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Conserved domains on  [gi|60390225|sp|Q9WV86|]
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RecName: Full=Katanin p60 ATPase-containing subunit A1; Short=Katanin p60 subunit A1; AltName: Full=Lipotransin; AltName: Full=p60 katanin

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 ...
 210-379 1.51e-128

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: 370.47  E-value: 1.51e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 60390225 370 RRRLEKRIYI 379
Cdd:cd19522 161 RRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 61-469 1.02e-71

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: 232.88  E-value: 1.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  61 VEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPS 140
Cdd:COG0464  18 LDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGEL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 141 PQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERdiisqnpnvRWYDIADLVEAKKL 220
Cdd:COG0464  98 LLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA---------ILDDLGGLEEVKEE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 221 LQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMAR 298
Cdd:COG0464 169 LRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKAR 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 299 FYSPATIFIDEIDSICSRRGTSEEHeASRRMKAELLVQMDGVggaseNDDpskmVMVLAATNFPWDIDEALRRRLEKRIY 378
Cdd:COG0464 248 GLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVVIAATNRPDLLDPALLRRFDEIIF 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 379 IPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRrriegltpeeirnlsreAMHMPTT 458
Cdd:COG0464 318 FPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR-----------------LGREPVT 380

                       410
                ....*....|.
gi 60390225 459 MEDFEMALKKI 469
Cdd:COG0464 381 TEDLLEALERE 391
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 4-72 2.57e-34

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: 123.07  E-value: 2.57e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390225   4 QMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKT 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 ...
 456-489 2.32e-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: 47.49  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 60390225   456 PTTMEDFEMALKKISKSVSAADIERYEKWIVEFG 489
Cdd:pfam09336  28 PVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 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 ...
 210-379 1.51e-128

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: 370.47  E-value: 1.51e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 60390225 370 RRRLEKRIYI 379
Cdd:cd19522 161 RRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 150-472 2.43e-94

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 288.83  E-value: 2.43e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 150 KAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERdiisqnPNVRWYDIADLVEAKKLLQEAVVLPM 229
Cdd:COG1222  25 LGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAES------PDVTFDDIGGLDEQIEEIREAVELPL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 230 WMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFI 307
Cdd:COG1222  99 KNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFI 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 308 DEIDSICSRRGTSEEHEASRRMKAELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAK 385
Cdd:COG1222 178 DEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEE 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 386 GREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLtpeeirnlsreamhmptTMEDFEMA 465
Cdd:COG1222 251 AREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV-----------------TMEDLEKA 313


                ....*..
gi 60390225 466 LKKISKS 472
Cdd:COG1222 314 IEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 189-489 1.42e-77

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: 257.14  E-value: 1.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   189 KDLVEALE-------RDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLA 259
Cdd:TIGR01243 426 KDFMEALKmvepsaiREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   260 KAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDG 339
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   340 VggasendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYS 417
Cdd:TIGR01243 585 I-------QELSNVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390225   418 GADITNVCRDASLMAMRRRIEGLTPEEIRNLSREAMH-MPTTMEDFEMALKKISKSVSAADIERYEKWIVEFG 489
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 204-471 2.22e-76

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 244.74  E-value: 2.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  204 PNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSK 281
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  282 YRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRMkAELLVQMDGVggasendDPSKMVMVLAA 358
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-------DPRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  359 TNFPwDI-DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRR 435
Cdd:PRK03992 277 TNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 60390225  436 RiegltpeeirnlsREAMhmptTMEDFEMALKKISK 471
Cdd:PRK03992 356 D-------------RTEV----TMEDFLKAIEKVMG 374
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 61-469 1.02e-71

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: 232.88  E-value: 1.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  61 VEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPS 140
Cdd:COG0464  18 LDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGEL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 141 PQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERdiisqnpnvRWYDIADLVEAKKL 220
Cdd:COG0464  98 LLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA---------ILDDLGGLEEVKEE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 221 LQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMAR 298
Cdd:COG0464 169 LRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKAR 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 299 FYSPATIFIDEIDSICSRRGTSEEHeASRRMKAELLVQMDGVggaseNDDpskmVMVLAATNFPWDIDEALRRRLEKRIY 378
Cdd:COG0464 248 GLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVVIAATNRPDLLDPALLRRFDEIIF 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 379 IPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRrriegltpeeirnlsreAMHMPTT 458
Cdd:COG0464 318 FPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR-----------------LGREPVT 380

                       410
                ....*....|.
gi 60390225 459 MEDFEMALKKI 469
Cdd:COG0464 381 TEDLLEALERE 391
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 245-381 2.29e-53

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: 175.86  E-value: 2.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHE 324
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG-GDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 60390225   325 ASRRMKAELLVQMDGVGGASENddpskmVMVLAATNFPWDIDEALRRRLEKRIYIPL 381
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSK------VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 4-72 2.57e-34

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: 123.07  E-value: 2.57e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390225   4 QMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKT 72
Cdd:cd21748   1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 241-382 7.97e-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: 77.41  E-value: 7.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225    241 PWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYSPA 303
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225    304 TIFIDEIDSICsrrgtseeheasrRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 382
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 403-447 4.87e-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: 63.33  E-value: 4.87e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 60390225   403 DVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRN 447
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 456-489 2.32e-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: 47.49  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 60390225   456 PTTMEDFEMALKKISKSVSAADIERYEKWIVEFG 489
Cdd:pfam09336  28 PVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 245-310 7.51e-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: 37.09  E-value: 7.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390225  245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYSPATIFIDEI 310
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 ...
 210-379 1.51e-128

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: 370.47  E-value: 1.51e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 60390225 370 RRRLEKRIYI 379
Cdd:cd19522 161 RRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 150-472 2.43e-94

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 288.83  E-value: 2.43e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 150 KAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERdiisqnPNVRWYDIADLVEAKKLLQEAVVLPM 229
Cdd:COG1222  25 LGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAES------PDVTFDDIGGLDEQIEEIREAVELPL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 230 WMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFI 307
Cdd:COG1222  99 KNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFI 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 308 DEIDSICSRRGTSEEHEASRRMKAELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAK 385
Cdd:COG1222 178 DEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEE 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 386 GREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLtpeeirnlsreamhmptTMEDFEMA 465
Cdd:COG1222 251 AREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV-----------------TMEDLEKA 313


                ....*..
gi 60390225 466 LKKISKS 472
Cdd:COG1222 314 IEKVKKK 320
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 211-379 1.95e-93

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: 280.39  E-value: 1.95e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 211 IADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLV 290
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 291 RLLFEMARFYSPATIFIDEIDSICSRRGtSEEHEASRRMKAELLVQMDGVGgasenDDPSKMVMVLAATNFPWDIDEALR 370
Cdd:cd19509  81 RALFALARELQPSIIFIDEIDSLLSERG-SGEHEASRRVKTEFLVQMDGVL-----NKPEDRVLVLGATNRPWELDEAFL 154


                ....*....
gi 60390225 371 RRLEKRIYI 379
Cdd:cd19509 155 RRFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 204-379 2.37e-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: 242.07  E-value: 2.37e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 204 PNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYR 283
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 284 GESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEhEASRRMKAELLVQMDGVGGASENddpskmVMVLAATNFPW 363
Cdd:cd19521  82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGES-EASRRIKTELLVQMNGVGNDSQG------VLVLGATNIPW 154

                       170
                ....*....|....*.
gi 60390225 364 DIDEALRRRLEKRIYI 379
Cdd:cd19521 155 QLDSAIRRRFEKRIYI 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 189-489 1.42e-77

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: 257.14  E-value: 1.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   189 KDLVEALE-------RDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLA 259
Cdd:TIGR01243 426 KDFMEALKmvepsaiREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   260 KAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDG 339
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   340 VggasendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYS 417
Cdd:TIGR01243 585 I-------QELSNVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390225   418 GADITNVCRDASLMAMRRRIEGLTPEEIRNLSREAMH-MPTTMEDFEMALKKISKSVSAADIERYEKWIVEFG 489
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 204-471 2.22e-76

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 244.74  E-value: 2.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  204 PNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSK 281
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  282 YRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRMkAELLVQMDGVggasendDPSKMVMVLAA 358
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-------DPRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  359 TNFPwDI-DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRR 435
Cdd:PRK03992 277 TNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 60390225  436 RiegltpeeirnlsREAMhmptTMEDFEMALKKISK 471
Cdd:PRK03992 356 D-------------RTEV----TMEDFLKAIEKVMG 374
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 188-379 1.29e-73

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: 230.65  E-value: 1.29e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 188 DKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECK 267
Cdd:cd19525   1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 268 TTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRMKAELLVQMDGVGGASENd 347
Cdd:cd19525  81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-EHESSRRIKTEFLVQLDGATTSSED- 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 60390225 348 dpskMVMVLAATNFPWDIDEALRRRLEKRIYI 379
Cdd:cd19525 159 ----RILVVGATNRPQEIDEAARRRLVKRLYI 186
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 61-469 1.02e-71

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: 232.88  E-value: 1.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  61 VEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPS 140
Cdd:COG0464  18 LDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGEL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 141 PQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERdiisqnpnvRWYDIADLVEAKKL 220
Cdd:COG0464  98 LLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA---------ILDDLGGLEEVKEE 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 221 LQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMAR 298
Cdd:COG0464 169 LRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKAR 247

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 299 FYSPATIFIDEIDSICSRRGTSEEHeASRRMKAELLVQMDGVggaseNDDpskmVMVLAATNFPWDIDEALRRRLEKRIY 378
Cdd:COG0464 248 GLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVVIAATNRPDLLDPALLRRFDEIIF 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 379 IPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRrriegltpeeirnlsreAMHMPTT 458
Cdd:COG0464 318 FPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR-----------------LGREPVT 380

                       410
                ....*....|.
gi 60390225 459 MEDFEMALKKI 469
Cdd:COG0464 381 TEDLLEALERE 391
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 210-379 5.10e-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: 205.08  E-value: 5.10e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRMKAELLVQMDGVGGasendDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSEG-EHEASRRLKTEFLIEFDGVQS-----NGDDRVLVMGATNRPQELDDAV 154

                       170
                ....*....|
gi 60390225 370 RRRLEKRIYI 379
Cdd:cd19524 155 LRRFTKRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 193-472 8.15e-60

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: 209.38  E-value: 8.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   193 EALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTF 270
Cdd:TIGR01243 162 KPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAGAYF 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   271 FNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRgtsEE--HEASRRMKAELLVQMDGVGGASEndd 348
Cdd:TIGR01243 241 ISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR---EEvtGEVEKRVVAQLLTLMDGLKGRGR--- 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   349 pskmVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCR 426
Cdd:TIGR01243 315 ----VIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAK 390

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 60390225   427 DASLMAMRRRI-EGLTPEEIRNLSREAM-HMPTTMEDFEMALKKISKS 472
Cdd:TIGR01243 391 EAAMAALRRFIrEGKINFEAEEIPAEVLkELKVTMKDFMEALKMVEPS 438
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 245-381 2.29e-53

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: 175.86  E-value: 2.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHE 324
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG-GDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 60390225   325 ASRRMKAELLVQMDGVGGASENddpskmVMVLAATNFPWDIDEALRRRLEKRIYIPL 381
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSK------VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 217-379 2.47e-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: 176.71  E-value: 2.47e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 217 AKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLF 294
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 295 EMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGgasenddPSKMVMVLAATNFPWDIDEALRR--R 372
Cdd:cd19511  80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIE-------SLKGVVVIAATNRPDMIDPALLRpgR 152


                ....*..
gi 60390225 373 LEKRIYI 379
Cdd:cd19511 153 LDKLIYV 159
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 210-379 6.41e-52

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: 173.38  E-value: 6.41e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIR--RPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRgTSEEHEASRRMKAELLVQMDGVggaseNDDPSKMVMVLAATNFPWDIDE 367
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGL-----STDGNCRVIVMGATNRPQDLDE 154

                       170
                ....*....|..
gi 60390225 368 ALRRRLEKRIYI 379
Cdd:cd19520 155 AILRRMPKRFHI 166
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 210-379 2.09e-51

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: 172.09  E-value: 2.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRMKAELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 367
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERRVVAQLLTLMDGM-------SSRGKVVVIAATNRPDAIDP 151

                       170
                ....*....|....
gi 60390225 368 ALRR--RLEKRIYI 379
Cdd:cd19503 152 ALRRpgRFDREVEI 165
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
202-469 6.26e-51

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 182.16  E-value: 6.26e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 202 QNPNVRWYDIADLVEAKKLLQEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNV 273
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIV-------DFLKdpekftrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSI 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 274 SSSTLTSKY------RgeseklVRLLFEMARFYSPATIFIDEIDSICSRRGTS-----EEHE----AsrrmkaeLLVQMD 338
Cdd:COG0465 207 SGSDFVEMFvgvgasR------VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghDEREqtlnQ-------LLVEMD 273

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 339 GVGGaSENddpskmVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEG 415
Cdd:COG0465 274 GFEG-NEG------VIVIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPG 345

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 60390225 416 YSGADITNVCRDASLMAMRRRiegltpeeirnlsREAMhmptTMEDFEMALKKI 469
Cdd:COG0465 346 FSGADLANLVNEAALLAARRN-------------KKAV----TMEDFEEAIDRV 382
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
243-480 1.37e-49

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 170.06  E-value: 1.37e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARfYSPATIFIDEIDSICSRRGTSEE 322
Cdd:COG1223  36 RKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQND 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 323 HEASRRMKAELLVQMDGvggasendDPSKmVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELAD 402
Cdd:COG1223 115 VGEVKRVVNALLQELDG--------LPSG-SVVIAATNHPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF 185

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390225 403 DVNLASIAENMEGYSGADITNVCRDaslmAMRRRI-EGltPEEIrnlsreamhmptTMEDFEMALKKISKSVSAADIER 480
Cdd:COG1223 186 ELDLKKLAKKLEGLSGADIEKVLKT----ALKKAIlED--REKV------------TKEDLEEALKQRKERKKEPKKEG 246
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 217-379 2.82e-49

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: 166.30  E-value: 2.82e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 217 AKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEM 296
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 297 ARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASEnddpskmVMVLAATNFPWDIDEALRR--RLE 374
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSK-------VLVIAATNRPDLLDPALLRpgRFD 153


                ....*
gi 60390225 375 KRIYI 379
Cdd:cd19481 154 EVIEF 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 210-446 5.00e-49

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 174.19  E-value: 5.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  210 DIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:PTZ00361 184 DIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  288 KLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRMkAELLVQMDGVggasendDPSKMVMVLAATNFPWD 364
Cdd:PTZ00361 263 KLVRELFRVAEENAPSIVFIDEIDAIGTKRydaTSGGEKEIQRTM-LELLNQLDGF-------DSRGDVKVIMATNRIES 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  365 IDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTP 442
Cdd:PTZ00361 335 LDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQ 414


                 ....
gi 60390225  443 EEIR 446
Cdd:PTZ00361 415 ADFR 418
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 210-377 1.47e-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: 164.82  E-value: 1.47e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19502   4 DIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEGA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 288 KLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRMkAELLVQMDGVggasendDPSKMVMVLAATNFPWD 364
Cdd:cd19502  83 RLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTM-LELLNQLDGF-------DPRGNIKVIMATNRPDI 154

                       170
                ....*....|....*
gi 60390225 365 IDEALRR--RLEKRI 377
Cdd:cd19502 155 LDPALLRpgRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 200-463 1.06e-47

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 169.56  E-value: 1.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  200 ISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSST 277
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEqiGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  278 LTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEAsRRMKAELLVQMDGVggasendDPSKMVM 354
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGADREV-QRILLELLNQMDGF-------DQTTNVK 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  355 VLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMA 432
Cdd:PTZ00454 287 VIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQA 366

                        250       260       270
                 ....*....|....*....|....*....|.
gi 60390225  433 MRRRIEGLTPEEIRNLSREamHMPTTMEDFE 463
Cdd:PTZ00454 367 VRKNRYVILPKDFEKGYKT--VVRKTDRDYD 395
ftsH CHL00176
cell division protein; Validated
 210-445 1.83e-45

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 168.30  E-value: 1.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  210 DIADLVEAKKLLQEAVVLpMWMPEFFKGI-RRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEK 288
Cdd:CHL00176 184 DIAGIEEAKEEFEEVVSF-LKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  289 LVRLLFEMARFYSPATIFIDEIDSICSRRGT--SEEHEASRRMKAELLVQMDGVggaSENDDpskmVMVLAATNFPWDID 366
Cdd:CHL00176 263 RVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDEREQTLNQLLTEMDGF---KGNKG----VIVIAATNRVDILD 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  367 EALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEE 444
Cdd:CHL00176 336 AALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKE 415


                 .
gi 60390225  445 I 445
Cdd:CHL00176 416 I 416
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 217-379 1.69e-43

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 151.11  E-value: 1.69e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 217 AKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLF 294
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 295 EMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEALRR--R 372
Cdd:cd19529  80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-------EEMNGVVVIAATNRPDIIDPALLRagR 152


                ....*..
gi 60390225 373 LEKRIYI 379
Cdd:cd19529 153 FDRLIYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
210-437 4.73e-43

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 161.74  E-value: 4.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  210 DIADLVEAKKLLQEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  288 KLVRLLFEMARFYSPATIFIDEIDSICSRRGT--SEEHEASRRMKAELLVQMDGVGGasenddpSKMVMVLAATNFPWDI 365
Cdd:PRK10733 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEG-------NEGIIVIAATNRPDVL 303

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390225  366 DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMR--RRI 437
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 ...
 210-380 1.18e-41

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: 146.43  E-value: 1.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKaiGIKPP-RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRMKAELLVQMDGVGGASEnddpskmVMVLAATNFPWDIDE 367
Cdd:cd19519  80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT-HGEVERRIVSQLLTLMDGLKQRAH-------VIVMAATNRPNSIDP 151

                       170
                ....*....|....*
gi 60390225 368 ALRR--RLEKRIYIP 380
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 ...
 218-379 1.21e-40

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 143.42  E-value: 1.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 218 KKLLQEAVVLPMWMPE-FFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEM 296
Cdd:cd19528   2 KRELQELVQYPVEHPDkFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 297 ARFYSPATIFIDEIDSICSRRGTS--EEHEASRRMKAELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEALRR--R 372
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNigDAGGAADRVINQILTEMDGM-------NTKKNVFIIGATNRPDIIDPAILRpgR 154


                ....*..
gi 60390225 373 LEKRIYI 379
Cdd:cd19528 155 LDQLIYI 161
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 206-379 2.13e-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: 143.14  E-value: 2.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 206 VRWYDIADLVEAKKLLQEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSST 277
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVV-------EFLKnpekftklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 278 LTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGT--SEEHEASRRMKAELLVQMDGVGGasenddpSKMVMV 355
Cdd:cd19501  73 FVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglGGGHDEREQTLNQLLVEMDGFES-------NTGVIV 145

                       170       180
                ....*....|....*....|....*.
gi 60390225 356 LAATNFPWDIDEALRR--RLEKRIYI 379
Cdd:cd19501 146 IAATNRPDVLDPALLRpgRFDRQVYV 171
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 210-379 2.46e-39

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: 140.02  E-value: 2.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 290 VRLLFEMARFYSPATIFIDEIDSICSRRgtSEEHEASRRMKAELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 369
Cdd:cd19523  81 LQASFLAARCRQPSVLFISDLDALLSSQ--DDEASPVGRLQVELLAQLDGVLGSGEDG-----VLVVCTTSKPEEIDESL 153

                       170
                ....*....|
gi 60390225 370 RRRLEKRIYI 379
Cdd:cd19523 154 RRYFSKRLLV 163
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 214-379 3.26e-39

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 139.55  E-value: 3.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 214 LVEAKKLLQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVR 291
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 292 LLFEMARFYSPATIFIDEIDSICSRRGtSEEHEASRRMKAELLVQMDGVGGASEnddpskmVMVLAATNFPWDIDEALRR 371
Cdd:cd19530  80 QVFQRARASAPCVIFFDEVDALVPKRG-DGGSWASERVVNQLLTEMDGLEERSN-------VFVIAATNRPDIIDPAMLR 151

                       170
                ....*....|
gi 60390225 372 --RLEKRIYI 379
Cdd:cd19530 152 pgRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 221-377 3.08e-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: 129.06  E-value: 3.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 221 LQEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMAR 298
Cdd:cd19518  12 LCELLIHPILPPEYFQhlGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEKIRELFDQAI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 299 FYSPATIFIDEIDSICSRRGTSEEhEASRRMKAELLVQMDGVGGASENDDPskmVMVLAATNFPWDIDEALRR--RLEKR 376
Cdd:cd19518  91 SNAPCIVFIDEIDAITPKRESAQR-EMERRIVSQLLTCMDELNNEKTAGGP---VLVIGATNRPDSLDPALRRagRFDRE 166


                .
gi 60390225 377 I 377
Cdd:cd19518 167 I 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 218-379 1.57e-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: 126.86  E-value: 1.57e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 218 KKLLQEAVVLPMWMPEFF-KGIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEM 296
Cdd:cd19527   2 KKEILDTIQLPLEHPELFsSGLRKR-SGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 297 ARFYSPATIFIDEIDSICSRRGTS-EEHEASRRMKAELLVQMDGVGGASENddpskmVMVLAATNFPWDIDEALRR--RL 373
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMSSSGQD------VFVIGATNRPDLLDPALLRpgRF 154


                ....*.
gi 60390225 374 EKRIYI 379
Cdd:cd19527 155 DKLLYL 160
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 4-72 2.57e-34

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: 123.07  E-value: 2.57e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390225   4 QMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKT 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 ...
 217-378 3.80e-34

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: 126.00  E-value: 3.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 217 AKKLLQEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFE 295
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPlRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 296 MARFYSPATIFIDEIDSICSRRGtseeHEAS---RRMKAELLVQMDGVGGAsenddpsKMVMVLAATNFPWDIDEALRR- 371
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRG----HDSTgvtDRVVNQLLTQLDGVEGL-------DGVYVLAATSRPDLIDPALLRp 149


                ....*...
gi 60390225 372 -RLEKRIY 378
Cdd:cd19526 150 gRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 210-378 8.33e-33

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: 122.62  E-value: 8.33e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 210 DIADLVEAKKLLQEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATEC-----KTTFFNVSSSTLTSKYR 283
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 284 GESEKLVRLLFEMARFYSPATIFIDEIDSICSRRgTSEEHEASRRMKAELLVQMDGVGGASEnddpskmVMVLAATNFPW 363
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-SSKQEQIHASIVSTLLALMDGLDNRGQ-------VVVIGATNRPD 152

                       170
                ....*....|....*..
gi 60390225 364 DIDEALRR--RLEKRIY 378
Cdd:cd19517 153 ALDPALRRpgRFDREFY 169
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 239-381 4.63e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 100.68  E-value: 4.63e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 239 RRPWKGVLMVGPPGTGKTLLAKAVATEC---KTTFFNVSSSTLTSKYRGESEK---LVRLLFEMARFYSPATIFIDEIDS 312
Cdd:cd00009  16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390225 313 IcsrrgtseeheaSRRMKAELLVQMDGVggaSENDDPSKMVMVLAATNFPW--DIDEALRRRLEKRIYIPL 381
Cdd:cd00009  96 L------------SRGAQNALLRVLETL---NDLRIDRENVRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 243-379 1.24e-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: 80.61  E-value: 1.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 243 KGVLMVGPPGTGKTLLAKAV-----ATECKTtffnVSSSTLTSKYRGESEKLVRLLFEMA----RFYSPAT----IFIDE 309
Cdd:cd19504  36 KGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqRRLGANSglhiIIFDE 111

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390225 310 IDSICSRRGTSEEHEA-SRRMKAELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYI 379
Cdd:cd19504 112 IDAICKQRGSMAGSTGvHDTVVNQLLSKIDGV-------EQLNNILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 241-382 7.97e-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: 77.41  E-value: 7.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225    241 PWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYSPA 303
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225    304 TIFIDEIDSICsrrgtseeheasrRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 382
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 243-360 1.36e-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: 77.02  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEE 322
Cdd:cd19507  32 KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGD 111

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 60390225 323 HEASRRMKAELLVQMdgvggaSENDDPskmVMVLAATN 360
Cdd:cd19507 112 SGTSSRVLGTFLTWL------QEKKKP---VFVVATAN 140
ycf46 CHL00195
Ycf46; Provisional
 243-421 1.41e-13

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 72.74  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEE 322
Cdd:CHL00195 260 RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGD 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  323 HEASRRMKAELLVQMdgvggaSENDDPskmVMVLA-ATNFPWDIDEALRR-RLEKRIYIPLPSAKGREELLRISLREL-- 398
Cdd:CHL00195 340 SGTTNRVLATFITWL------SEKKSP---VFVVAtANNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKFrp 410

                        170       180
                 ....*....|....*....|...
gi 60390225  399 ELADDVNLASIAENMEGYSGADI 421
Cdd:CHL00195 411 KSWKKYDIKKLSKLSNKFSGAEI 433
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 403-447 4.87e-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: 63.33  E-value: 4.87e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 60390225   403 DVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRN 447
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 243-377 2.60e-11

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: 61.77  E-value: 2.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGES--EKLVRLLFEMARFYSPATIFIDEIDSICSRRGTS 320
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60390225 321 EEHEAS-RRMKAELLVQMdgvggasENDDPSKMVMVLAATNFPWDIDEALRRRLEKRI 377
Cdd:cd19506 107 TEKQLDpKRLKKDLPKIL-------KSLKPEDRVLIVGTTSRPFEADLKSFCKVYNKI 157
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 245-379 7.90e-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: 7.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 245 VLMVGPPGTGKTLLAKAVA---------TECKTTFFNVSSSTLTSKYRGESEKLVRLLF----EMARfYSPATIF--IDE 309
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELID-DKDALVFvlIDE 133

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390225 310 IDSICSRRGT----SEEHEASRRMKAeLLVQMDGVGGASENddpskmvMVLAATNFPWDIDEALRRRLEKRIYI 379
Cdd:cd19508 134 VESLAAARSAsssgTEPSDAIRVVNA-VLTQIDRIKRYHNN-------VILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 189-327 5.07e-09

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: 55.85  E-value: 5.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 189 KDLVEALERDIISQNpnvrwydiadlvEAKKLLqeAVVLP-----MWMPEFFKGIRRPwKGVLMVGPPGTGKTLLAKAVA 263
Cdd:cd19498   3 REIVSELDKYIIGQD------------EAKRAV--AIALRnrwrrMQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLA 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390225 264 TECKTTFFNVSSSTLTS-KYRG-ESEKLVRLLFEmarfyspATIFIDEIDSICSRRGTSeEHEASR 327
Cdd:cd19498  68 KLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGSS-GPDVSR 125
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 232-379 8.01e-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: 54.67  E-value: 8.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 232 PEFFKGIRRPWK-GVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTltskyRGESEKLVRLLfeMARFYSPATIFIDEI 310
Cdd:cd19510  12 EDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDI 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390225 311 D-SICSRRGTSEEHEASRRMKA----ELLVQMDGVGGASENddpskmvMVLAATNFPWDIDEALRR--RLEKRIYI 379
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 ...
 239-377 6.89e-08

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 51.76  E-value: 6.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 239 RRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRgESEKLVRLLFEMARFYSPATI-FIDEIDSICSRR 317
Cdd:cd19512  19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKR 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 318 GTSEEHEASRRMKAELLVQMdgvggasenDDPSKMVMVLAATNFPWDIDEALRRRLEKRI 377
Cdd:cd19512  98 STEKISEDLRAALNAFLYRT---------GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 241-369 8.20e-08

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 51.61  E-value: 8.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 241 PWKGVLMVGPPGTGKTLLAKAVATEC--------------KTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIF 306
Cdd:cd19505  11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPCIIW 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390225 307 IDEIDSICSRRGTsEEHEASRRMKAELLVQMdgVGGASENDDPSKMVmVLAATNFPWDIDEAL 369
Cdd:cd19505  91 IPNIHELNVNRST-QNLEEDPKLLLGLLLNY--LSRDFEKSSTRNIL-VIASTHIPQKVDPAL 149
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 456-489 2.32e-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: 47.49  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 60390225   456 PTTMEDFEMALKKISKSVSAADIERYEKWIVEFG 489
Cdd:pfam09336  28 PVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 245-313 3.55e-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: 48.37  E-value: 3.55e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390225 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLT-SKYRGESEK--LVRLL----FEMARfYSPATIFIDEIDSI 313
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDVEniLLKLLqaadYDVER-AQRGIVYIDEIDKI 127
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 246-414 7.45e-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: 48.30  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   246 LMVGPPGTGKTLLAKAVATE-C------KTTFFNVSSSTLTSKYRGESEKLVRLLFEMARfysPATIFIDEIDSICSRR- 317
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADLIGQYIGESEAKTNEIIDSAL---GGVLFLDEAYTLVETGy 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   318 GTSEEHEASrrMKAELLVQMDG------VGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEKRIYIPLPSAkgrEELL 391
Cdd:TIGR03922 393 GQKDPFGLE--AIDTLLARMENdrdrlvVIGAGYRKDLDKFL----------EVNEGLRSRFTRVIEFPSYSP---DELV 457

                         170       180
                  ....*....|....*....|...
gi 60390225   392 RISLRELELADDVNLASIAENME 414
Cdd:TIGR03922 458 EIARRMATERDSVLDDAAADALL 480
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
243-293 1.32e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.66  E-value: 1.32e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 60390225 243 KGVLMVGPPGTGKTLLAKAVATEC--KTTFFNVSSSTLTSKYRGESEKLVRLL 293
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYSAELKKTEFLMQAL 117
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
245-318 1.52e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 47.08  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLT-SKYRGES-EK-LVRLLfeMARFYSPAT-----IFIDEIDSIcSR 316
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEDvENiLLKLL--QAADYDVEKaqrgiVYIDEIDKI-AR 187


                 ..
gi 60390225  317 RG 318
Cdd:PRK05342 188 KS 189
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 249-310 2.46e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 46.59  E-value: 2.46e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390225 249 GPPGTGKTLLAKAVATECKTTFFNVsSSTLTSKyrgeseKLVRLLFE---MARFYSPATI-FIDEI 310
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVAL-SAVTSGV------KDIREVIEearERRAYGRRTIlFVDEI 114
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 245-315 3.54e-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: 44.11  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   245 VLMVGPPGTGKTLLAKAVA-----TECKTTFFNVSS---STLTSKYRGESEKLVR-----LLFEMARFYSPATIFIDEID 311
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgDERALIRIDMSEymeEHSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85


                  ....
gi 60390225   312 SICS 315
Cdd:pfam07724  86 KAHP 89
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 249-310 8.75e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 44.69  E-value: 8.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390225  249 GPPGTGKTLLAKAVATECKTTFFNVsSSTLTSKyrgeseKLVRLLFEMA---RFYSPATI-FIDEI 310
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEAL-SAVTSGV------KDLREVIEEArqrRSAGRRTIlFIDEI 101
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 244-373 1.10e-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: 42.28  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225   244 GVLMVGPPGTGKTLLAK--AVATECKTTFF-----NVSSSTLTSKYR---GESEKLVRLLFEMARfySPATIFIDEIDsi 313
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNidpGGASWVDGPLVRAAR--EGEIAVLDEIN-- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390225   314 csrRGTSE---------EHeasRRMkaellVQMDGVGgasENDDPSKMVMVLAATNFP----WDIDEALRRRL 373
Cdd:pfam07728  77 ---RANPDvlnsllsllDE---RRL-----LLPDGGE---LVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 245-318 1.64e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 43.88  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 245 VLMVGPPGTGKTLLAKAVAtecktTFFNV-----SSSTLT-SKYRGES-EK-LVRLL----FEMARfyspAT---IFIDE 309
Cdd:COG1219 112 ILLIGPTGSGKTLLAQTLA-----RILDVpfaiaDATTLTeAGYVGEDvENiLLKLLqaadYDVEK----AErgiIYIDE 182


                ....*....
gi 60390225 310 IDSIcSRRG 318
Cdd:COG1219 183 IDKI-ARKS 190
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 243-288 2.63e-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: 43.07  E-value: 2.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 60390225   243 KGVLMVGPPGTGKTLLAKAVATEC--KTTFFNVSSSTLtskYRGESEK 288
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEV---YSLEMKK 95
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 246-374 3.34e-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: 41.39  E-value: 3.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 246 LMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLtskyRGESE--------------KLVRLLFEmARFYSPaTIFIDEID 311
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGV----RDEAEirghrrtyvgampgRIIQALKK-AGTNNP-VFLLDEID 114

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390225 312 SI-CSRRGTSEeheasrrmkAELLVQMDGVGGASEND-------DPSKmVMVLAATNFPWDIDEALRRRLE 374
Cdd:cd19500 115 KIgSSFRGDPA---------SALLEVLDPEQNSTFSDhyldvpfDLSK-VLFIATANSLDTIPGPLLDRME 175
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 245-264 4.34e-04

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: 42.72  E-value: 4.34e-04
                        10        20
                ....*....|....*....|
gi 60390225 245 VLMVGPPGTGKTLLAKAVAT 264
Cdd:COG0606 214 LLMIGPPGSGKTMLARRLPG 233
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 245-393 6.90e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 41.69  E-value: 6.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVS-SSTL-------TSKYRGESEKLV---RLLFEmarfyspATIFIDEIDsi 313
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQfTPDLlpsdilgTYIYDQQTGEFEfrpGPLFA-------NVLLADEIN-- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225 314 csRrgtseeheASRRMKAELLVQMD----GVGGasENDDPSKMVMVLAATNfPWDID------EALRRRLEKRIYIPLPS 383
Cdd:COG0714 105 --R--------APPKTQSALLEAMEerqvTIPG--GTYKLPEPFLVIATQN-PIEQEgtyplpEAQLDRFLLKLYIGYPD 171

                       170
                ....*....|
gi 60390225 384 akgREELLRI 393
Cdd:COG0714 172 ---AEEEREI 178
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 245-264 1.15e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.21  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|
gi 60390225   245 VLMVGPPGTGKTLLAKAVAT 264
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
PRK04195 PRK04195
replication factor C large subunit; Provisional
 211-265 1.26e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.06  E-value: 1.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 60390225  211 IADLV---EAKKLLQEavvlpmWMPEFFKGirRPWKGVLMVGPPGTGKTLLAKAVATE 265
Cdd:PRK04195  13 LSDVVgneKAKEQLRE------WIESWLKG--KPKKALLLYGPPGVGKTSLAHALAND 62
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
243-274 2.01e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 2.01e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 60390225 243 KGVLMVGPPGTGKTLLAKAVATEC-----KTTFFNVS 274
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTAP 136
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 239-313 5.26e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.43  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  239 RRPWKGVLMVGPPGTGKTLLAKAVA------------TECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIF 306
Cdd:PRK11034 204 RRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILF 283


                 ....*..
gi 60390225  307 IDEIDSI 313
Cdd:PRK11034 284 IDEIHTI 290
44 PHA02544
clamp loader, small subunit; Provisional
 223-372 7.13e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.43  E-value: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  223 EAVVLPMWMPEFFKGIRRpwKG-----VLMVGPPGTGKTLLAKAVATE--CKTTFFNVSSSTLtskyrgeseKLVRllFE 295
Cdd:PHA02544  21 DECILPAADKETFKSIVK--KGripnmLLHSPSPGTGKTTVAKALCNEvgAEVLFVNGSDCRI---------DFVR--NR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390225  296 MARFYSPAT-------IFIDEIDsicsRRGTSEEHEASRrmkaellvqmdgvgGASEndDPSKMVMVLAATNFPWDIDEA 368
Cdd:PHA02544  88 LTRFASTVSltgggkvIIIDEFD----RLGLADAQRHLR--------------SFME--AYSKNCSFIITANNKNGIIEP 147


                 ....
gi 60390225  369 LRRR 372
Cdd:PHA02544 148 LRSR 151
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 243-277 7.31e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 37.37  E-value: 7.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 60390225   243 KGVLMVGPPGTGKTLLAKAV-----ATECKTTFFNVSSST 277
Cdd:pfam12775  32 KPVLLVGPTGTGKTVIIQNLlrkldKEKYLPLFINFSAQT 71
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 245-310 7.51e-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: 37.09  E-value: 7.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390225  245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYSPATIFIDEI 310
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINVNLElsrrllELPEKQR--ALRAPRLLDEIAEKSSGDVVLLDNI 88
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
245-269 9.64e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.19  E-value: 9.64e-03
                         10        20
                 ....*....|....*....|....*....
gi 60390225  245 VLMVGPPGTGKTLLAKAVATE----CKTT 269
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEmgvnIRIT 82
 
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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