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Conserved domains on  [gi|2015239388|gb|KAG5211637|]
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hypothetical protein JEQ12_014066 [Ovis aries]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
341-504 2.35e-108

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: 333.74  E-value: 2.35e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 420
Cdd:cd19524      1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  421 VRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTK 500
Cdd:cd19524     81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160

                   ....
gi 2015239388  501 RVYV 504
Cdd:cd19524    161 RVYV 164
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
114-193 8.49e-33

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


:

Pssm-ID: 239142  Cd Length: 79  Bit Score: 121.62  E-value: 8.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  114 VRAFHKQAFEYISVALRIDEDekvGQKDQAVEWYKKGIEELEKGIAVVV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 191
Cdd:cd02679      1 IRGYYKQAFEEISKALRADEW---GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQ 77

                   ..
gi 2015239388  192 LL 193
Cdd:cd02679     78 VL 79
Cation_efflux pfam01545
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
633-829 3.13e-27

Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.


:

Pssm-ID: 426316 [Multi-domain]  Cd Length: 189  Bit Score: 109.67  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  633 ALTAYTYLTIFDLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLE-QPEIHTGRL 711
Cdd:pfam01545   17 ALLADAVHSLIDLISSLLALLALRLSRKPPDERFPFGHGRLEPLAALVVGILLLGGGVFLLYESIQRLLSpGEEIDPGLA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  712 LVGTFVALSFNLFTMLSIRNKPFAYvseaastswlqehvadlsrslcgiipglSSIFLPRMNPFVLIDLAGAFALCITYM 791
Cdd:pfam01545   97 LILALVSLLVNLFLLLYLRRAARRI----------------------------RSPALKADALHALSDVLASLGVLISAL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2015239388  792 LIEINNYFA---VDTASAIAIALMTFGTMYPMSVYSGKVLL 829
Cdd:pfam01545  149 LIYLGPITGgllADPLASLLIGLLILYTALRLLKESLSILL 189
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
531-585 2.20e-07

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


:

Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 48.30  E-value: 2.20e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015239388  531 ELAQLARMTDGYSGSDLTALAKDAALGPIRElkpeqvknmsasEMRNIRLSDFTE 585
Cdd:pfam17862    3 DLEELAERTEGFSGADLEALCREAALAALRR------------GLEAVTQEDLEE 45
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
578-610 2.13e-05

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: 42.87  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2015239388  578 IRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFG 610
Cdd:pfam09336   29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
341-504 2.35e-108

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: 333.74  E-value: 2.35e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 420
Cdd:cd19524      1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  421 VRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTK 500
Cdd:cd19524     81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160

                   ....
gi 2015239388  501 RVYV 504
Cdd:cd19524    161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
337-593 3.55e-78

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 258.78  E-value: 3.55e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  337 VKFDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV 414
Cdd:COG1222     75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  415 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE-GEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEA 493
Cdd:COG1222    154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDPA 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  494 VLR--RFTKRVYVSLPNEETRLLLLKNLLckQGSPLTQKE-LAQLARMTDGYSGSDLTALAKDAALGPIRELKPEqvknm 570
Cdd:COG1222    232 LLRpgRFDRVIEVPLPDEEAREEILKIHL--RDMPLADDVdLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT----- 304
                          250       260
                   ....*....|....*....|...
gi 2015239388  571 sasemrnIRLSDFTESLKKIKRS 593
Cdd:COG1222    305 -------VTMEDLEKAIEKVKKK 320
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
331-592 2.52e-59

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 208.53  E-value: 2.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  331 VDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAAS 408
Cdd:PRK03992   122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  409 LTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE----GEHDASRRLkTEFLIEFDGVQSAGDdrVLVMGAT 484
Cdd:PRK03992   201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGN--VKIIAAT 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  485 NRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLlckqgsplTQK-------ELAQLARMTDGYSGSDLTALAKDAA 555
Cdd:PRK03992   278 NRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIH--------TRKmnladdvDLEELAELTEGASGADLKAICTEAG 349
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2015239388  556 LGPIRELKPEqvknmsasemrnIRLSDFTESLKKIKR 592
Cdd:PRK03992   350 MFAIRDDRTE------------VTMEDFLKAIEKVMG 374
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
309-613 8.48e-57

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: 210.15  E-value: 8.48e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  309 KKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGK 386
Cdd:TIGR01243  422 KVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGK 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  387 TMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCER--REGEhDASRRLKTEFL 464
Cdd:TIGR01243  501 TLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgaRFDT-SVTDRIVNQLL 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  465 IEFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLCKQgsPLTQK-ELAQLARMTDG 541
Cdd:TIGR01243  580 TEMDGIQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSM--PLAEDvDLEELAEMTEG 655
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  542 YSGSDLTALAKDAALGPIREL-------KPEQVKNMSASEMRnIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTT 613
Cdd:TIGR01243  656 YTGADIEAVCREAAMAALRESigspakeKLEVGEEEFLKDLK-VEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
376-506 4.45e-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: 175.86  E-value: 4.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  376 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDA 455
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2015239388  456 SRRLKTEFLIEFDGVQSAGdDRVLVMGATNRPQELDEAVLRRFTKRVYVSL 506
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSN-SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
114-193 8.49e-33

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


Pssm-ID: 239142  Cd Length: 79  Bit Score: 121.62  E-value: 8.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  114 VRAFHKQAFEYISVALRIDEDekvGQKDQAVEWYKKGIEELEKGIAVVV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 191
Cdd:cd02679      1 IRGYYKQAFEEISKALRADEW---GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQ 77

                   ..
gi 2015239388  192 LL 193
Cdd:cd02679     78 VL 79
Cation_efflux pfam01545
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
633-829 3.13e-27

Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.


Pssm-ID: 426316 [Multi-domain]  Cd Length: 189  Bit Score: 109.67  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  633 ALTAYTYLTIFDLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLE-QPEIHTGRL 711
Cdd:pfam01545   17 ALLADAVHSLIDLISSLLALLALRLSRKPPDERFPFGHGRLEPLAALVVGILLLGGGVFLLYESIQRLLSpGEEIDPGLA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  712 LVGTFVALSFNLFTMLSIRNKPFAYvseaastswlqehvadlsrslcgiipglSSIFLPRMNPFVLIDLAGAFALCITYM 791
Cdd:pfam01545   97 LILALVSLLVNLFLLLYLRRAARRI----------------------------RSPALKADALHALSDVLASLGVLISAL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2015239388  792 LIEINNYFA---VDTASAIAIALMTFGTMYPMSVYSGKVLL 829
Cdd:pfam01545  149 LIYLGPITGgllADPLASLLIGLLILYTALRLLKESLSILL 189
CzcD COG1230
Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism];
644-905 8.68e-26

Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism];


Pssm-ID: 440843 [Multi-domain]  Cd Length: 294  Bit Score: 108.67  E-value: 8.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  644 DLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALSFNL 723
Cdd:COG1230     56 DALALGLALFAYRLARRPADARFTFGYKRAEILAALANALLLLVVAGYILYEAIQRLFNPPPVAGGGMLVVAVIGLVVNL 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  724 FTMLSIRnkpfayvseaastswlQEHVADLSrslcgiipgLSSIFLprmnpFVLIDLAGAFALCITYMLIEINNYFAVDT 803
Cdd:COG1230    136 VSAWLLH----------------RGSKHDLN---------LRGAYL-----HVLADALGSVAVIVAALVILFTGWTWLDP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  804 ASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVigQLDKLIREVSTLDGVLEVRNEHFWTLGFGSLAGSVHVRIRRDANE 883
Cdd:COG1230    186 LLSLLIALLILRSAWGLLRESLRILLEGVPDGI--DLEEVRAALEALPGVADVHDLHVWSLSSGENALTAHVVVDDGADA 263
                          250       260
                   ....*....|....*....|....
gi 2015239388  884 QMVLAHVTNRLYTL--VSTLTVQI 905
Cdd:COG1230    264 DAILDEIRELLAERfgIEHVTIQI 287
CDF TIGR01297
cation diffusion facilitator family transporter; This model describes a broadly distributed ...
643-882 4.92e-23

cation diffusion facilitator family transporter; This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273544 [Multi-domain]  Cd Length: 268  Bit Score: 99.99  E-value: 4.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  643 FDLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLE-QPEIHTGRLLVGTFVALSF 721
Cdd:TIGR01297   27 SDVAASAIALLALRISRRPADERHPFGHGRAEILAALLNGLFLVVVALFILYEAIERLINpEPEIDGGTMLIVAIVGLIV 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  722 NLFtMLSIRNKPFAYVSEAASTSWLQEHVADLSRSLCGIIPGLSSIFlprmnpfvlidlagafalcitymlieinNYFAV 801
Cdd:TIGR01297  107 NLI-LALYLHRVGHRLGSLALRAAALHVLSDALSSVGVLIGALLIYF----------------------------GWHWA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  802 DTASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVigQLDKLIREVSTLDGVLEVRNEHFWTLGFGSLAGSVHVRIRRDA 881
Cdd:TIGR01297  158 DPIAALLISLLILYTAFRLLKESINVLLDAAPDEE--DLEEIKKAILSIPGVKGVHDLHIWRIGPGKLFLDVHVVVDPDL 235

                   .
gi 2015239388  882 N 882
Cdd:TIGR01297  236 D 236
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
372-508 4.92e-17

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 78.95  E-value: 4.92e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388   372 PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-----------------SKYVGEGEKLVRALFAVARELQPS 434
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015239388   435 IIFIDEVDSLLcerregeHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLR-RFTKRVYVSLPN 508
Cdd:smart00382   81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
114-191 4.84e-16

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 73.88  E-value: 4.84e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388   114 VRAFHKQAFEYISVALRIDEdekVGQKDQAVEWYKKGIEELEKGIAVVV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 191
Cdd:smart00745    1 TRDYLSKAKELISKALKADE---AGNYEEALELYKKAIEYLLEGIKVESdsKRREALKAKAAEYLDRAEEIKKSLLERLA 77
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
531-585 2.20e-07

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 48.30  E-value: 2.20e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015239388  531 ELAQLARMTDGYSGSDLTALAKDAALGPIRElkpeqvknmsasEMRNIRLSDFTE 585
Cdd:pfam17862    3 DLEELAERTEGFSGADLEALCREAALAALRR------------GLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
578-610 2.13e-05

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: 42.87  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2015239388  578 IRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFG 610
Cdd:pfam09336   29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
341-504 2.35e-108

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: 333.74  E-value: 2.35e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 420
Cdd:cd19524      1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  421 VRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTK 500
Cdd:cd19524     81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160

                   ....
gi 2015239388  501 RVYV 504
Cdd:cd19524    161 RVYV 164
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
342-504 5.75e-95

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 298.11  E-value: 5.75e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  342 IAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLV 421
Cdd:cd19509      1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  422 RALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTKR 501
Cdd:cd19509     81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160

                   ...
gi 2015239388  502 VYV 504
Cdd:cd19509    161 IYI 163
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
319-504 2.86e-92

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: 291.89  E-value: 2.86e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  319 DSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN 398
Cdd:cd19525      1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  399 ATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRV 478
Cdd:cd19525     81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160
                          170       180
                   ....*....|....*....|....*.
gi 2015239388  479 LVMGATNRPQELDEAVLRRFTKRVYV 504
Cdd:cd19525    161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
337-593 3.55e-78

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 258.78  E-value: 3.55e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  337 VKFDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV 414
Cdd:COG1222     75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  415 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE-GEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEA 493
Cdd:COG1222    154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDPA 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  494 VLR--RFTKRVYVSLPNEETRLLLLKNLLckQGSPLTQKE-LAQLARMTDGYSGSDLTALAKDAALGPIRELKPEqvknm 570
Cdd:COG1222    232 LLRpgRFDRVIEVPLPDEEAREEILKIHL--RDMPLADDVdLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT----- 304
                          250       260
                   ....*....|....*....|...
gi 2015239388  571 sasemrnIRLSDFTESLKKIKRS 593
Cdd:COG1222    305 -------VTMEDLEKAIEKVKKK 320
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
337-504 1.53e-69

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: 229.36  E-value: 1.53e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  337 VKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGE 416
Cdd:cd19521      4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  417 GEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVqSAGDDRVLVMGATNRPQELDEAVLR 496
Cdd:cd19521     84 SEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGV-GNDSQGVLVLGATNIPWQLDSAIRR 162

                   ....*...
gi 2015239388  497 RFTKRVYV 504
Cdd:cd19521    163 RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
341-504 6.20e-67

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: 221.91  E-value: 6.20e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELF--TGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 418
Cdd:cd19520      1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  419 KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRF 498
Cdd:cd19520     81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160

                   ....*.
gi 2015239388  499 TKRVYV 504
Cdd:cd19520    161 PKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
341-504 9.41e-64

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: 213.31  E-value: 9.41e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 420
Cdd:cd19522      1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  421 VRALFAVARELQPSIIFIDEVDSlLCERR--EGEHDASRRLKTEFLIEFDGVQ--SAGDDR---VLVMGATNRPQELDEA 493
Cdd:cd19522     81 VRLLFEMARFYAPTTIFIDEIDS-ICSRRgtSEEHEASRRVKSELLVQMDGVGgaSENDDPskmVMVLAATNFPWDIDEA 159
                          170
                   ....*....|.
gi 2015239388  494 VLRRFTKRVYV 504
Cdd:cd19522    160 LRRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
339-591 8.32e-61

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: 213.23  E-value: 8.32e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  339 FDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGE 416
Cdd:COG0464    156 LDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  417 GEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQsagdDRVLVMGATNRPQELDEAVLR 496
Cdd:COG0464    235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR----SDVVVIAATNRPDLLDPALLR 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  497 RFTKRVYVSLPNEETRLLLLKNLLckQGSPLTQK-ELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEqvknmsasem 575
Cdd:COG0464    311 RFDEIIFFPLPDAEERLEIFRIHL--RKRPLDEDvDLEELAEATEGLSGADIRNVVRRAALQALRLGREP---------- 378
                          250
                   ....*....|....*.
gi 2015239388  576 rnIRLSDFTESLKKIK 591
Cdd:COG0464    379 --VTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
331-592 2.52e-59

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 208.53  E-value: 2.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  331 VDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAAS 408
Cdd:PRK03992   122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  409 LTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE----GEHDASRRLkTEFLIEFDGVQSAGDdrVLVMGAT 484
Cdd:PRK03992   201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGN--VKIIAAT 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  485 NRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLlckqgsplTQK-------ELAQLARMTDGYSGSDLTALAKDAA 555
Cdd:PRK03992   278 NRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIH--------TRKmnladdvDLEELAELTEGASGADLKAICTEAG 349
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2015239388  556 LGPIRELKPEqvknmsasemrnIRLSDFTESLKKIKR 592
Cdd:PRK03992   350 MFAIRDDRTE------------VTMEDFLKAIEKVMG 374
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
309-613 8.48e-57

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: 210.15  E-value: 8.48e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  309 KKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGK 386
Cdd:TIGR01243  422 KVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGK 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  387 TMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCER--REGEhDASRRLKTEFL 464
Cdd:TIGR01243  501 TLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgaRFDT-SVTDRIVNQLL 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  465 IEFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLCKQgsPLTQK-ELAQLARMTDG 541
Cdd:TIGR01243  580 TEMDGIQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSM--PLAEDvDLEELAEMTEG 655
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  542 YSGSDLTALAKDAALGPIREL-------KPEQVKNMSASEMRnIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTT 613
Cdd:TIGR01243  656 YTGADIEAVCREAAMAALRESigspakeKLEVGEEEFLKDLK-VEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
337-593 6.90e-54

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: 201.29  E-value: 6.90e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  337 VKFDDIAGQELAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVG 415
Cdd:TIGR01243  175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  416 EGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAVL 495
Cdd:TIGR01243  255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRG--RVIVIGATNRPDALDPALR 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  496 R--RFTKRVYVSLPNEETRLLLLKNLLckQGSPLTQ-KELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSA 572
Cdd:TIGR01243  333 RpgRFDREIVIRVPDKRARKEILKVHT--RNMPLAEdVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKINFEA 410
                          250       260
                   ....*....|....*....|....*...
gi 2015239388  573 SE-----MRNIRLS--DFTESLKKIKRS 593
Cdd:TIGR01243  411 EEipaevLKELKVTmkDFMEALKMVEPS 438
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
341-504 1.69e-53

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: 183.93  E-value: 1.69e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 420
Cdd:cd19523      1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  421 VRALFAVARELQPSIIFIDEVDSLLCERREgEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTK 500
Cdd:cd19523     81 LQASFLAARCRQPSVLFISDLDALLSSQDD-EASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159

                   ....
gi 2015239388  501 RVYV 504
Cdd:cd19523    160 RLLV 163
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
341-504 2.30e-52

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 180.57  E-value: 2.30e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFT--GLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 418
Cdd:cd19503      1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  419 KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAVLR-- 496
Cdd:cd19503     80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG--KVVVIAATNRPDAIDPALRRpg 157

                   ....*...
gi 2015239388  497 RFTKRVYV 504
Cdd:cd19503    158 RFDREVEI 165
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
348-504 4.10e-52

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: 179.79  E-value: 4.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  348 AKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAV 427
Cdd:cd19481      1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  428 ARELQPSIIFIDEVDSLLCER-REGEHDASRRLKTEFLIEFDGVQSagDDRVLVMGATNRPQELDEAVLR--RFTKRVYV 504
Cdd:cd19481     81 ARRLAPCILFIDEIDAIGRKRdSSGESGELRRVLNQLLTELDGVNS--RSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
376-506 4.45e-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: 175.86  E-value: 4.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  376 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDA 455
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2015239388  456 SRRLKTEFLIEFDGVQSAGdDRVLVMGATNRPQELDEAVLRRFTKRVYVSL 506
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSN-SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
348-504 1.73e-50

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: 175.16  E-value: 1.73e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  348 AKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALF 425
Cdd:cd19511      1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  426 AVARELQPSIIFIDEVDSLLCER-REGEHDASRRLKTEFLIEFDGVQSAgdDRVLVMGATNRPQELDEAVLR--RFTKRV 502
Cdd:cd19511     80 QKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIESL--KGVVVIAATNRPDMIDPALLRpgRLDKLI 157

                   ..
gi 2015239388  503 YV 504
Cdd:cd19511    158 YV 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
339-504 2.60e-47

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: 166.74  E-value: 2.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  339 FDDIAGQELAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG 417
Cdd:cd19502      2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  418 EKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASR---RLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAV 494
Cdd:cd19502     82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGN--IKVIMATNRPDILDPAL 159
                          170
                   ....*....|..
gi 2015239388  495 LR--RFTKRVYV 504
Cdd:cd19502    160 LRpgRFDRKIEF 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
339-596 2.61e-47

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 169.29  E-value: 2.61e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  339 FDDIAGQELAKQALQEIVI--LPSLRPELFtGLrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGE 416
Cdd:COG1223      1 LDDVVGQEEAKKKLKLIIKelRRRENLRKF-GL-WPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  417 GEKLVRALFAVARELqPSIIFIDEVDSLLCERR-EGEHDASRRLKTEFLIEFDGVQSagddRVLVMGATNRPQELDEAVL 495
Cdd:COG1223     79 TARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGdQNDVGEVKRVVNALLQELDGLPS----GSVVIAATNHPELLDSALW 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  496 RRFTKRVYVSLPNEETRLLLLKNLLCKQGSPLtQKELAQLARMTDGYSGSDLTALAKDAalgpirelkpeqVKNMSASEM 575
Cdd:COG1223    154 RRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTA------------LKKAILEDR 220
                          250       260
                   ....*....|....*....|.
gi 2015239388  576 RNIRLSDFTESLKKIKRSVSP 596
Cdd:COG1223    221 EKVTKEDLEEALKQRKERKKE 241
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
337-504 3.11e-47

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 166.25  E-value: 3.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  337 VKFDDIAGQELAKQALQEIV-ILpsLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV 414
Cdd:cd19501      1 VTFKDVAGCEEAKEELKEVVeFL--KNPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  415 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGE---HDASRRLKTEFLIEFDGVQSagDDRVLVMGATNRPQELD 491
Cdd:cd19501     79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFES--NTGVIVIAATNRPDVLD 156
                          170
                   ....*....|....*
gi 2015239388  492 EAVLR--RFTKRVYV 504
Cdd:cd19501    157 PALLRpgRFDRQVYV 171
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
348-504 1.26e-46

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 164.21  E-value: 1.26e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  348 AKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALF 425
Cdd:cd19529      1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  426 AVARELQPSIIFIDEVDSLLCER-REGEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFTKRV 502
Cdd:cd19529     80 RKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLI 157

                   ..
gi 2015239388  503 YV 504
Cdd:cd19529    158 YI 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
332-602 1.30e-46

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 175.17  E-value: 1.30e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  332 DNGTAVKFDDIAGQELAKQALQEIVILpsLR-PELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASL 409
Cdd:TIGR01241   47 EEKPKVTFKDVAGIDEAKEELMEIVDF--LKnPSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  410 TSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREG---EHDASRRLKTEFLIEFDGVQSAgdDRVLVMGATNR 486
Cdd:TIGR01241  125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGNDEREQTLNQLLVEMDGFGTN--TGVIVIAATNR 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  487 PQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLckQGSPLTQK-ELAQLARMTDGYSGSDLTALAKDAALGPIRELK 563
Cdd:TIGR01241  203 PDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHA--KNKKLAPDvDLKAVARRTPGFSGADLANLLNEAALLAARKNK 280
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2015239388  564 PEqvknmsasemrnIRLSDFTESLKKI-----KRS--VSPQ--TLEAY 602
Cdd:TIGR01241  281 TE------------ITMNDIEEAIDRViagpeKKSrvISEKekKLVAY 316
ftsH CHL00176
cell division protein; Validated
335-565 7.16e-43

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 166.76  E-value: 7.16e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  335 TAVKFDDIAGQELAKQALQEIVILpsLR-PELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK 412
Cdd:CHL00176   178 TGITFRDIAGIEEAKEEFEEVVSF--LKkPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  413 YVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREG---EHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQE 489
Cdd:CHL00176   256 FVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFK--GNKGVIVIAATNRVDI 333
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  490 LDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLckQGSPLTQK-ELAQLARMTDGYSGSDLTALAKDAALGPIRELKPE 565
Cdd:CHL00176   334 LDAALLRpgRFDRQITVSLPDREGRLDILKVHA--RNKKLSPDvSLELIARRTPGFSGADLANLLNEAAILTARRKKAT 410
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
330-593 1.38e-41

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 161.74  E-value: 1.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  330 IVDNGTAVKFDDIAGQELAKQALQEIVILpsLR-PELFTGL--RAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISA 406
Cdd:COG0465    132 YDEDKPKVTFDDVAGVDEAKEELQEIVDF--LKdPEKFTRLgaKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  407 ASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLlcERREGE-----HDasrrlktE-------FLIEFDGVqsAG 474
Cdd:COG0465    209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV--GRQRGAglgggHD-------EreqtlnqLLVEMDGF--EG 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  475 DDRVLVMGATNRPQELDEAVLR--RFTKRVYVSLPN----EE-----TRllllknllckqGSPLTQK-ELAQLARMTDGY 542
Cdd:COG0465    278 NEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDvkgrEAilkvhAR-----------KKPLAPDvDLEVIARRTPGF 346
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2015239388  543 SGSDLTALAKDAALGPIRELKPEqvknmsasemrnIRLSDFTESLKKI-----KRS 593
Cdd:COG0465    347 SGADLANLVNEAALLAARRNKKA------------VTMEDFEEAIDRViagpeRKS 390
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
341-498 2.40e-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: 149.51  E-value: 2.40e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 419
Cdd:cd19519      1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  420 LVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAvLRRF 498
Cdd:cd19519     81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPA-LRRF 156
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
331-574 8.75e-41

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 156.47  E-value: 8.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  331 VDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELF--TGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAAS 408
Cdd:PTZ00361   174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  409 LTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE----GEHDASRRLkTEFLIEFDGVQSAGDdrVLVMGAT 484
Cdd:PTZ00361   253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatsgGEKEIQRTM-LELLNQLDGFDSRGD--VKVIMAT 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  485 NRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLCKqgspLTQKE---LAQLARMTDGYSGSDLTALAKDAALGPI 559
Cdd:PTZ00361   330 NRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSK----MTLAEdvdLEEFIMAKDELSGADIKAICTEAGLLAL 405
                          250
                   ....*....|....*..
gi 2015239388  560 RE--LKPEQVKNMSASE 574
Cdd:PTZ00361   406 RErrMKVTQADFRKAKE 422
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
349-504 1.58e-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: 143.78  E-value: 1.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  349 KQALQEIVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFA 426
Cdd:cd19530      5 REELTMSILRPIKRPDIYKalGIDLPT-GVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  427 VARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQELDEAVLR--RFTKRVYV 504
Cdd:cd19530     84 RARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE--ERSNVFVIAATNRPDIIDPAMLRpgRLDKTLYV 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
319-560 3.69e-39

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 150.68  E-value: 3.69e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  319 DSNLANLIMNEIVDngtaVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAES 397
Cdd:PTZ00454   128 DSSIQLLQMSEKPD----VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIdPPRGVLLYGPPGTGKTMLAKAVAHHT 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  398 NATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASR---RLKTEFLIEFDGV-QSA 473
Cdd:PTZ00454   204 TATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFdQTT 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  474 GddrVLVMGATNRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLCKQG-SPltQKELAQLARMTDGYSGSDLTAL 550
Cdd:PTZ00454   284 N---VKVIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNlSE--EVDLEDFVSRPEKISAADIAAI 358
                          250
                   ....*....|
gi 2015239388  551 AKDAALGPIR 560
Cdd:PTZ00454   359 CQEAGMQAVR 368
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
349-504 3.37e-38

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: 139.95  E-value: 3.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  349 KQALQEIVILPSLRPELFT--GLrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFA 426
Cdd:cd19528      2 KRELQELVQYPVEHPDKFLkfGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  427 VARELQPSIIFIDEVDSLLCER---REGEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFTKR 501
Cdd:cd19528     81 KARAAAPCVLFFDELDSIAKARggnIGDAGGAADRVINQILTEMDGMNTKKN--VFIIGATNRPDIIDPAILRpgRLDQL 158

                   ...
gi 2015239388  502 VYV 504
Cdd:cd19528    159 IYI 161
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
339-582 4.11e-37

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 149.41  E-value: 4.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  339 FDDIAGQELAKQALQEIVilPSLR-PELFTGL--RAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVG 415
Cdd:PRK10733   151 FADVAGCDEAKEEVAELV--EYLRePSRFQKLggKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  416 EGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE---GEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQELDE 492
Cdd:PRK10733   228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE--GNEGIIVIAATNRPDVLDP 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  493 AVLR--RFTKRVYVSLPNEETRLLLLKNLLCKqgSPL-TQKELAQLARMTDGYSGSDLTALAKDAALGPIR--------- 560
Cdd:PRK10733   306 ALLRpgRFDRQVVVGLPDVRGREQILKVHMRR--VPLaPDIDAAIIARGTPGFSGADLANLVNEAALFAARgnkrvvsmv 383
                          250       260
                   ....*....|....*....|..
gi 2015239388  561 ELKPEQVKNMSASEMRNIRLSD 582
Cdd:PRK10733   384 EFEKAKDKIMMGAERRSMVMTE 405
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
341-502 7.43e-37

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: 136.77  E-value: 7.43e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 418
Cdd:cd19518      1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  419 KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDD--RVLVMGATNRPQELDEAVLR 496
Cdd:cd19518     80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAggPVLVIGATNRPDSLDPALRR 159

                   ....*...
gi 2015239388  497 --RFTKRV 502
Cdd:cd19518    160 agRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
349-504 8.44e-37

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: 136.10  E-value: 8.44e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  349 KQALQEIVILPSLRPELFT-GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAV 427
Cdd:cd19527      2 KKEILDTIQLPLEHPELFSsGLRKRS-GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  428 ARELQPSIIFIDEVDSLLCER-REGEHDASR-RLKTEFLIEFDGVQSAGDDrVLVMGATNRPQELDEAVLR--RFTKRVY 503
Cdd:cd19527     81 ARDAKPCVIFFDELDSLAPSRgNSGDSGGVMdRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLY 159

                   .
gi 2015239388  504 V 504
Cdd:cd19527    160 L 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
348-503 7.37e-35

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 130.63  E-value: 7.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  348 AKQALQEIVILPSLRPELFTGLRAPAR-GLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFA 426
Cdd:cd19526      1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  427 VARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQELDEAVLR--RFTKRVY 503
Cdd:cd19526     81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVE--GLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
114-193 8.49e-33

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


Pssm-ID: 239142  Cd Length: 79  Bit Score: 121.62  E-value: 8.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  114 VRAFHKQAFEYISVALRIDEDekvGQKDQAVEWYKKGIEELEKGIAVVV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 191
Cdd:cd02679      1 IRGYYKQAFEEISKALRADEW---GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQ 77

                   ..
gi 2015239388  192 LL 193
Cdd:cd02679     78 VL 79
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
341-503 2.38e-32

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 123.77  E-value: 2.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNA-----TFFNISAASLTSKYV 414
Cdd:cd19517      1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  415 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAV 494
Cdd:cd19517     81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRG--QVVVIGATNRPDALDPAL 158
                          170
                   ....*....|.
gi 2015239388  495 LR--RFTKRVY 503
Cdd:cd19517    159 RRpgRFDREFY 169
Cation_efflux pfam01545
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
633-829 3.13e-27

Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.


Pssm-ID: 426316 [Multi-domain]  Cd Length: 189  Bit Score: 109.67  E-value: 3.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  633 ALTAYTYLTIFDLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLE-QPEIHTGRL 711
Cdd:pfam01545   17 ALLADAVHSLIDLISSLLALLALRLSRKPPDERFPFGHGRLEPLAALVVGILLLGGGVFLLYESIQRLLSpGEEIDPGLA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  712 LVGTFVALSFNLFTMLSIRNKPFAYvseaastswlqehvadlsrslcgiipglSSIFLPRMNPFVLIDLAGAFALCITYM 791
Cdd:pfam01545   97 LILALVSLLVNLFLLLYLRRAARRI----------------------------RSPALKADALHALSDVLASLGVLISAL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2015239388  792 LIEINNYFA---VDTASAIAIALMTFGTMYPMSVYSGKVLL 829
Cdd:pfam01545  149 LIYLGPITGgllADPLASLLIGLLILYTALRLLKESLSILL 189
CzcD COG1230
Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism];
644-905 8.68e-26

Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism];


Pssm-ID: 440843 [Multi-domain]  Cd Length: 294  Bit Score: 108.67  E-value: 8.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  644 DLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALSFNL 723
Cdd:COG1230     56 DALALGLALFAYRLARRPADARFTFGYKRAEILAALANALLLLVVAGYILYEAIQRLFNPPPVAGGGMLVVAVIGLVVNL 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  724 FTMLSIRnkpfayvseaastswlQEHVADLSrslcgiipgLSSIFLprmnpFVLIDLAGAFALCITYMLIEINNYFAVDT 803
Cdd:COG1230    136 VSAWLLH----------------RGSKHDLN---------LRGAYL-----HVLADALGSVAVIVAALVILFTGWTWLDP 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  804 ASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVigQLDKLIREVSTLDGVLEVRNEHFWTLGFGSLAGSVHVRIRRDANE 883
Cdd:COG1230    186 LLSLLIALLILRSAWGLLRESLRILLEGVPDGI--DLEEVRAALEALPGVADVHDLHVWSLSSGENALTAHVVVDDGADA 263
                          250       260
                   ....*....|....*....|....
gi 2015239388  884 QMVLAHVTNRLYTL--VSTLTVQI 905
Cdd:COG1230    264 DAILDEIRELLAERfgIEHVTIQI 287
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
343-506 1.38e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 100.68  E-value: 1.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  343 AGQELAKQALQEIVILPSLRPelftglrapargLLLFGPPGNGKTMLAKAVAAES---NATFFNISAASLTSKYVGEGEK 419
Cdd:cd00009      1 VGQEEAIEALREALELPPPKN------------LLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  420 ---LVRALFAVARELQPSIIFIDEVDSLlcerREGEHDASRRLKTEFLIEFDGVqsagdDRVLVMGATNRP--QELDEAV 494
Cdd:cd00009     69 ghfLVRLLFELAEKAKPGVLFIDEIDSL----SRGAQNALLRVLETLNDLRIDR-----ENVRVIGATNRPllGDLDRAL 139
                          170
                   ....*....|..
gi 2015239388  495 LRRFTKRVYVSL 506
Cdd:cd00009    140 YDRLDIRIVIPL 151
CDF TIGR01297
cation diffusion facilitator family transporter; This model describes a broadly distributed ...
643-882 4.92e-23

cation diffusion facilitator family transporter; This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273544 [Multi-domain]  Cd Length: 268  Bit Score: 99.99  E-value: 4.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  643 FDLFSLITCLISYWVMMRKPSPAYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLE-QPEIHTGRLLVGTFVALSF 721
Cdd:TIGR01297   27 SDVAASAIALLALRISRRPADERHPFGHGRAEILAALLNGLFLVVVALFILYEAIERLINpEPEIDGGTMLIVAIVGLIV 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  722 NLFtMLSIRNKPFAYVSEAASTSWLQEHVADLSRSLCGIIPGLSSIFlprmnpfvlidlagafalcitymlieinNYFAV 801
Cdd:TIGR01297  107 NLI-LALYLHRVGHRLGSLALRAAALHVLSDALSSVGVLIGALLIYF----------------------------GWHWA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  802 DTASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVigQLDKLIREVSTLDGVLEVRNEHFWTLGFGSLAGSVHVRIRRDA 881
Cdd:TIGR01297  158 DPIAALLISLLILYTAFRLLKESINVLLDAAPDEE--DLEEIKKAILSIPGVKGVHDLHIWRIGPGKLFLDVHVVVDPDL 235

                   .
gi 2015239388  882 N 882
Cdd:TIGR01297  236 D 236
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
374-496 6.32e-20

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: 88.32  E-value: 6.32e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  374 RGLLLFGPPGNGKTMLAKAVAAESNATFFNI-SAASLTSKYVGEGEKLVRALFAVARELQPS--------IIFIDEVDSl 444
Cdd:cd19504     36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDA- 114
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2015239388  445 LCERR------EGEHDAsrrLKTEFLIEFDGVQSAgdDRVLVMGATNRPQELDEAVLR 496
Cdd:cd19504    115 ICKQRgsmagsTGVHDT---VVNQLLSKIDGVEQL--NNILVIGMTNRKDLIDEALLR 167
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
374-502 1.70e-17

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: 80.65  E-value: 1.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  374 RGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG--EKLVRALFAVARELQPSIIFIDEVDSLLCER--R 449
Cdd:cd19506     27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKvpK 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2015239388  450 EGEHDASRRLKTEFLIEFDGVqsAGDDRVLVMGATNRPQELDEAVLRRFTKRV 502
Cdd:cd19506    107 TEKQLDPKRLKKDLPKILKSL--KPEDRVLIVGTTSRPFEADLKSFCKVYNKI 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
372-508 4.92e-17

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 78.95  E-value: 4.92e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388   372 PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-----------------SKYVGEGEKLVRALFAVARELQPS 434
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015239388   435 IIFIDEVDSLLcerregeHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLR-RFTKRVYVSLPN 508
Cdd:smart00382   81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
114-191 4.84e-16

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 73.88  E-value: 4.84e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388   114 VRAFHKQAFEYISVALRIDEdekVGQKDQAVEWYKKGIEELEKGIAVVV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 191
Cdd:smart00745    1 TRDYLSKAKELISKALKADE---AGNYEEALELYKKAIEYLLEGIKVESdsKRREALKAKAAEYLDRAEEIKKSLLERLA 77
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
368-504 4.64e-14

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: 70.86  E-value: 4.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  368 GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLC- 446
Cdd:cd19507     27 GLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSn 105
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  447 ERREGEHDASRRLKTEFLIEFdgvqSAGDDRVLVMGATNRPQELDEAVLR--RFTKRVYV 504
Cdd:cd19507    106 ADSKGDSGTSSRVLGTFLTWL----QEKKKPVFVVATANNVQSLPPELLRkgRFDEIFFV 161
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
370-502 1.15e-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: 63.70  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  370 RAPARGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVARELQPS-IIFIDEVDSL 444
Cdd:cd19512     19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDY-----AIMTGGDVApmgrEGVTAIHKVFDWANTSRRGlLLFVDEADAF 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  445 LCER-REGEHDASRRLKTEFLIEfDGVQSagDDRVLVMgATNRPQELDEAVLRRFTKRV 502
Cdd:cd19512     94 LRKRsTEKISEDLRAALNAFLYR-TGEQS--NKFMLVL-ASNQPEQFDWAINDRIDEMV 148
ycf46 CHL00195
Ycf46; Provisional
337-547 1.16e-11

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 68.51  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  337 VKFDDIAGQELAKQALQeivilpsLRPELFT------GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT 410
Cdd:CHL00195   225 EKISDIGGLDNLKDWLK-------KRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  411 SKYVGEGEKLVRALFAVARELQPSIIFIDEVDsllcerregehdasrrlKTeflieFDGVQSAGD----DRVL------- 479
Cdd:CHL00195   297 GGIVGESESRMRQMIRIAEALSPCILWIDEID-----------------KA-----FSNSESKGDsgttNRVLatfitwl 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  480 --------VMGATNRPQELDEAVLR--RFTKRVYVSLPNEETRLLLLKNLLcKQGSPLTQK--ELAQLARMTDGYSGSDL 547
Cdd:CHL00195   355 sekkspvfVVATANNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHL-QKFRPKSWKkyDIKKLSKLSNKFSGAEI 433
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
116-191 3.38e-11

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 60.02  E-value: 3.38e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015239388  116 AFHKQAFEYISVALRIDEDekvGQKDQAVEWYKKGIEELEKGIAVVV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 191
Cdd:cd02656      1 ELLQQAKELIKQAVKEDED---GNYEEALELYKEALDYLLQALKAEKepKLRKLLRKKVKEYLDRAEFLKELLKKQKQ 75
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
374-497 9.46e-11

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 61.21  E-value: 9.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  374 RGLLLFGPPGNGKTMLAKAVAAESNatfFNISAASLTSkyVGEGEKLVRALFAVARelQPSIIFIDEVDSLLCERregEH 453
Cdd:cd19510     24 RGYLLYGPPGTGKSSFIAALAGELD---YDICDLNLSE--VVLTDDRLNHLLNTAP--KQSIILLEDIDAAFESR---EH 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2015239388  454 DASRRLKTEFL--IEF-------DGVQSaGDDRVLVMgATNRPQELDEAVLRR 497
Cdd:cd19510     94 NKKNPSAYGGLsrVTFsgllnalDGVAS-SEERIVFM-TTNHIERLDPALIRP 144
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
340-445 1.21e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 65.08  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  340 DDIAGQE--LAKQALqeivilpsLRpelftglRAPARG----LLLFGPPGNGKTMLAKAVAAESNATFFNISAasltsky 413
Cdd:COG2256     25 DEVVGQEhlLGPGKP--------LR-------RAIEAGrlssMILWGPPGTGKTTLARLIANATDAEFVALSA------- 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2015239388  414 VGEGEKLVRALFAVAREL----QPSIIFIDEV--------DSLL 445
Cdd:COG2256     83 VTSGVKDIREVIEEARERraygRRTILFVDEIhrfnkaqqDALL 126
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
374-504 4.60e-10

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: 60.15  E-value: 4.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  374 RGLLLFGPPGNGKTMLAKAVAAE---------SNATFFNISAASLTSKYVGEGEKLVRALFAVAREL---QPSIIF--ID 439
Cdd:cd19508     53 RLVLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlID 132
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  440 EVDSLLCER-----REGEHDASRRLKTeFLIEFDGVQSAgdDRVLVMGATNRPQELDEAVLRRFTKRVYV 504
Cdd:cd19508    133 EVESLAAARsasssGTEPSDAIRVVNA-VLTQIDRIKRY--HNNVILLTSNLLEKIDVAFVDRADIKQYI 199
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
338-445 1.56e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 61.25  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  338 KFDDIAGQE--LAK-QALQEIV---ILPSLrpelftglraparglLLFGPPGNGKTMLAKAVAAESNATFFNISAASlts 411
Cdd:PRK13342    10 TLDEVVGQEhlLGPgKPLRRMIeagRLSSM---------------ILWGPPGTGKTTLARIIAGATDAPFEALSAVT--- 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2015239388  412 kyvgEGEKLVRALFAVAREL----QPSIIFIDEV--------DSLL 445
Cdd:PRK13342    72 ----SGVKDLREVIEEARQRrsagRRTILFIDEIhrfnkaqqDALL 113
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
375-498 7.99e-08

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 52.29  E-value: 7.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  375 GLLLFGPPGNGKTMLAKAVAAE-SNATFF------NISAASLTSKYVGEGEKLVRALFAVARELQPS-IIFIDEVD---- 442
Cdd:pfam07728    1 GVLLVGPPGTGKTELAERLAAAlSNRPVFyvqltrDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEINranp 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015239388  443 -------SLLCERREGehdasrrlktefLIEFDGVQSAGDDRVLVMGATNRP----QELDEAVLRRF 498
Cdd:pfam07728   81 dvlnsllSLLDERRLL------------LPDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
342-457 1.02e-07

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 53.15  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  342 IAGQELAKQALQEIVILPSLRPELFTGLR---APaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVGeg 417
Cdd:cd19498     13 IIGQDEAKRAVAIALRNRWRRMQLPEELRdevTP-KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG-- 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2015239388  418 eklvRALFAVARELQPSIIFIDEVDSLLCERREGEHDASR 457
Cdd:cd19498     90 ----RDVESIIRDLVEGIVFIDEIDKIAKRGGSSGPDVSR 125
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
531-585 2.20e-07

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 48.30  E-value: 2.20e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015239388  531 ELAQLARMTDGYSGSDLTALAKDAALGPIRElkpeqvknmsasEMRNIRLSDFTE 585
Cdd:pfam17862    3 DLEELAERTEGFSGADLEALCREAALAALRR------------GLEAVTQEDLEE 45
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
342-442 1.70e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 50.68  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  342 IAGQELAKQALQEIVILPSLRpeLFTGLRAPARGL-------LLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKY 413
Cdd:cd19497     14 VIGQERAKKVLSVAVYNHYKR--IRNNLKQKDDDVeleksniLLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2015239388  414 VGEG-----EKLVR-ALFAVARElQPSIIFIDEVD 442
Cdd:cd19497     92 VGEDvenilLKLLQaADYDVERA-QRGIVYIDEID 125
FieF COG0053
Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];
641-891 2.01e-06

Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];


Pssm-ID: 439823 [Multi-domain]  Cd Length: 284  Bit Score: 50.49  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  641 TIFDLFSLITCLISYWVMMRKPSPAYSFGFERLEVLA-VFASTVLAqLGALFILKESAERFLE-QPEIHTGRLLVGTFVA 718
Cdd:COG0053     38 SLSDLVASLLVLLGLRLAAKPADEEHPYGHGKAEYLAsLIVAVLIL-LAGLFILYEAIERLLHpEPVEPSGLGLAVLLIS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  719 LSFNLFTMLSIRNKPFAYVSEAASTSWLqEHVADLsrslcgiipgLSSIflprmnpFVLIDLAGAFALcitymlieinNY 798
Cdd:COG0053    117 IVVNEALARYLRRVGKKTGSPALKADAL-HDRSDA----------LTSL-------GVLIGLLLALLT----------GW 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  799 FAVDTASAIAIALMTFGTMYPMSVYSGKVLL-QTTPPHVIGQLDKLIREVstlDGVLEVrneHfwtlgfgslagsvHVRI 877
Cdd:COG0053    169 PWLDPIAAILIGLLILKVAYKLARESLSLLMdEALDEELVERIRAIILSV---PGVIGV---H-------------DLRT 229
                          250
                   ....*....|....
gi 2015239388  878 RRDANEQMVLAHVT 891
Cdd:COG0053    230 RKSGPRIFVDLHIE 243
PRK04195 PRK04195
replication factor C large subunit; Provisional
338-444 2.08e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 51.46  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  338 KFDDIAGQELAKQALQEIVilpslrpELFTGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA-----ASLTSK 412
Cdd:PRK04195    12 TLSDVVGNEKAKEQLREWI-------ESWLKGK-PKKALLLYGPPGVGKTSLAHALANDYGWEVIELNAsdqrtADVIER 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2015239388  413 YVGEGEKlVRALFAVARELqpsiIFIDEVDSL 444
Cdd:PRK04195    84 VAGEAAT-SGSLFGARRKL----ILLDEVDGI 110
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
338-441 3.09e-06

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: 48.27  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  338 KFDDIAGQELAKQALqEIVILPslrpelftglrAPARG-----LLLFGPPGNGKTMLAKAVAAESNAtffNISAASltsk 412
Cdd:pfam05496    5 TLDEYIGQEKVKENL-KIFIEA-----------AKQRGealdhVLLYGPPGLGKTTLANIIANEMGV---NIRITS---- 65
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2015239388  413 yvgeGEKLVRA--LFAVARELQP-SIIFIDEV 441
Cdd:pfam05496   66 ----GPAIERPgdLAAILTNLEPgDVLFIDEI 93
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
339-395 3.60e-06

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: 49.07  E-value: 3.60e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  339 FDDIAGQELAKQALqEIvilpslrpelftglrAPARG--LLLFGPPGNGKTMLAKAVAA 395
Cdd:pfam01078    2 LADVKGQEQAKRAL-EI---------------AAAGGhnLLMIGPPGSGKTMLAKRLPG 44
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
365-511 4.69e-06

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: 49.78  E-value: 4.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  365 LFTGLRApaRG-LLLFGPPGNGKTMLAKAVAAESNATFFNIS------AASLT--SKYVGEGEKLV---RALFAvarelq 432
Cdd:COG0714     24 VLIALLA--GGhLLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILgtYIYDQQTGEFEfrpGPLFA------ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  433 pSIIFIDEVDsllceRregehdASRrlKTE-FLIEF--------DGVQSAGDDRVLVMgATNRPQE------LDEAVLRR 497
Cdd:COG0714     96 -NVLLADEIN-----R------APP--KTQsALLEAmeerqvtiPGGTYKLPEPFLVI-ATQNPIEqegtypLPEAQLDR 160
                          170
                   ....*....|....
gi 2015239388  498 FTKRVYVSLPNEET 511
Cdd:COG0714    161 FLLKLYIGYPDAEE 174
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
339-391 6.14e-06

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: 50.04  E-value: 6.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2015239388  339 FDDIAGQELAKQALqEIvilpslrpelftglrAPARG--LLLFGPPGNGKTMLAK 391
Cdd:COG0606    191 LADVKGQEQAKRAL-EI---------------AAAGGhnLLMIGPPGSGKTMLAR 229
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
578-610 2.13e-05

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: 42.87  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2015239388  578 IRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFG 610
Cdd:pfam09336   29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
332-424 2.15e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.04  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  332 DNGTAvKF--DDIAGQELAKQALQEIVILpsLRPELFTGlrapaRGLLLFGPPGNGKTMLAKAVAAE--SNATFFNISAA 407
Cdd:COG1224     29 ENGKA-KFvaDGLVGQVEAREAAGIVVKM--IKEGKMAG-----KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGS 100
                           90
                   ....*....|....*..
gi 2015239388  408 SLTSKYVGEGEKLVRAL 424
Cdd:COG1224    101 EIYSAELKKTEFLMQAL 117
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
342-442 2.63e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 46.02  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  342 IAGQELAKQALQEIVILPSlrpelfTGLRAPARG---LLLFGPPGNGKTMLAKAVAA-----ESNATFFNISAAS----- 408
Cdd:cd19499     13 VVGQDEAVKAVSDAIRRAR------AGLSDPNRPigsFLFLGPTGVGKTELAKALAEllfgdEDNLIRIDMSEYMekhsv 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2015239388  409 -----LTSKYVG--EGEKLVRALfavaRELQPSIIFIDEVD 442
Cdd:cd19499     87 srligAPPGYVGytEGGQLTEAV----RRKPYSVVLLDEIE 123
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
338-444 2.78e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.43  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  338 KFDDIAGQELAKQALqEIVILPSLRpelftglrapaRG-----LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLtsk 412
Cdd:PRK00080    23 SLDEFIGQEKVKENL-KIFIEAAKK-----------RGealdhVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL--- 87
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2015239388  413 yvgegEK---LVrALFAvarELQP-SIIFIDEVDSL 444
Cdd:PRK00080    88 -----EKpgdLA-AILT---NLEEgDVLFIDEIHRL 114
44 PHA02544
clamp loader, small subunit; Provisional
356-466 6.93e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 46.14  E-value: 6.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  356 VILPSLRPELFTGL----RAPArgLLLFGP-PGNGKTMLAKAVAAESNATFFNISAASLTSKYVgeGEKLVRALFAVARE 430
Cdd:PHA02544    23 CILPAADKETFKSIvkkgRIPN--MLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFV--RNRLTRFASTVSLT 98
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2015239388  431 LQPSIIFIDEVDsllcerREGEHDASRRLKTefLIE 466
Cdd:PHA02544    99 GGGKVIIIDEFD------RLGLADAQRHLRS--FME 126
PRK13341 PRK13341
AAA family ATPase;
376-441 6.96e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.97  E-value: 6.96e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015239388  376 LLLFGPPGNGKTMLAKAVAAESNATFFNISAasltskyVGEGEKLVRALFAVAREL-----QPSIIFIDEV 441
Cdd:PRK13341    55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERlerhgKRTILFIDEV 118
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
376-506 7.02e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 43.26  E-value: 7.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  376 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTskyvgegEKLVRALFAVARELQPSIIFIDEVDSLLcerREGEHDA 455
Cdd:cd01120      1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFL-------DTILEAIEDLIEEKKLDIIIIDSLSSLA---RASQGDR 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2015239388  456 SRRLKTEFLIEfdgVQSAGDDRVLVMGATNRPQELDEAVLRRFTKRVYVSL 506
Cdd:cd01120     71 SSELLEDLAKL---LRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSL 118
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
377-442 1.27e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.53  E-value: 1.27e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015239388  377 LLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEG-EK-LVRALFA----VARElQPSIIFIDEVD 442
Cdd:PRK05342   112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEDvENiLLKLLQAadydVEKA-QRGIVYIDEID 183
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
332-424 2.07e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 44.61  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  332 DNGTAVKFDD-IAGQELAKQALQEIVilpslrpELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNAT--FFNISAAS 408
Cdd:pfam06068   15 EDGEARYVSGgLVGQEKAREAAGVIV-------EMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSE 87
                           90
                   ....*....|....*.
gi 2015239388  409 LTSKYVGEGEKLVRAL 424
Cdd:pfam06068   88 VYSLEMKKTEALTQAF 103
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
377-442 2.11e-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: 42.95  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  377 LLFGPPGNGKTMLAKAVAA-----ESNATFFNISA---ASLTSK-------YVG--EGEKLVRALfavaRELQPSIIFID 439
Cdd:pfam07724    7 LFLGPTGVGKTELAKALAEllfgdERALIRIDMSEymeEHSVSRligappgYVGyeEGGQLTEAV----RRKPYSIVLID 82

                   ...
gi 2015239388  440 EVD 442
Cdd:pfam07724   83 EIE 85
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
368-502 3.53e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 44.45  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  368 GLRAP--ARGLLLFGPPGNGKTMLAKAVAAE-------SNATFFNISAASLTSKYVGEGEKLVRALFAVARElqpSIIFI 438
Cdd:TIGR03922  305 GLPVAqtSNHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFL 381
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015239388  439 DEVDSLLcERREGEHDASRRLKTEFLIEFdgvQSAGDDRVLVMGATNRPQ-----ELDEAVLRRFTKRV 502
Cdd:TIGR03922  382 DEAYTLV-ETGYGQKDPFGLEAIDTLLAR---MENDRDRLVVIGAGYRKDldkflEVNEGLRSRFTRVI 446
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
376-444 3.81e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 42.55  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  376 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK---------YVGE--GeKLVRALfAVARELQPsIIFIDEVDSL 444
Cdd:cd19500     40 LCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmpG-RIIQAL-KKAGTNNP-VFLLDEIDKI 116
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
338-444 4.37e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 43.44  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  338 KFDDIAGQELAKQALQeIVILPS-LRPElftglraPARGLLLFGPPGNGKTMLAKAVAAESNAtffNISAASltskyvge 416
Cdd:TIGR00635    2 LLAEFIGQEKVKEQLQ-LFIEAAkMRQE-------ALDHLLLYGPPGLGKTTLAHIIANEMGV---NLKITS-------- 62
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2015239388  417 GEKLVRA--LFAVARELQP-SIIFIDEVDSL 444
Cdd:TIGR00635   63 GPALEKPgdLAAILTNLEEgDVLFIDEIHRL 93
TIGR00368 TIGR00368
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ...
339-391 5.06e-04

Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]


Pssm-ID: 129465 [Multi-domain]  Cd Length: 499  Bit Score: 44.06  E-value: 5.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2015239388  339 FDDIAGQELAKQALqEIVIlpslrpelftglrAPARGLLLFGPPGNGKTMLAK 391
Cdd:TIGR00368  191 LKDIKGQQHAKRAL-EIAA-------------AGGHNLLLFGPPGSGKTMLAS 229
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
336-422 6.62e-04

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 43.05  E-value: 6.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  336 AVKFDDIAGQELAKQALQEIVILPSLRpelftglraparGLLLFGPPGNGKTMLAKAVA-------AESNATFFNISAA- 407
Cdd:PRK12402    11 PALLEDILGQDEVVERLSRAVDSPNLP------------HLLVQGPPGSGKTAAVRALArelygdpWENNFTEFNVADFf 78
                           90
                   ....*....|....*
gi 2015239388  408 SLTSKYVGEGEKLVR 422
Cdd:PRK12402    79 DQGKKYLVEDPRFAH 93
PRK09862 PRK09862
ATP-dependent protease;
341-413 8.60e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 43.04  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  341 DIAGQELAKQALqEIVIlpslrpelftglrAPARGLLLFGPPGNGKTMLAKAV-----------AAESNATFFNISAASL 409
Cdd:PRK09862   192 DVIGQEQGKRGL-EITA-------------AGGHNLLLIGPPGTGKTMLASRIngllpdlsneeALESAAILSLVNAESV 257

                   ....
gi 2015239388  410 TSKY 413
Cdd:PRK09862   258 QKQW 261
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
338-440 1.28e-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: 42.38  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  338 KFDDIAGQELAKQALqEIVILPslrpelftglrAPARG-----LLLFGPPGNGKTMLAKAVAAESNATFFNIS------- 405
Cdd:COG2255     26 RLDEYIGQEKVKENL-KIFIEA-----------AKKRGealdhVLLYGPPGLGKTTLAHIIANEMGVNIRITSgpaiekp 93
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2015239388  406 ---AASLTSkyvgegeklvralfavareLQP-SIIFIDE 440
Cdd:COG2255     94 gdlAAILTN-------------------LEEgDVLFIDE 113
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
377-500 2.66e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 41.75  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015239388  377 LLFGPPGNGKTMLAKAVAAE----------SNATFFNISAASLT--SKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 444
Cdd:PRK11034   211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015239388  445 L--CERREGEHDASRRLKTefliefdgVQSAGddRVLVMGATNRPQ-----ELDEAVLRRFTK 500
Cdd:PRK11034   291 IgaGAASGGQVDAANLIKP--------LLSSG--KIRVIGSTTYQEfsnifEKDRALARRFQK 343
PRK08116 PRK08116
hypothetical protein; Validated
366-396 3.48e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.39  E-value: 3.48e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2015239388  366 FTGLRAPARGLLLFGPPGNGKTMLAKAVAAE 396
Cdd:PRK08116   107 FEEMKKENVGLLLWGSVGTGKTYLAACIANE 137
 
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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