRPDLIDPALLRpgRL 152


                 ....*
gi 568939006 371 EKRIY 375
Cdd:cd19526  153 DKLVY 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 207-374 1.88e-35

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 129.83  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQhlGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 285 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSdEHEASRRVKSELLIQMDGVGgalENDDPSKMVMVLAATNFPWDIDE 364
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESA-QREMERRIVSQLLTCMDELN---NEKTAGGPVLVIGATNRPDSLDP 155

                        170
                 ....*....|..
gi 568939006 365 ALRR--RLEKRI 374
Cdd:cd19518  156 ALRRagRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 215-376 2.58e-34

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 126.47  E-value: 2.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 215 KKLLREAVVLPMWMPDFF-KGIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEM 293
Cdd:cd19527    2 KKEILDTIQLPLEHPELFsSGLRKR-SGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 294 ARFYAPTTIFIDEIDSICSRRGTS-DEHEASRRVKSELLIQMDGVGGALENddpskmVMVLAATNFPWDIDEALRR--RL 370
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMSSSGQD------VFVIGATNRPDLLDPALLRpgRF 154


                 ....*.
gi 568939006 371 EKRIYI 376
Cdd:cd19527  155 DKLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 207-375 1.87e-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: 118.77  E-value: 1.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLLREAVVLPMWMPDFFKGIR-RPWKGVLMVGPPGTGKTMLAKAVATECGT-----TFFNVSSSTLTSKYR 280
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 281 GESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVkSELLIQMDGVggalendDPSKMVMVLAATNFPW 360
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIV-STLLALMDGL-------DNRGQVVVIGATNRPD 152

                        170
                 ....*....|....*..
gi 568939006 361 DIDEALRR--RLEKRIY 375
Cdd:cd19517  153 ALDPALRRpgRFDREFY 169
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 209-378 1.37e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 99.53  E-value: 1.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 209 ADLEEAKKLLREAVvlpmwmpdffkgIRRPWKGVLMVGPPGTGKTMLAKAVATEC---GTTFFNVSSSTLTSKYRGESEK 285
Cdd:cd00009    1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 286 ---LVRLLFEMARFYAPTTIFIDEIDSIcsrrgtsdeheaSRRVKSELLIQMDGVggaLENDDPSKMVMVLAATNFPW-- 360
Cdd:cd00009   69 ghfLVRLLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLETL---NDLRIDRENVRVIGATNRPLlg 133

                        170
                 ....*....|....*...
gi 568939006 361 DIDEALRRRLEKRIYIPL 378
Cdd:cd00009  134 DLDRALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 240-376 1.44e-17

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: 80.23  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 240 KGVLMVGPPGTGKTMLAKAVAtecgtTFFN------VSSSTLTSKYRGESEKLVRLLFEMA----RFYAPTT----IFID 305
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIG-----KMLNarepkiVNGPEILNKYVGESEANIRKLFADAeeeqRRLGANSglhiIIFD 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939006 306 EIDSICSRRGTS-DEHEASRRVKSELLIQMDGVgGALENddpskmVMVLAATNFPWDIDEALRR--RLEKRIYI 376
Cdd:cd19504  111 EIDAICKQRGSMaGSTGVHDTVVNQLLSKIDGV-EQLNN------ILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 238-380 3.60e-17

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: 78.18  E-value: 3.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006   238 PWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYAPT 300
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006   301 TIFIDEIDSICsrrgtsdeheasrRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 379
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147


                   .
gi 568939006   380 T 380
Cdd:smart00382 148 L 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 207-334 2.13e-16

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: 76.64  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 207 DIADLEEAKKLL--REAVVLPmwmPDFFKGIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19507    1 DVGGLDNLKDWLkkRKAAFSK---QASAYGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568939006 285 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQM 334
Cdd:cd19507   77 SRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWL 126
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 240-374 3.74e-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: 67.17  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 240 KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGES--EKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTS 317
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568939006 318 DEHEAS-RRVKSELliqmdgvGGALENDDPSKMVMVLAATNFPWDIDEALRRRLEKRI 374
Cdd:cd19506  107 TEKQLDpKRLKKDL-------PKILKSLKPEDRVLIVGTTSRPFEADLKSFCKVYNKI 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 400-444 5.72e-13

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 62.94  E-value: 5.72e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568939006  400 DVHLEDIADKTEGYSGADITNICRDASLMAMRRRINGLSPEEIRA 444
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
ycf46 CHL00195
Ycf46; Provisional
 240-418 3.24e-12

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 68.51  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 240 KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDE 319
Cdd:CHL00195 260 RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGD 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 320 HEASRRVKSELLIQMDgvggalENDDPskmVMVLA-ATNFPWDIDEALRR-RLEKRIYIPLPTAKGRAELLKISLREVEL 397
Cdd:CHL00195 340 SGTTNRVLATFITWLS------EKKSP---VFVVAtANNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKFRP 410

                        170       180
                 ....*....|....*....|...
gi 568939006 398 DP--DVHLEDIADKTEGYSGADI 418
Cdd:CHL00195 411 KSwkKYDIKKLSKLSNKFSGAEI 433
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 242-376 7.76e-11

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: 61.31  E-value: 7.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 242 VLMVGPPGTGKTMLAKAVATECG---------TTFFNVSSSTLTSKYRGESEKLVRLLF----EMARFY-APTTIFIDEI 307
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKdALVFVLIDEV 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939006 308 DSICSRRGTS---DEHEASRRVKSELLIQMDgvggALENDDPskmVMVLAATNFPWDIDEALRRRLEKRIYI 376
Cdd:cd19508  135 ESLAAARSASssgTEPSDAIRVVNAVLTQID----RIKRYHN---NVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 229-376 4.14e-09

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: 55.44  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 229 PDFFKGIRRPWK-GVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTltskyRGESEKLVRLLfeMARFYAPTTIFIDEI 307
Cdd:cd19510   12 EDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDI 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939006 308 D-SICSRRGTSDEHEA----SRRVKSELLIQMDGVGGALENddpskmvMVLAATNFPWDIDEALRR--RLEKRIYI 376
Cdd:cd19510   85 DaAFESREHNKKNPSAygglSRVTFSGLLNALDGVASSEER-------IVFMTTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 236-374 7.74e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 54.45  E-value: 7.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 236 RRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEmarfYAPTT-----IFIDEIDSI 310
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFD----WANTSrrgllLFVDEADAF 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939006 311 CSRRGTSDEHEASRRVKSELLIQMdgvggalenDDPSKMVMVLAATNFPWDIDEALRRRLEKRI 374
Cdd:cd19512   94 LRKRSTEKISEDLRAALNAFLYRT---------GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 240-331 4.81e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 52.77  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 240 KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTS-KYRG-ESEKLVRLLFEmarfyapTTIFIDEIDSICSRRGTS 317
Cdd:cd19498   47 KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGSS 119

                         90
                 ....*....|....*
gi 568939006 318 DeHEASRR-VKSELL 331
Cdd:cd19498  120 G-PDVSREgVQRDLL 133
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 448-486 4.76e-07

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: 46.72  E-value: 4.76e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568939006  448 EELQMP-VTRGDLELALKKIAKSVSAADLEKYEKWMVEFG 486
Cdd:pfam09336  22 DKLLEPpVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 242-408 5.88e-07

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: 50.94  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 242 VLMVGPPGTGKTMLAKAVATECGTTFFNVS-SSTL-------TSKYRGESEKLV---RLLFEmarfyapTTIFIDEIDsi 310
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQfTPDLlpsdilgTYIYDQQTGEFEfrpGPLFA-------NVLLADEIN-- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 311 csRrgtsdeheASRRVKSELL-------IQMDGVGGALEnddpsKMVMVLAATNfPWDID------EALRRRLEKRIYIP 377
Cdd:COG0714  105 --R--------APPKTQSALLeameerqVTIPGGTYKLP-----EPFLVIATQN-PIEQEgtyplpEAQLDRFLLKLYIG 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568939006 378 LPTakgRAELLKI-----SLREVELDPDVHLEDIAD 408
Cdd:COG0714  169 YPD---AEEEREIlrrhtGRHLAEVEPVLSPEELLA 201
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
240-290 1.34e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 50.74  E-value: 1.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568939006 240 KGVLMVGPPGTGKTMLAKAVATECG--TTFFNVSSSTLTSKYRGESEKLVRLL 290
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEIYSAELKKTEFLMQAL 117
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 243-410 1.67e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 50.61  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  243 LMVGPPGTGKTMLAKAVATE-CGTTFF------NVSSSTLTSKYRGESEKLVRLLFEMArfyAPTTIFIDEIDSICSRR- 314
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLGVLrkplvrEVSRADLIGQYIGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGy 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  315 GTSDEHEASrrVKSELLIQMDG------VGGALENDDPSKMVmvlaatnfpwDIDEALRRRLEKRIYIPLPTAkgrAELL 388
Cdd:TIGR03922 393 GQKDPFGLE--AIDTLLARMENdrdrlvVIGAGYRKDLDKFL----------EVNEGLRSRFTRVIEFPSYSP---DELV 457

                         170       180
                  ....*....|....*....|..
gi 568939006  389 KISLREVELDPDVhLEDIADKT 410
Cdd:TIGR03922 458 EIARRMATERDSV-LDDAAADA 478
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 238-366 4.82e-06

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 46.60  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 238 PWKGVLMVGPPGTGKTMLAKAVATEC--------------GTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 303
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPCIIW 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939006 304 IDEIDSICSRRGTSDEHEASrrvKSELLIQMDGVGGALENDDPSKMVmVLAATNFPWDIDEAL 366
Cdd:cd19505   91 IPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTRNIL-VIASTHIPQKVDPAL 149
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 212-310 9.33e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 47.21  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 212 EEAKKLLREAVVlpmwmpDFFKGIRRPWKG-----------VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLT-SKY 279
Cdd:cd19497   18 ERAKKVLSVAVY------NHYKRIRNNLKQkdddveleksnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568939006 280 RGESEK--LVRLL----FEMARfyAPTTI-FIDEIDSI 310
Cdd:cd19497   92 VGEDVEniLLKLLqaadYDVER--AQRGIvYIDEIDKI 127
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 246-307 4.01e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 45.82  E-value: 4.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939006 246 GPPGTGKTMLAKAVATECGTTFFNVsSSTLTSKyrgeseKLVRLLFEMARFYA----PTTIFIDEI 307
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFVAL-SAVTSGV------KDIREVIEEARERRaygrRTILFVDEI 114
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 242-261 4.23e-05

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: 45.80  E-value: 4.23e-05
                         10        20
                 ....*....|....*....|
gi 568939006 242 VLMVGPPGTGKTMLAKAVAT 261
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 246-307 4.58e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 45.85  E-value: 4.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939006 246 GPPGTGKTMLAKAVATECGTTFFNVsSSTLTSKyrgeseKLVRLLFEMA---RFYAPTTI-FIDEI 307
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEAL-SAVTSGV------KDLREVIEEArqrRSAGRRTIlFIDEI 101
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 242-312 6.67e-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: 43.34  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  242 VLMVGPPGTGKTMLAKAVA-----TECGTTFFNVSS---STLTSKYRGESEKLVR-----LLFEMARFYAPTTIFIDEID 308
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgDERALIRIDMSEymeEHSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85


                  ....
gi 568939006  309 SICS 312
Cdd:pfam07724  86 KAHP 89
PRK04195 PRK04195
replication factor C large subunit; Provisional
 206-262 1.27e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.53  E-value: 1.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939006 206 DDIADLEEAKKLLREavvlpmWMPDFFKGirRPWKGVLMVGPPGTGKTMLAKAVATE 262
Cdd:PRK04195  14 SDVVGNEKAKEQLRE------WIESWLKG--KPKKALLLYGPPGVGKTSLAHALAND 62
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 242-261 1.36e-04

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: 42.91  E-value: 1.36e-04
                          10        20
                  ....*....|....*....|
gi 568939006  242 VLMVGPPGTGKTMLAKAVAT 261
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 240-285 1.37e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 43.84  E-value: 1.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568939006  240 KGVLMVGPPGTGKTMLAKAVATECG--TTFFNVSSSTLtskYRGESEK 285
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV---YSLEMKK 95
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 241-370 3.33e-04

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: 40.74  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006  241 GVLMVGPPGTGKTMLAK--AVATECGTTFF-----NVSSSTLTSKYR---GESEKLVRLLFEMARfyAPTTIFIDEIDsi 310
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNidpGGASWVDGPLVRAAR--EGEIAVLDEIN-- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939006  311 csrrgtsdehEASRRVKSEL--------LIQMDGVGgalENDDPSKMVMVLAATNFP----WDIDEALRRRL 370
Cdd:pfam07728  77 ----------RANPDVLNSLlsllderrLLLPDGGE---LVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
242-315 4.14e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.45  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 242 VLMVGPPGTGKTMLAKAVAtecgtTFFNV-----SSSTLT-SKYRGES-EK-LVRLL----FEMARfyAPTTI-FIDEID 308
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLA-----RILDVpfaiaDATTLTeAGYVGEDvENiLLKLLqaadYDVEK--AQRGIvYIDEID 183


                 ....*..
gi 568939006 309 SIcSRRG 315
Cdd:PRK05342 184 KI-ARKS 189
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 243-271 7.54e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 40.62  E-value: 7.54e-04
                         10        20
                 ....*....|....*....|....*....
gi 568939006 243 LMVGPPGTGKTMLAKAVATECGTTFFNVS 271
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRIS 69
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 242-315 1.32e-03

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 41.19  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939006 242 VLMVGPPGTGKTMLAK----------AVA-----TECGttffnvssstltskYRGES-EK-LVRLL----FEMARfyAPT 300
Cdd:COG1219  112 ILLIGPTGSGKTLLAQtlarildvpfAIAdattlTEAG--------------YVGEDvENiLLKLLqaadYDVEK--AER 175

                         90
                 ....*....|....*.
gi 568939006 301 TI-FIDEIDSIcSRRG 315
Cdd:COG1219  176 GIiYIDEIDKI-ARKS 190
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 242-307 1.99e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 38.63  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939006 242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYAPTTIFIDEI 307
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINVNLElsrrllELPEKQR--ALRAPRLLDEIAEKSSGDVVLLDNI 88
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
242-307 2.10e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 2.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939006 242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLtskyrgesEK---LVRLLfemarfyapTTI------FIDEI 307
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL--------EKpgdLAAIL---------TNLeegdvlFIDEI 111
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
240-263 3.64e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 3.64e-03
                         10        20
                 ....*....|....*....|....
gi 568939006 240 KGVLMVGPPGTGKTMLAKAVATEC 263
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEA 123
 
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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