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Conserved domains on  [gi|257732100|emb|CBC87296|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
240-410 1.23e-122

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19522:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 170  Bit Score: 356.60  E-value: 1.23e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERM 319
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 320 VRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTATNEDgSRKIVMVLAATNFPWDIDEA 399
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDD-PSKMVMVLAATNFPWDIDEA 159
                        170
                 ....*....|.
gi 257732100 400 LRRRLEKRIYI 410
Cdd:cd19522  160 LRRRLEKRIYI 170
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
9-77 8.85e-28

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: 105.74  E-value: 8.85e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257732100   9 AGLQDHLKLAREYALEGSYDTSVIFFDGAIAQINKHLNTLDDPLARTKWMNVKKAIMEETEVVKQLDAE 77
Cdd:cd21748    1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
434-478 6.17e-11

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: 57.55  E-value: 6.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 257732100  434 DVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKIAGKTRDEIKN 478
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
479-521 2.28e-10

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: 56.35  E-value: 2.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 257732100  479 MSKDDISND-----PVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEFG 521
Cdd:pfam09336  14 MTWMDIPSDkllepPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 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 ...
240-410 1.23e-122

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: 356.60  E-value: 1.23e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERM 319
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 320 VRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTATNEDgSRKIVMVLAATNFPWDIDEA 399
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDD-PSKMVMVLAATNFPWDIDEA 159
                        170
                 ....*....|.
gi 257732100 400 LRRRLEKRIYI 410
Cdd:cd19522  160 LRRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
197-508 1.03e-92

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 285.75  E-value: 1.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 197 AESMNGDAEDGKSKRGLYEGPDEDLAAMLERDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKG 274
Cdd:COG1222   36 VKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHE 354
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 355 SSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVA 432
Cdd:COG1222  195 EVQRTVNQLLAELDGFE--------SRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLA 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257732100 433 SDVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKiagktRDEIknmskddisndpvAMCDFEEAIRKVQPSVSSS 508
Cdd:COG1222  267 DDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREG-----RDTV-------------TMEDLEKAIEKVKKKTETA 324
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
227-523 2.87e-80

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: 265.23  E-value: 2.87e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  227 RDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVS 304
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVR 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  305 SATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTatnedgsrKIV 384
Cdd:TIGR01243 520 GPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQEL--------SNV 591
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  385 MVLAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMN 462
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMA 671
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257732100  463 GMRRKIAGKTRDEIKNMSKDDISNDPVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEFGSA 523
Cdd:TIGR01243 672 ALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRL 732
cell_div_CdvC NF041006
cell division protein CdvC;
229-520 3.37e-69

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 226.54  E-value: 3.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 229 VLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFqgirrP--W-KGVLMFGPPGTGKTLLAKAVATECGTTFFNVSS 305
Cdd:NF041006  93 VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 306 ATLASKWRGESERMVRCLFDLARAYA-----PSTIFIDEIDSLCNSRggSGEHESSRRVKSELLVQVDGVsntatnEDGS 380
Cdd:NF041006 168 ASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVY--SSEVGGEVRVRNQFLKEMDGL------QDKS 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 381 RKI-VMVLAATNFPWDIDEALRRRLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDA 459
Cdd:NF041006 240 ENYhVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAA 319
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257732100 460 SMngmrrkiagKTrdeIKNMSKDDISND-PVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEF 520
Cdd:NF041006 320 HM---------RV---VKEMFEKGLGEPrPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
230-502 1.86e-68

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 225.10  E-value: 1.86e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 230 LDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSAT 307
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 308 LASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSR---GGSGEHESSRRVkSELLVQVDGVSNtatnedgsRKIV 384
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGFDP--------RGNV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 385 MVLAATNFPwDI-DEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASM 461
Cdd:PRK03992 272 KIIAATNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGM 350
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 257732100 462 NGMRRKiagktRDEIKnmskddisndpvaMCDFEEAIRKVQ 502
Cdd:PRK03992 351 FAIRDD-----RTEVT-------------MEDFLKAIEKVM 373
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
275-412 7.64e-51

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: 170.08  E-value: 7.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  275 VLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHE 354
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100  355 SSRRVKSELLVQVDGVSNTATNedgsrkiVMVLAATNFPWDIDEALRRRLEKRIYIPL 412
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSK-------VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
9-77 8.85e-28

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: 105.74  E-value: 8.85e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257732100   9 AGLQDHLKLAREYALEGSYDTSVIFFDGAIAQINKHLNTLDDPLARTKWMNVKKAIMEETEVVKQLDAE 77
Cdd:cd21748    1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
271-414 3.79e-16

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 75.49  E-value: 3.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100   271 PWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATL-----------------ASKWRGESERMVRCLFDLARAYAPS 333
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGedileevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100   334 TIFIDEIDSLCnsrggsgehessrRVKSELLVQVDGVSNTATNEDGSRKIVMVLAATNFPWDIDEALRRRLEKRIYIPLP 413
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147

                   .
gi 257732100   414 D 414
Cdd:smart00382 148 L 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
434-478 6.17e-11

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: 57.55  E-value: 6.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 257732100  434 DVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKIAGKTRDEIKN 478
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
479-521 2.28e-10

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: 56.35  E-value: 2.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 257732100  479 MSKDDISND-----PVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEFG 521
Cdd:pfam09336  14 MTWMDIPSDkllepPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 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 ...
240-410 1.23e-122

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: 356.60  E-value: 1.23e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERM 319
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 320 VRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTATNEDgSRKIVMVLAATNFPWDIDEA 399
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDD-PSKMVMVLAATNFPWDIDEA 159
                        170
                 ....*....|.
gi 257732100 400 LRRRLEKRIYI 410
Cdd:cd19522  160 LRRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
197-508 1.03e-92

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 285.75  E-value: 1.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 197 AESMNGDAEDGKSKRGLYEGPDEDLAAMLERDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKG 274
Cdd:COG1222   36 VKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHE 354
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 355 SSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVA 432
Cdd:COG1222  195 EVQRTVNQLLAELDGFE--------SRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLA 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257732100 433 SDVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKiagktRDEIknmskddisndpvAMCDFEEAIRKVQPSVSSS 508
Cdd:COG1222  267 DDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREG-----RDTV-------------TMEDLEKAIEKVKKKTETA 324
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
241-410 6.21e-88

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: 267.30  E-value: 6.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 241 VAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMV 320
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 321 RCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVSNTATNEdgsrkiVMVLAATNFPWDIDEAL 400
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSER-GSGEHEASRRVKTEFLVQMDGVLNKPEDR------VLVLGATNRPWELDEAF 153
                        170
                 ....*....|
gi 257732100 401 RRRLEKRIYI 410
Cdd:cd19509  154 LRRFEKRIYI 163
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
227-523 2.87e-80

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: 265.23  E-value: 2.87e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  227 RDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVS 304
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVR 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  305 SATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTatnedgsrKIV 384
Cdd:TIGR01243 520 GPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQEL--------SNV 591
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  385 MVLAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMN 462
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMA 671
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257732100  463 GMRRKIAGKTRDEIKNMSKDDISNDPVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEFGSA 523
Cdd:TIGR01243 672 ALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRL 732
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
234-410 5.84e-80

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: 247.08  E-value: 5.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 234 PGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWR 313
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 314 GESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVSNtatNEDGsrkiVMVLAATNFP 393
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR-GEGESEASRRIKTELLVQMNGVGN---DSQG----VLVLGATNIP 153
                        170
                 ....*....|....*..
gi 257732100 394 WDIDEALRRRLEKRIYI 410
Cdd:cd19521  154 WQLDSAIRRRFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
218-410 1.72e-74

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: 233.73  E-value: 1.72e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 218 DEDLAAMLERDVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECG 297
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 298 TTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVsNTATNE 377
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR-GEGEHESSRRIKTEFLVQLDGA-TTSSED 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 257732100 378 DgsrkiVMVLAATNFPWDIDEALRRRLEKRIYI 410
Cdd:cd19525  159 R-----ILVVGATNRPQEIDEAARRRLVKRLYI 186
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
228-502 5.17e-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: 232.11  E-value: 5.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 228 DVLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSS 305
Cdd:COG0464  146 EELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 306 ATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHeSSRRVKSELLVQVDGVSNTatnedgsrkiVM 385
Cdd:COG0464  225 SDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEELRSD----------VV 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 386 VLAATNFPWDIDEALRRRLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNGMR 465
Cdd:COG0464  294 VIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 257732100 466 rkiagktrdeiknmskddISNDPVAMCDFEEAIRKVQ 502
Cdd:COG0464  374 ------------------LGREPVTTEDLLEALERED 392
cell_div_CdvC NF041006
cell division protein CdvC;
229-520 3.37e-69

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 226.54  E-value: 3.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 229 VLDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFqgirrP--W-KGVLMFGPPGTGKTLLAKAVATECGTTFFNVSS 305
Cdd:NF041006  93 VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 306 ATLASKWRGESERMVRCLFDLARAYA-----PSTIFIDEIDSLCNSRggSGEHESSRRVKSELLVQVDGVsntatnEDGS 380
Cdd:NF041006 168 ASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVY--SSEVGGEVRVRNQFLKEMDGL------QDKS 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 381 RKI-VMVLAATNFPWDIDEALRRRLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDA 459
Cdd:NF041006 240 ENYhVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAA 319
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257732100 460 SMngmrrkiagKTrdeIKNMSKDDISND-PVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEF 520
Cdd:NF041006 320 HM---------RV---VKEMFEKGLGEPrPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
230-502 1.86e-68

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 225.10  E-value: 1.86e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 230 LDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSAT 307
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 308 LASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSR---GGSGEHESSRRVkSELLVQVDGVSNtatnedgsRKIV 384
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGFDP--------RGNV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 385 MVLAATNFPwDI-DEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASM 461
Cdd:PRK03992 272 KIIAATNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGM 350
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 257732100 462 NGMRRKiagktRDEIKnmskddisndpvaMCDFEEAIRKVQ 502
Cdd:PRK03992 351 FAIRDD-----RTEVT-------------MEDFLKAIEKVM 373
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
240-410 4.24e-62

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: 200.85  E-value: 4.24e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERM 319
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 320 VRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVSNtatnedGSRKIVMVLAATNFPWDIDEA 399
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSER-SEGEHEASRRLKTEFLIEFDGVQS------NGDDRVLVMGATNRPQELDDA 153
                        170
                 ....*....|.
gi 257732100 400 LRRRLEKRIYI 410
Cdd:cd19524  154 VLRRFTKRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
234-504 1.13e-58

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: 207.07  E-value: 1.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  234 PGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASK 311
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSK 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  312 WRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRG-GSGEHEssRRVKSELLVQVDGVSntatnedgSRKIVMVLAAT 390
Cdd:TIGR01243 252 YYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREeVTGEVE--KRVVAQLLTLMDGLK--------GRGRVIVIGAT 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  391 NFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKI 468
Cdd:TIGR01243 322 NRPDALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI 401
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 257732100  469 -AGKTRDEIKNMSKDDISNDPVAMCDFEEAIRKVQPS 504
Cdd:TIGR01243 402 rEGKINFEAEEIPAEVLKELKVTMKDFMEALKMVEPS 438
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
247-410 4.93e-54

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: 179.40  E-value: 4.93e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 247 AKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLF 324
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 325 DLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDIDEALRR-- 402
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIE--------SLKGVVVIAATNRPDMIDPALLRpg 151

                 ....*...
gi 257732100 403 RLEKRIYI 410
Cdd:cd19511  152 RLDKLIYV 159
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
207-514 1.48e-53

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 190.25  E-value: 1.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 207 GKSKrglyegpdedlAAMLErdvlDSTPGVRWDDVAGLSEAKRLLEEaVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTG 284
Cdd:COG0465  125 GKSK-----------AKLYD----EDKPKVTFDDVAGVDEAKEELQE-IVDFLKDPEKFTrlGAKIP-KGVLLVGPPGTG 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 285 KTLLAKAVATECGTTFFNVSsatlaskwrGeSE-----------RmVRCLFDLARAYAPSTIFIDEIDSLCNSRG---GS 350
Cdd:COG0465  188 KTLLAKAVAGEAGVPFFSIS---------G-SDfvemfvgvgasR-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGG 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 351 GEHEssRrvksE-----LLVQVDGVSntaTNEDgsrkiVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPDFESRKALI 422
Cdd:COG0465  257 GHDE--R----EqtlnqLLVEMDGFE---GNEG-----VIVIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAIL 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 423 NINLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRkiaGKTRdeiknmskddisndpVAMCDFEEAIRKVQ 502
Cdd:COG0465  322 KVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARR---NKKA---------------VTMEDFEEAIDRVI 383
                        330       340
                 ....*....|....*....|..
gi 257732100 503 --PSVSS---SDIEK-----HE 514
Cdd:COG0465  384 agPERKSrviSEKEKkitayHE 405
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
240-410 3.29e-53

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 177.62  E-value: 3.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIR--RPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESE 317
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 318 RMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVSNtatnedGSRKIVMVLAATNFPWDID 397
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLST------DGNCRVIVMGATNRPQDLD 153
                        170
                 ....*....|...
gi 257732100 398 EALRRRLEKRIYI 410
Cdd:cd19520  154 EAILRRMPKRFHI 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 ...
240-410 4.91e-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: 171.71  E-value: 4.91e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESE 317
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 318 RMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVSNTATnedgsrkiVMVLAATNFPWDID 397
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKR-EEDQREVERRVVAQLLTLMDGMSSRGK--------VVVIAATNRPDAID 150
                        170
                 ....*....|....*
gi 257732100 398 EALRR--RLEKRIYI 410
Cdd:cd19503  151 PALRRpgRFDREVEI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
275-412 7.64e-51

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: 170.08  E-value: 7.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  275 VLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHE 354
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100  355 SSRRVKSELLVQVDGVSNTATNedgsrkiVMVLAATNFPWDIDEALRRRLEKRIYIPL 412
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSK-------VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
231-466 3.82e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 174.18  E-value: 3.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 231 DSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATL 308
Cdd:PTZ00454 137 SEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEqiGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 309 ASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSR--GGSGEHESSRRVKSELLVQVDGVSNTATnedgsrkiVMV 386
Cdd:PTZ00454 216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdAQTGADREVQRILLELLNQMDGFDQTTN--------VKV 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 387 LAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNGM 464
Cdd:PTZ00454 288 IMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAV 367

                 ..
gi 257732100 465 RR 466
Cdd:PTZ00454 368 RK 369
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
238-459 5.02e-49

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 169.29  E-value: 5.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 238 WDDVAGLSEAKRLLEEAVvlplwmpEYFQGIRRP-----W--KGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLAS 310
Cdd:COG1223    1 LDDVVGQEEAKKKLKLII-------KELRRRENLrkfglWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 311 KWRGESERMVRCLFDLARAyAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTatnedgsrkiVMVLAAT 390
Cdd:COG1223   74 SYLGETARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSG----------SVVIAAT 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257732100 391 NFPWDIDEALRRRLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDA 459
Cdd:COG1223  143 NHPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
247-410 1.13e-48

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: 165.15  E-value: 1.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 247 AKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDL 326
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 327 ARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTATnedgsrkiVMVLAATNFPWDIDEALRR--RL 404
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSK--------VLVIAATNRPDLLDPALLRpgRF 152

                 ....*.
gi 257732100 405 EKRIYI 410
Cdd:cd19481  153 DEVIEF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
238-408 3.18e-46

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: 159.43  E-value: 3.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 238 WDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGE 315
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 316 SERMVRCLFDLARAYAPSTIFIDEIDSLCNSR---GGSGEHESSRRVkSELLVQVDGVSntatnedgSRKIVMVLAATNF 392
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTM-LELLNQLDGFD--------PRGNIKVIMATNR 151
                        170
                 ....*....|....*...
gi 257732100 393 PWDIDEALRR--RLEKRI 408
Cdd:cd19502  152 PDILDPALLRpgRFDRKI 169
ftsH CHL00176
cell division protein; Validated
235-476 2.21e-45

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 168.69  E-value: 2.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 235 GVRWDDVAGLSEAKRLLEEAVVLpLWMPEYFQGI-RRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWR 313
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 314 GESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGG--SGEHESSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATN 391
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDEREQTLNQLLTEMDGFK--------GNKGVIVIAATN 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 392 FPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKIA 469
Cdd:CHL00176 330 RVDILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKA 409

                 ....*..
gi 257732100 470 GKTRDEI 476
Cdd:CHL00176 410 TITMKEI 416
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
247-410 3.38e-45

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 156.12  E-value: 3.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 247 AKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLF 324
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 325 DLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELLVQVDGVSNTatnedgsrKIVMVLAATNFPWDIDEALRR-- 402
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGLEEM--------NGVVVIAATNRPDIIDPALLRag 151

                 ....*...
gi 257732100 403 RLEKRIYI 410
Cdd:cd19529  152 RFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
248-410 5.52e-45

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: 155.75  E-value: 5.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 248 KRLLEEAVVLPLWMPEYFQGI-RRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDL 326
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLKFgMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 327 ARAYAPSTIFIDEIDSLCNSRGGS--GEHESSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDIDEALRR-- 402
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNigDAGGAADRVINQILTEMDGMN--------TKKNVFIIGATNRPDIIDPAILRpg 153

                 ....*...
gi 257732100 403 RLEKRIYI 410
Cdd:cd19528  154 RLDQLIYI 161
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
230-467 3.15e-44

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 161.86  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 230 LDSTPGVRWDDVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSAT 307
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 308 LASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSR--GGSGEHESSRRVKSELLVQVDGVSntatnedgSRKIVM 385
Cdd:PTZ00361 253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGFD--------SRGDVK 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 386 VLAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNVCRDASMNG 463
Cdd:PTZ00361 325 VIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLA 404

                 ....
gi 257732100 464 MRRK 467
Cdd:PTZ00361 405 LRER 408
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
240-410 1.59e-43

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: 151.96  E-value: 1.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERM 319
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 320 VRCLFDLARAYAPSTIFIDEIDSLCNSRggSGEHESSRRVKSELLVQVDGVSNTAtnEDGsrkiVMVLAATNFPWDIDEA 399
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQ--DDEASPVGRLQVELLAQLDGVLGSG--EDG----VLVVCTTSKPEEIDES 152
                        170
                 ....*....|.
gi 257732100 400 LRRRLEKRIYI 410
Cdd:cd19523  153 LRRYFSKRLLV 163
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
240-411 2.67e-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: 146.04  E-value: 2.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESE 317
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKaiGIKPP-RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 318 RMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGS-GEHEssRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDI 396
Cdd:cd19519   80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKThGEVE--RRIVSQLLTLMDGLK--------QRAHVIVMAATNRPNSI 149
                        170
                 ....*....|....*..
gi 257732100 397 DEALRR--RLEKRIYIP 411
Cdd:cd19519  150 DPALRRfgRFDREIDIG 166
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
236-410 4.97e-41

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: 145.45  E-value: 4.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 236 VRWDDVAGLSEAKRLLEEAVVLpLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWR 313
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 314 GESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRG--GSGEHESSRRVKSELLVQVDGVsntatnedGSRKIVMVLAATN 391
Cdd:cd19501   79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGagLGGGHDEREQTLNQLLVEMDGF--------ESNTGVIVIAATN 150
                        170       180
                 ....*....|....*....|.
gi 257732100 392 FPWDIDEALRR--RLEKRIYI 410
Cdd:cd19501  151 RPDVLDPALLRpgRFDRQVYV 171
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
222-501 2.84e-40

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 154.42  E-value: 2.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 222 AAMLERDVLDSTpgvrWDDVAGLSEAKRLLEEAVVLpLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTT 299
Cdd:PRK10733 139 ARMLTEDQIKTT----FADVAGCDEAKEEVAELVEY-LREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVP 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 300 FFNVSSATLASKWRGESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGG--SGEHESSRRVKSELLVQVDGVsntatne 377
Cdd:PRK10733 213 FFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGF------- 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 378 DGSRKIVmVLAATNFPWDIDEALRR--RLEKRIYIPLPDFESRKALININLRTVEVASDVNIEDVARRTEGYSGDDLTNV 455
Cdd:PRK10733 286 EGNEGII-VIAATNRPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANL 364
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 257732100 456 CRDASMNGMRrkiaGKTRdeiknmskddisndPVAMCDFEEAIRKV 501
Cdd:PRK10733 365 VNEAALFAAR----GNKR--------------VVSMVEFEKAKDKI 392
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
244-410 3.88e-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: 139.93  E-value: 3.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 244 LSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVR 321
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 322 CLFDLARAYAPSTIFIDEIDSLCNSRGGsGEHESSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDIDEALR 401
Cdd:cd19530   80 QVFQRARASAPCVIFFDEVDALVPKRGD-GGSWASERVVNQLLTEMDGLE--------ERSNVFVIAATNRPDIIDPAML 150
                        170
                 ....*....|.
gi 257732100 402 R--RLEKRIYI 410
Cdd:cd19530  151 RpgRLDKTLYV 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
240-409 1.99e-36

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: 133.02  E-value: 1.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQGIR-RPWKGVLMFGPPGTGKTLLAKAVATECGT-----TFFNVSSATLASKWR 313
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 314 GESERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVkSELLVQVDGVSNtatnedgsRKIVMVLAATNFP 393
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIV-STLLALMDGLDN--------RGQVVVIGATNRP 151
                        170
                 ....*....|....*...
gi 257732100 394 WDIDEALRR--RLEKRIY 409
Cdd:cd19517  152 DALDPALRRpgRFDREFY 169
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
240-408 3.65e-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: 129.45  E-value: 3.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVVLPLWMPEYFQ--GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESE 317
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQhlGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 318 RMVRCLFDLARAYAPSTIFIDEIDSLCNSRgGSGEHESSRRVKSELLVQVDGVSNTATNedgsRKIVMVLAATNFPWDID 397
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKTA----GGPVLVIGATNRPDSLD 154
                        170
                 ....*....|...
gi 257732100 398 EALRR--RLEKRI 408
Cdd:cd19518  155 PALRRagRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
248-410 5.71e-35

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 128.78  E-value: 5.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 248 KRLLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFDLA 327
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 328 RAYAPSTIFIDEIDSLCNSRGGSGEHESSR-RVKSELLVQVDGVSNTATNedgsrkiVMVLAATNFPWDIDEALRR--RL 404
Cdd:cd19527   82 RDAKPCVIFFDELDSLAPSRGNSGDSGGVMdRVVSQLLAELDGMSSSGQD-------VFVIGATNRPDLLDPALLRpgRF 154

                 ....*.
gi 257732100 405 EKRIYI 410
Cdd:cd19527  155 DKLLYL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
247-409 9.51e-33

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: 122.54  E-value: 9.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 247 AKRLLEEAVVLPLWMPEYFQGIR-RPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESERMVRCLFD 325
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPlRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 326 LARAYAPSTIFIDEIDSLCNSRGgsgeHESS---RRVKSELLVQVDGVSNTatneDGsrkiVMVLAATNFPWDIDEALRR 402
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRG----HDSTgvtDRVVNQLLTQLDGVEGL----DG----VYVLAATSRPDLIDPALLR 148

                 ....*....
gi 257732100 403 --RLEKRIY 409
Cdd:cd19526  149 pgRLDKLVY 157
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
9-77 8.85e-28

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: 105.74  E-value: 8.85e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257732100   9 AGLQDHLKLAREYALEGSYDTSVIFFDGAIAQINKHLNTLDDPLARTKWMNVKKAIMEETEVVKQLDAE 77
Cdd:cd21748    1 AEICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
269-412 1.58e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 102.22  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 269 RRPWKGVLMFGPPGTGKTLLAKAVATEC---GTTFFNVSSATLASKWRGESER---MVRCLFDLARAYAPSTIFIDEIDS 342
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257732100 343 LcnsrggsgehesSRRVKSELLVQVDGVSNTATNEDGsrkiVMVLAATNFPW--DIDEALRRRLEKRIYIPL 412
Cdd:cd00009   96 L------------SRGAQNALLRVLETLNDLRIDREN----VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
240-364 3.71e-18

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: 81.65  E-value: 3.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 240 DVAGLSEAKRLLEEAVvlPLWMPEYFQ-GIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESER 318
Cdd:cd19507    1 DVGGLDNLKDWLKKRK--AAFSKQASAyGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 257732100 319 MVRCLFDLARAYAPSTIFIDEIDSLCNSRGGSGEHESSRRVKSELL 364
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFL 123
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
273-410 4.91e-18

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: 81.77  E-value: 4.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 273 KGVLMFGPPGTGKTLLAKAVAtecgtTFFN------VSSATLASKWRGESERMVRCLFDLA----RAYAPST----IFID 338
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIG-----KMLNarepkiVNGPEILNKYVGESEANIRKLFADAeeeqRRLGANSglhiIIFD 110
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100 339 EIDSLCNSRG----GSGEHESsrrVKSELLVQVDGVSNTATnedgsrkiVMVLAATNFPWDIDEALRR--RLEKRIYI 410
Cdd:cd19504  111 EIDAICKQRGsmagSTGVHDT---VVNQLLSKIDGVEQLNN--------ILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
271-414 3.79e-16

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 75.49  E-value: 3.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100   271 PWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATL-----------------ASKWRGESERMVRCLFDLARAYAPS 333
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGedileevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100   334 TIFIDEIDSLCnsrggsgehessrRVKSELLVQVDGVSNTATNEDGSRKIVMVLAATNFPWDIDEALRRRLEKRIYIPLP 413
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147

                   .
gi 257732100   414 D 414
Cdd:smart00382 148 L 148
ycf46 CHL00195
Ycf46; Provisional
239-518 1.25e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 79.29  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 239 DDVAGLSEAKRLLEE-AVVLPLWMPEYfqGIRRPwKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGESE 317
Cdd:CHL00195 228 SDIGGLDNLKDWLKKrSTSFSKQASNY--GLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESE 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 318 RMVRCLFDLARAYAPSTIFIDEID---SLCNSRGGSGeheSSRRVKSELLvqvdgvsnTATNEdgSRKIVMVLA-ATNFP 393
Cdd:CHL00195 305 SRMRQMIRIAEALSPCILWIDEIDkafSNSESKGDSG---TTNRVLATFI--------TWLSE--KKSPVFVVAtANNID 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 394 WDIDEALRR-RLEKRIYIPLPDFESRKALININLRTVEVAS--DVNIEDVARRTEGYSGDDLtnvcRDASMNGMRrkIAg 470
Cdd:CHL00195 372 LLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSwkKYDIKKLSKLSNKFSGAEI----EQSIIEAMY--IA- 444
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 257732100 471 ktRDEIKNMSKDDISNdpvamcdfeeAIRKVQP--SVSSSDIEKHEKWLS 518
Cdd:CHL00195 445 --FYEKREFTTDDILL----------ALKQFIPlaQTEKEQIEALQNWAS 482
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
275-410 1.65e-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: 63.62  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECG---------TTFFNVSSATLASKWRGESERMVRCLFD-----LARAYAPSTIFIDEI 340
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257732100 341 DSLCNSRGGS---GEHESSRRVKSELLVQVDGVSntatnedgSRKIVMVLAATNFPWDIDEALRRRLEKRIYI 410
Cdd:cd19508  135 ESLAAARSASssgTEPSDAIRVVNAVLTQIDRIK--------RYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
434-478 6.17e-11

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: 57.55  E-value: 6.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 257732100  434 DVNIEDVARRTEGYSGDDLTNVCRDASMNGMRRKIAGKTRDEIKN 478
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
269-408 6.60e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 60.62  E-value: 6.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 269 RRPWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRgESERMVRCLFDLARAYAPSTI-FIDEIDSLCNSR 347
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKR 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257732100 348 GGSGEHESSRRVKSELLVQVDgvsntatneDGSRKIVMVLaATNFPWDIDEALRRRLEKRI 408
Cdd:cd19512   98 STEKISEDLRAALNAFLYRTG---------EQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
479-521 2.28e-10

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: 56.35  E-value: 2.28e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 257732100  479 MSKDDISND-----PVAMCDFEEAIRKVQPSVSSSDIEKHEKWLSEFG 521
Cdd:pfam09336  14 MTWMDIPSDkllepPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
273-408 3.86e-10

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 58.69  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 273 KGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKWRGES--ERMVRCLFDLARAYAPSTIFIDEIDSLCNSRGGS 350
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 257732100 351 GEHESS-RRVKSELlvqvDGVSNTATNEDGsrkiVMVLAATNFPWDIDEALRRRLEKRI 408
Cdd:cd19506  107 TEKQLDpKRLKKDL----PKILKSLKPEDR----VLIVGTTSRPFEADLKSFCKVYNKI 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
262-410 7.07e-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: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 262 PEYFQGIRRPWK-GVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATlaskwRGESERMVRCLfdLARAYAPSTIFIDEI 340
Cdd:cd19510   12 EDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDI 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257732100 341 DSLCNSRGGSGEHES-----SRRVKSELLVQVDGVsnTATNEdgsRKIVMvlaATNFPWDIDEALRR--RLEKRIYI 410
Cdd:cd19510   85 DAAFESREHNKKNPSaygglSRVTFSGLLNALDGV--ASSEE---RIVFM---TTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
273-408 8.27e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 52.38  E-value: 8.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 273 KGVLMFGPPGTGKTLLAKAVATECGTTFFNVSsatlASKWRG------ESERMVRclfDLARAyapsTIFIDEIDSLCNS 346
Cdd:cd19498   47 KNILMIGPTGVGKTEIARRLAKLAGAPFIKVE----ATKFTEvgyvgrDVESIIR---DLVEG----IVFIDEIDKIAKR 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100 347 RGGSGEHESSRRVKSELLVQVDGvsNTATNEDGSRKI--VMVLAATNF----PWDIDEALRRRLEKRI 408
Cdd:cd19498  116 GGSSGPDVSREGVQRDLLPIVEG--STVSTKYGPVKTdhILFIAAGAFhvakPSDLIPELQGRFPIRV 181
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
271-400 2.51e-07

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 50.45  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 271 PWKGVLMFGPPGTGKTLLAKAVATECGTTFFNVSSATLASKW--------------RGESERMVRCLFDLARAYAPSTIF 336
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 257732100 337 IDEIDSLcNSRGGSGEHESSRRVKSELLVQV--DGVSNTATNEdgsrkiVMVLAATNFPWDIDEAL 400
Cdd:cd19505   91 IPNIHEL-NVNRSTQNLEEDPKLLLGLLLNYlsRDFEKSSTRN------ILVIASTHIPQKVDPAL 149
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
227-405 6.78e-07

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 49.48  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 227 RDVLDstpgvrwDDVAGLSEAK-RLLEEAVVLPLwmpeyfqgiRRPWKG-VLMF-GPPGTGKTLLAKAVATECGTTFFNV 303
Cdd:cd19500    5 RKVLD-------ADHYGLEDVKeRILEYLAVRKL---------KGSMKGpILCLvGPPGVGKTSLGKSIARALGRKFVRI 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 304 SSATLaskwRGESE--------------RMVRCLFDlARAYAPsTIFIDEIDSLcnSRGGSGEHESSrrvkseLLVQVDG 369
Cdd:cd19500   69 SLGGV----RDEAEirghrrtyvgampgRIIQALKK-AGTNNP-VFLLDEIDKI--GSSFRGDPASA------LLEVLDP 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 257732100 370 VSNTATNE-------DGSRkiVMVLAATNFPWDIDEALRRRLE 405
Cdd:cd19500  135 EQNSTFSDhyldvpfDLSK--VLFIATANSLDTIPGPLLDRME 175
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
275-442 8.61e-07

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 50.55  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECGTTFF--NVSSATLASKWRGESermvrclfDLARAYAP----------STIFIDEIDs 342
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriQFTPDLLPSDILGTY--------IYDQQTGEfefrpgplfaNVLLADEIN- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 343 lcnsRggsgeheSSRRVKSELL-------VQVDGVSNTAtnedgsRKIVMVLAATNfPWDID------EALRRRLEKRIY 409
Cdd:COG0714  105 ----R-------APPKTQSALLeameerqVTIPGGTYKL------PEPFLVIATQN-PIEQEgtyplpEAQLDRFLLKLY 166
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 257732100 410 IPLPDFESRKALIN--INLRTVEVASDVNIEDVAR 442
Cdd:COG0714  167 IGYPDAEEEREILRrhTGRHLAEVEPVLSPEELLA 201
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
275-340 1.02e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.21  E-value: 1.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECGTTFFNVsSATLASKwrgeSErmVRCLFDLA---RAYAPSTI-FIDEI 340
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVAL-SAVTSGV----KD--IREVIEEArerRAYGRRTIlFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
278-340 1.69e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.47  E-value: 1.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257732100 278 FGPPGTGKTLLAKAVATECGTTFFNVsSATLASKwrgeSErmVRCLFDLA---RAYAPSTI-FIDEI 340
Cdd:PRK13342  42 WGPPGTGKTTLARIIAGATDAPFEAL-SAVTSGV----KD--LREVIEEArqrRSAGRRTIlFIDEI 101
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
273-323 7.65e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 45.35  E-value: 7.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 257732100 273 KGVLMFGPPGTGKTLLAKAVATECG--TTFFNVSSATLASKWRGESERMVRCL 323
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEIYSAELKKTEFLMQAL 117
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
240-294 1.04e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 43.68  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100  240 DVAGLSEAKRLLEEAVVlplwmpeyfqgirrpwkG---VLMFGPPGTGKTLLAKAVAT 294
Cdd:pfam01078   4 DVKGQEQAKRALEIAAA-----------------GghnLLMIGPPGSGKTMLAKRLPG 44
PRK04195 PRK04195
replication factor C large subunit; Provisional
239-295 1.06e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.91  E-value: 1.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 257732100 239 DDVAGLSEAKRLLEEavvlplWMPEYFQGirRPWKGVLMFGPPGTGKTLLAKAVATE 295
Cdd:PRK04195  14 SDVVGNEKAKEQLRE------WIESWLKG--KPKKALLLYGPPGVGKTSLAHALAND 62
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
240-294 2.14e-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: 43.88  E-value: 2.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100 240 DVAGLSEAKRLLEEAVVlplwmpeyfqgirrpwkG---VLMFGPPGTGKTLLAKAVAT 294
Cdd:COG0606  193 DVKGQEQAKRALEIAAA-----------------GghnLLMIGPPGSGKTMLARRLPG 233
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
270-341 2.45e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 41.80  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  270 RPwKGVLMF-GPPGTGKTLLAKAVA-----TECGTTFFNVSSAT---LASKWRGESERMVRC-----LFDLARAYAPSTI 335
Cdd:pfam07724   1 RP-IGSFLFlGPTGVGKTELAKALAellfgDERALIRIDMSEYMeehSVSRLIGAPPGYVGYeeggqLTEAVRRKPYSIV 79

                  ....*.
gi 257732100  336 FIDEID 341
Cdd:pfam07724  80 LIDEIE 85
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
275-300 3.67e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 3.67e-04
                         10        20
                 ....*....|....*....|....*.
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECGTTF 300
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNI 79
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
243-444 1.06e-03

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: 41.75  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  243 GLSEAKR---LLEEAVVLPLWMPEYFQGIRRPWKGVLMFGPPGTGKTLLAKAVATE-CGTTFF------NVSSATLASKW 312
Cdd:TIGR03922 280 GLERVKRqvaALKSSTAMALARAERGLPVAQTSNHMLFAGPPGTGKTTIARVVAKIyCGLGVLrkplvrEVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100  313 RGESERMVRCLFDLARAYApstIFIDEIDSLCNSRGGSGEHESSRRVKSeLLVQVdgvsntatnEDGSRKIVMVLA---- 388
Cdd:TIGR03922 360 IGESEAKTNEIIDSALGGV---LFLDEAYTLVETGYGQKDPFGLEAIDT-LLARM---------ENDRDRLVVIGAgyrk 426
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 257732100  389 ATNFPWDIDEALRRRLEKRIyiplpDFESRKA--LININLRTVEVASDVnIEDVARRT 444
Cdd:TIGR03922 427 DLDKFLEVNEGLRSRFTRVI-----EFPSYSPdeLVEIARRMATERDSV-LDDAAADA 478
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
275-300 2.59e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 2.59e-03
                          10        20
                  ....*....|....*....|....*.
gi 257732100  275 VLMFGPPGTGKTLLAKAVATECGTTF 300
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI 61
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
273-307 4.86e-03

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 39.21  E-value: 4.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 257732100  273 KGVLMFGPPGTGKTLLAKAVATECGT-TFFNVSSAT 307
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEdTPFTSISGS 86
PRK08116 PRK08116
hypothetical protein; Validated
274-409 6.22e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.46  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 274 GVLMFGPPGTGKTLLAKAVATECgttffnvssatlaskwrgeSERMVRCLFDlarayapSTI-FIDEIDSLCNSRGGSGE 352
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANEL-------------------IEKGVPVIFV-------NFPqLLNRIKSTYKSSGKEDE 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257732100 353 HESSRRVKS-ELLVQVD-GVSNtaTNEDGSRKIVMVL-----------AATNFPwdIDEaLRRRLEKRIY 409
Cdd:PRK08116 170 NEIIRSLVNaDLLILDDlGAER--DTEWAREKVYNIIdsryrkglptiVTTNLS--LEE-LKNQYGKRIY 234
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
273-296 6.91e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.22  E-value: 6.91e-03
                         10        20
                 ....*....|....*....|....
gi 257732100 273 KGVLMFGPPGTGKTLLAKAVATEC 296
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEA 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
275-300 9.45e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.14  E-value: 9.45e-03
                         10        20
                 ....*....|....*....|....*.
gi 257732100 275 VLMFGPPGTGKTLLAKAVATECGTTF 300
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 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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