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Conserved domains on  [gi|1393630394|ref|NP_001350804|]
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spastin isoform 4 [Homo sapiens]

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 ...
 310-473 7.67e-111

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: 328.35  E-value: 7.67e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 389
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 390 VRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIK 469
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1393630394 470 RVYV 473
Cdd:cd19524   161 RVYV 164
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 116-194 1.87e-31

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: 116.61  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 116 VRVFHKQAFEYISIALRIDEDekGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQL 193
Cdd:cd02679     1 IRGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQV 78


                  .
gi 1393630394 194 L 194
Cdd:cd02679    79 L 79
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 500-554 4.26e-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: 46.76  E-value: 4.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394 500 ELAQLARMTDGYSGSDLTALAKDAALGPIRElkpeqvknmsasEMRNIRLSDFTE 554
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 ...
 547-579 1.18e-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: 1.18e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1393630394 547 IRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFG 579
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 ...
 310-473 7.67e-111

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: 328.35  E-value: 7.67e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 389
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 390 VRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIK 469
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1393630394 470 RVYV 473
Cdd:cd19524   161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 306-567 1.52e-78

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 251.08  E-value: 1.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 306 VKFDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV 383
Cdd:COG1222    75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 384 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE-GEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEA 462
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDPA 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 463 VLR--RFIKRVYVSLPNEETRLLLLKNLLckQGSPLTQKE-LAQLARMTDGYSGSDLTALAKDAALGPIRELKPEqvknm 539
Cdd:COG1222   232 LLRpgRFDRVIEVPLPDEEAREEILKIHL--RDMPLADDVdLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT----- 304

                         250       260
                  ....*....|....*....|....*...
gi 1393630394 540 sasemrnIRLSDFTESLKKIKRSVSPQT 567
Cdd:COG1222   305 -------VTMEDLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 300-561 6.07e-59

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 201.60  E-value: 6.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 300 VDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAAS 377
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 378 LTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE----GEHDASRRLkTEFLIEFDGVQSAGDdrVLVMGAT 453
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGN--VKIIAAT 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 454 NRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLlckqgsplTQK-------ELAQLARMTDGYSGSDLTALAKDAA 524
Cdd:PRK03992  278 NRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIH--------TRKmnladdvDLEELAELTEGASGADLKAICTEAG 349

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1393630394 525 LGPIRELKPEqvknmsasemrnIRLSDFTESLKKIKR 561
Cdd:PRK03992  350 MFAIRDDRTE------------VTMEDFLKAIEKVMG 374
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 278-582 7.49e-55

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: 198.21  E-value: 7.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 278 KKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGK 355
Cdd:TIGR01243 422 KVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGK 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 356 TMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDA-SRRLKTEFLI 434
Cdd:TIGR01243 501 TLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLT 580

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 435 EFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLCKQgsPLTQK-ELAQLARMTDGY 511
Cdd:TIGR01243 581 EMDGIQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSM--PLAEDvDLEELAEMTEGY 656

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393630394 512 SGSDLTALAKDAALGPIREL-------KPEQVKNMSASEMRnIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTT 582
Cdd:TIGR01243 657 TGADIEAVCREAAMAALRESigspakeKLEVGEEEFLKDLK-VEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 345-475 1.69e-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: 172.78  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 345 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDA 424
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1393630394 425 SRRLKTEFLIEFDGVQSAGdDRVLVMGATNRPQELDEAVLRRFIKRVYVSL 475
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSN-SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 116-194 1.87e-31

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: 116.61  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 116 VRVFHKQAFEYISIALRIDEDekGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQL 193
Cdd:cd02679     1 IRGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQV 78


                  .
gi 1393630394 194 L 194
Cdd:cd02679    79 L 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
116-192 2.81e-16

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 73.88  E-value: 2.81e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394  116 VRVFHKQAFEYISIALriDEDEKGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 192
Cdd:smart00745   1 TRDYLSKAKELISKAL--KADEAGNYEEALELYKKAIEYLLEGIKVESdsKRREALKAKAAEYLDRAEEIKKSLLERLA 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 341-477 3.93e-16

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 75.87  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394  341 PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-----------------SKYVGEGEKLVRALFAVARELQPS 403
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394  404 IIFIDEVDSLLcerregeHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLR-RFIKRVYVSLPN 477
Cdd:smart00382  81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 500-554 4.26e-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: 46.76  E-value: 4.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394 500 ELAQLARMTDGYSGSDLTALAKDAALGPIRElkpeqvknmsasEMRNIRLSDFTE 554
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRR------------GLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 547-579 1.18e-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: 1.18e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1393630394 547 IRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFG 579
Cdd:pfam09336  29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 122-184 5.84e-03

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 35.59  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393630394 122 QAFEYISIAlrIDEDEKGQKEQAVEWYKKGIEELEKGIavivtgQGEQCERARR-LQAKMMTNL 184
Cdd:pfam04212   3 KALELVKKA--VEEDNAGNYEEALELYKEALDYLLLAL------KETKNEERRElLRAKIAEYL 58
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 310-473 7.67e-111

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: 328.35  E-value: 7.67e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 389
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 390 VRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIK 469
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1393630394 470 RVYV 473
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 ...
 311-473 5.58e-98

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: 295.03  E-value: 5.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 311 IAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLV 390
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 391 RALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKR 470
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                  ...
gi 1393630394 471 VYV 473
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; ...
 288-473 2.07e-94

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: 286.88  E-value: 2.07e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 288 DSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN 367
Cdd:cd19525     1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 368 ATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRV 447
Cdd:cd19525    81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                         170       180
                  ....*....|....*....|....*.
gi 1393630394 448 LVMGATNRPQELDEAVLRRFIKRVYV 473
Cdd:cd19525   161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 306-567 1.52e-78

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 251.08  E-value: 1.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 306 VKFDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV 383
Cdd:COG1222    75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 384 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE-GEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEA 462
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDPA 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 463 VLR--RFIKRVYVSLPNEETRLLLLKNLLckQGSPLTQKE-LAQLARMTDGYSGSDLTALAKDAALGPIRELKPEqvknm 539
Cdd:COG1222   232 LLRpgRFDRVIEVPLPDEEAREEILKIHL--RDMPLADDVdLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT----- 304

                         250       260
                  ....*....|....*....|....*...
gi 1393630394 540 sasemrnIRLSDFTESLKKIKRSVSPQT 567
Cdd:COG1222   305 -------VTMEDLEKAIEKVKKKTETAT 325
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 306-473 1.91e-70

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: 224.36  E-value: 1.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 306 VKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGE 385
Cdd:cd19521     4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 386 GEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVqSAGDDRVLVMGATNRPQELDEAVLR 465
Cdd:cd19521    84 SEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGV-GNDSQGVLVLGATNIPWQLDSAIRR 162


                  ....*...
gi 1393630394 466 RFIKRVYV 473
Cdd:cd19521   163 RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 310-473 1.66e-68

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: 218.83  E-value: 1.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELF--TGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 387
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 388 KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRF 467
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                  ....*.
gi 1393630394 468 IKRVYV 473
Cdd:cd19520   161 PKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 310-473 3.94e-65

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: 210.23  E-value: 3.94e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 389
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 390 VRALFAVARELQPSIIFIDEVDSlLCERR--EGEHDASRRLKTEFLIEFDGVQ--SAGDDR---VLVMGATNRPQELDEA 462
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDS-ICSRRgtSEEHEASRRVKSELLVQMDGVGgaSENDDPskmVMVLAATNFPWDIDEA 159

                         170
                  ....*....|.
gi 1393630394 463 VLRRFIKRVYV 473
Cdd:cd19522   160 LRRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 308-560 2.67e-60

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: 205.53  E-value: 2.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 308 FDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGE 385
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 386 GEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQsagdDRVLVMGATNRPQELDEAVLR 465
Cdd:COG0464   235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR----SDVVVIAATNRPDLLDPALLR 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 466 RFIKRVYVSLPNEETRLLLLKNLLckQGSPLTQK-ELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEqvknmsasem 544
Cdd:COG0464   311 RFDEIIFFPLPDAEERLEIFRIHL--RKRPLDEDvDLEELAEATEGLSGADIRNVVRRAALQALRLGREP---------- 378

                         250
                  ....*....|....*.
gi 1393630394 545 rnIRLSDFTESLKKIK 560
Cdd:COG0464   379 --VTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 300-561 6.07e-59

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 201.60  E-value: 6.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 300 VDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAAS 377
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 378 LTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE----GEHDASRRLkTEFLIEFDGVQSAGDdrVLVMGAT 453
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGN--VKIIAAT 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 454 NRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLlckqgsplTQK-------ELAQLARMTDGYSGSDLTALAKDAA 524
Cdd:PRK03992  278 NRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIH--------TRKmnladdvDLEELAELTEGASGADLKAICTEAG 349

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1393630394 525 LGPIRELKPEqvknmsasemrnIRLSDFTESLKKIKR 561
Cdd:PRK03992  350 MFAIRDDRTE------------VTMEDFLKAIEKVMG 374
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 310-473 3.63e-55

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: 3.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 389
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 390 VRALFAVARELQPSIIFIDEVDSLLCERREgEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIK 469
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQDD-EASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                  ....
gi 1393630394 470 RVYV 473
Cdd:cd19523   160 RLLV 163
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 278-582 7.49e-55

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: 198.21  E-value: 7.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 278 KKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGK 355
Cdd:TIGR01243 422 KVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGK 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 356 TMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDA-SRRLKTEFLI 434
Cdd:TIGR01243 501 TLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLT 580

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 435 EFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLCKQgsPLTQK-ELAQLARMTDGY 511
Cdd:TIGR01243 581 EMDGIQELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSM--PLAEDvDLEELAEMTEGY 656

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393630394 512 SGSDLTALAKDAALGPIREL-------KPEQVKNMSASEMRnIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTT 582
Cdd:TIGR01243 657 TGADIEAVCREAAMAALRESigspakeKLEVGEEEFLKDLK-VEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 310-473 4.75e-53

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: 178.25  E-value: 4.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFT--GLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 387
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 388 KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAVLR-- 465
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG--KVVVIAATNRPDAIDPALRRpg 157


                  ....*...
gi 1393630394 466 RFIKRVYV 473
Cdd:cd19503   158 RFDREVEI 165
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 317-473 9.88e-53

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: 177.09  E-value: 9.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 317 AKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAV 396
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 397 ARELQPSIIFIDEVDSLLCER-REGEHDASRRLKTEFLIEFDGVQSagDDRVLVMGATNRPQELDEAVLR--RFIKRVYV 473
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRdSSGESGELRRVLNQLLTELDGVNS--RSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 306-562 2.88e-52

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 190.89  E-value: 2.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 306 VKFDDIAGQDLAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVG 384
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 385 EGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAVL 464
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRG--RVIVIGATNRPDALDPALR 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 465 R--RFIKRVYVSLPNEETRLLLLKNLLckQGSPLTQ-KELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSA 541
Cdd:TIGR01243 333 RpgRFDREIVIRVPDKRARKEILKVHT--RNMPLAEdVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKINFEA 410

                         250       260
                  ....*....|....*....|....*...
gi 1393630394 542 SE-----MRNIRLS--DFTESLKKIKRS 562
Cdd:TIGR01243 411 EEipaevLKELKVTmkDFMEALKMVEPS 438
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 345-475 1.69e-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: 172.78  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 345 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDA 424
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1393630394 425 SRRLKTEFLIEFDGVQSAGdDRVLVMGATNRPQELDEAVLRRFIKRVYVSL 475
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 ...
 317-473 5.41e-51

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: 172.47  E-value: 5.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 317 AKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALF 394
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 395 AVARELQPSIIFIDEVDSLLCER-REGEHDASRRLKTEFLIEFDGVQSAgdDRVLVMGATNRPQELDEAVLR--RFIKRV 471
Cdd:cd19511    80 QKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIESL--KGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                  ..
gi 1393630394 472 YV 473
Cdd:cd19511   158 YV 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 308-473 2.96e-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: 162.89  E-value: 2.96e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 308 FDDIAGQDLAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG 386
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 387 EKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASR---RLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAV 463
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGN--IKVIMATNRPDILDPAL 159

                         170
                  ....*....|..
gi 1393630394 464 LR--RFIKRVYV 473
Cdd:cd19502   160 LRpgRFDRKIEF 171
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 306-473 3.29e-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: 162.79  E-value: 3.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 306 VKFDDIAGQDLAKQALQEIV-ILpsLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYV 383
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVeFL--KNPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 384 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGE---HDASRRLKTEFLIEFDGVQSagDDRVLVMGATNRPQELD 460
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFES--NTGVIVIAATNRPDVLD 156

                         170
                  ....*....|....*
gi 1393630394 461 EAVLR--RFIKRVYV 473
Cdd:cd19501   157 PALLRpgRFDRQVYV 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 301-559 2.11e-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: 170.16  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 301 DNGTAVKFDDIAGQDLAKQALQEIVILpsLR-PELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASL 378
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVDF--LKnPSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 379 TSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREG---EHDASRRLKTEFLIEFDGVQSAgdDRVLVMGATNR 455
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGNDEREQTLNQLLVEMDGFGTN--TGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 456 PQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLckQGSPLTQK-ELAQLARMTDGYSGSDLTALAKDAALGPIRELK 532
Cdd:TIGR01241 203 PDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHA--KNKKLAPDvDLKAVARRTPGFSGADLANLLNEAALLAARKNK 280

                         250       260
                  ....*....|....*....|....*..
gi 1393630394 533 PEqvknmsasemrnIRLSDFTESLKKI 559
Cdd:TIGR01241 281 TE------------ITMNDIEEAIDRV 295
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 317-473 3.59e-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: 159.58  E-value: 3.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 317 AKQALQEIVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALF 394
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 395 AVARELQPSIIFIDEVDSLLCER-REGEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFIKRV 471
Cdd:cd19529    80 RKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLI 157


                  ..
gi 1393630394 472 YV 473
Cdd:cd19529   158 YI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
308-565 1.33e-45

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 161.20  E-value: 1.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 308 FDDIAGQDLAKQALQEIVI--LPSLRPELFtGLrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGE 385
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKelRRRENLRKF-GL-WPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 386 GEKLVRALFAVARELqPSIIFIDEVDSLLCERR-EGEHDASRRLKTEFLIEFDGVQSagddRVLVMGATNRPQELDEAVL 464
Cdd:COG1223    79 TARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGdQNDVGEVKRVVNALLQELDGLPS----GSVVIAATNHPELLDSALW 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 465 RRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLtQKELAQLARMTDGYSGSDLTALAKDAalgpirelkpeqVKNMSASEM 544
Cdd:COG1223   154 RRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTA------------LKKAILEDR 220

                         250       260
                  ....*....|....*....|.
gi 1393630394 545 RNIRLSDFTESLKKIKRSVSP 565
Cdd:COG1223   221 EKVTKEDLEEALKQRKERKKE 241
ftsH CHL00176
cell division protein; Validated
 304-534 3.07e-43

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 163.68  E-value: 3.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 304 TAVKFDDIAGQDLAKQALQEIVILpsLR-PELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK 381
Cdd:CHL00176  178 TGITFRDIAGIEEAKEEFEEVVSF--LKkPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 382 YVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE---GEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQE 458
Cdd:CHL00176  256 FVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigGGNDEREQTLNQLLTEMDGFK--GNKGVIVIAATNRVDI 333

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394 459 LDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLckQGSPLTQK-ELAQLARMTDGYSGSDLTALAKDAALGPIRELKPE 534
Cdd:CHL00176  334 LDAALLRpgRFDRQITVSLPDREGRLDILKVHA--RNKKLSPDvSLELIARRTPGFSGADLANLLNEAAILTARRKKAT 410
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
299-562 1.47e-41

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 158.28  E-value: 1.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 299 IVDNGTAVKFDDIAGQDLAKQALQEIVILpsLR-PELFTGL--RAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISA 375
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIVDF--LKdPEKFTRLgaKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 376 ASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLlcERREGE-----HDasrrlktE-------FLIEFDGVqsAG 443
Cdd:COG0465   209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV--GRQRGAglgggHD-------EreqtlnqLLVEMDGF--EG 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 444 DDRVLVMGATNRPQELDEAVLR--RFIKRVYVSLPN----EE-----TRllllknllckqGSPLTQK-ELAQLARMTDGY 511
Cdd:COG0465   278 NEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDvkgrEAilkvhAR-----------KKPLAPDvDLEVIARRTPGF 346

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1393630394 512 SGSDLTALAKDAALGPIRELKPEqvknmsasemrnIRLSDFTESLKKI-----KRS 562
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 ...
 310-467 2.35e-40

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: 144.12  E-value: 2.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 388
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394 389 LVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAvLRRF 467
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPA-LRRF 156
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 318-473 2.01e-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: 141.47  E-value: 2.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 318 KQALQEIVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFA 395
Cdd:cd19530     5 REELTMSILRPIKRPDIYKalGIDLPT-GVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 396 VARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQELDEAVLR--RFIKRVYV 473
Cdd:cd19530    84 RARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE--ERSNVFVIAATNRPDIIDPAMLRpgRLDKTLYV 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 288-529 2.79e-39

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 148.37  E-value: 2.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 288 DSNLANLIMNEIVDngtaVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAES 366
Cdd:PTZ00454  128 DSSIQLLQMSEKPD----VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIdPPRGVLLYGPPGTGKTMLAKAVAHHT 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 367 NATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASR---RLKTEFLIEFDGV-QSA 442
Cdd:PTZ00454  204 TATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFdQTT 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 443 GddrVLVMGATNRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLCKQG-SPltQKELAQLARMTDGYSGSDLTAL 519
Cdd:PTZ00454  284 N---VKVIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNlSE--EVDLEDFVSRPEKISAADIAAI 358

                         250
                  ....*....|
gi 1393630394 520 AKDAALGPIR 529
Cdd:PTZ00454  359 CQEAGMQAVR 368
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 300-530 8.67e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 148.00  E-value: 8.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 300 VDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELF--TGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAAS 377
Cdd:PTZ00361  174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 378 LTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE----GEHDASRRLkTEFLIEFDGVQSAGDdrVLVMGAT 453
Cdd:PTZ00361  253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatsgGEKEIQRTM-LELLNQLDGFDSRGD--VKVIMAT 329

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394 454 NRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLCKQgSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRE 530
Cdd:PTZ00361  330 NRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKM-TLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRE 407
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 318-473 2.04e-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: 138.80  E-value: 2.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 318 KQALQEIVILPSLRPELFT--GLrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFA 395
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLkfGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 396 VARELQPSIIFIDEVDSLLCER---REGEHDASRRLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAVLR--RFIKR 470
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARggnIGDAGGAADRVINQILTEMDGMNTKKN--VFIIGATNRPDIIDPAILRpgRLDQL 158


                  ...
gi 1393630394 471 VYV 473
Cdd:cd19528   159 IYI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 310-466 1.54e-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: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 387
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 388 KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDD--RVLVMGATNRPQELDEAvLR 465
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAggPVLVIGATNRPDSLDPA-LR 158


                  .
gi 1393630394 466 R 466
Cdd:cd19518   159 R 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
308-551 1.75e-37

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 147.49  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 308 FDDIAGQDLAKQALQEIVilPSLR-PELFTGL--RAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVG 384
Cdd:PRK10733  151 FADVAGCDEAKEEVAELV--EYLRePSRFQKLggKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 385 EGEKLVRALFAVARELQPSIIFIDEVDSLLCERRE---GEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQELDE 461
Cdd:PRK10733  228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE--GNEGIIVIAATNRPDVLDP 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 462 AVLR--RFIKRVYVSLPNEETRLLLLKNLLCKqgSPL-TQKELAQLARMTDGYSGSDLTALAKDAALGPIR--------- 529
Cdd:PRK10733  306 ALLRpgRFDRQVVVGLPDVRGREQILKVHMRR--VPLaPDIDAAIIARGTPGFSGADLANLVNEAALFAARgnkrvvsmv 383

                         250       260
                  ....*....|....*....|..
gi 1393630394 530 ELKPEQVKNMSASEMRNIRLSD 551
Cdd:PRK10733  384 EFEKAKDKIMMGAERRSMVMTE 405
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 318-473 1.07e-36

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: 134.18  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 318 KQALQEIVILPSLRPELFT-GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAV 396
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSsGLRKRS-GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 397 ARELQPSIIFIDEVDSLLCER-REGEHDASR-RLKTEFLIEFDGVQSAGDDrVLVMGATNRPQELDEAVLR--RFIKRVY 472
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRgNSGDSGGVMdRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLY 159


                  .
gi 1393630394 473 V 473
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 ...
 317-472 3.87e-35

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 129.86  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 317 AKQALQEIVILPSLRPELFTGLRAPAR-GLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFA 395
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394 396 VARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQsaGDDRVLVMGATNRPQELDEAVLR--RFIKRVY 472
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVE--GLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 310-472 2.48e-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: 122.23  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALQEIVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNA-----TFFNISAASLTSKYV 383
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 384 GEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGddRVLVMGATNRPQELDEAV 463
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRG--QVVVIGATNRPDALDPAL 158

                         170
                  ....*....|.
gi 1393630394 464 LR--RFIKRVY 472
Cdd:cd19517   159 RRpgRFDREFY 169
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 116-194 1.87e-31

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: 116.61  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 116 VRVFHKQAFEYISIALRIDEDekGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQL 193
Cdd:cd02679     1 IRGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQV 78


                  .
gi 1393630394 194 L 194
Cdd:cd02679    79 L 79
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 312-475 3.31e-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: 98.76  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 312 AGQDLAKQALQEIVILPSLRPelftglrapargLLLFGPPGNGKTMLAKAVAAES---NATFFNISAASLTSKYVGEGEK 388
Cdd:cd00009     1 VGQEEAIEALREALELPPPKN------------LLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 389 ---LVRALFAVARELQPSIIFIDEVDSLlcerREGEHDASRRLKTEFLIEFDGVqsagdDRVLVMGATNRP--QELDEAV 463
Cdd:cd00009    69 ghfLVRLLFELAEKAKPGVLFIDEIDSL----SRGAQNALLRVLETLNDLRIDR-----ENVRVIGATNRPllGDLDRAL 139

                         170
                  ....*....|..
gi 1393630394 464 LRRFIKRVYVSL 475
Cdd:cd00009   140 YDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 343-465 1.37e-19

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: 86.39  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 343 RGLLLFGPPGNGKTMLAKAVAAESNATFFNI-SAASLTSKYVGEGEKLVRALFAVARELQPS--------IIFIDEVDSl 413
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDA- 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1393630394 414 LCERR------EGEHDAsrrLKTEFLIEFDGVQSAGDdrVLVMGATNRPQELDEAVLR 465
Cdd:cd19504   115 ICKQRgsmagsTGVHDT---VVNQLLSKIDGVEQLNN--ILVIGMTNRKDLIDEALLR 167
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 343-471 1.74e-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: 79.88  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 343 RGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG--EKLVRALFAVARELQPSIIFIDEVDSLLCER--R 418
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKvpK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393630394 419 EGEHDASRRLKTEFLIEFDGVqsAGDDRVLVMGATNRPQELDEAVLRRFIKRV 471
Cdd:cd19506   107 TEKQLDPKRLKKDLPKILKSL--KPEDRVLIVGTTSRPFEADLKSFCKVYNKI 157
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
116-192 2.81e-16

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 73.88  E-value: 2.81e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394  116 VRVFHKQAFEYISIALriDEDEKGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 192
Cdd:smart00745   1 TRDYLSKAKELISKAL--KADEAGNYEEALELYKKAIEYLLEGIKVESdsKRREALKAKAAEYLDRAEEIKKSLLERLA 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 341-477 3.93e-16

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 75.87  E-value: 3.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394  341 PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-----------------SKYVGEGEKLVRALFAVARELQPS 403
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394  404 IIFIDEVDSLLcerregeHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLR-RFIKRVYVSLPN 477
Cdd:smart00382  81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 337-467 5.87e-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: 69.70  E-value: 5.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 337 GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLC- 415
Cdd:cd19507    27 GLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSn 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1393630394 416 ERREGEHDASRRLKTEFLIEFdgvqSAGDDRVLVMGATNRPQELDEAVLR--RF 467
Cdd:cd19507   106 ADSKGDSGTSSRVLGTFLTWL----QEKKKPVFVVATANNVQSLPPELLRkgRF 155
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 118-192 4.15e-13

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: 64.64  E-value: 4.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393630394 118 VFHKQAFEYISIAlrIDEDEKGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 192
Cdd:cd02656     1 ELLQQAKELIKQA--VKEDEDGNYEEALELYKEALDYLLQALKAEKepKLRKLLRKKVKEYLDRAEFLKELLKKQKQ 75
ycf46 CHL00195
Ycf46; Provisional
 306-516 1.22e-11

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 66.97  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 306 VKFDDIAGQDLAKQALQeivilpsLRPELFT------GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT 379
Cdd:CHL00195  225 EKISDIGGLDNLKDWLK-------KRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 380 SKYVGEGEKLVRALFAVARELQPSIIFIDEVDsllcerregehdasrrlKTeflieFDGVQSAGD----DRVL------- 448
Cdd:CHL00195  297 GGIVGESESRMRQMIRIAEALSPCILWIDEID-----------------KA-----FSNSESKGDsgttNRVLatfitwl 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 449 --------VMGATNRPQELDEAVLR--RFIKRVYVSLPNEETRLLLLKNLLcKQGSPLTQK--ELAQLARMTDGYSGSDL 516
Cdd:CHL00195  355 sekkspvfVVATANNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHL-QKFRPKSWKkyDIKKLSKLSNKFSGAEI 433
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 339-467 2.30e-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: 62.16  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 339 RAPARGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVARELQPS-IIFIDEVDSL 413
Cdd:cd19512    19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDY-----AIMTGGDVApmgrEGVTAIHKVFDWANTSRRGlLLFVDEADAF 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394 414 LCER-REGEHDASRRLKTEFLIEfDGVQSagDDRVLVMgATNRPQELDEAVLRRF 467
Cdd:cd19512    94 LRKRsTEKISEDLRAALNAFLYR-TGEQS--NKFMLVL-ASNQPEQFDWAINDRI 144
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 343-466 4.94e-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: 4.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 343 RGLLLFGPPGNGKTMLAKAVAAESNatfFNISAASLTSkyVGEGEKLVRALFAVARelQPSIIFIDEVDSLLCERregEH 422
Cdd:cd19510    24 RGYLLYGPPGTGKSSFIAALAGELD---YDICDLNLSE--VVLTDDRLNHLLNTAP--KQSIILLEDIDAAFESR---EH 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393630394 423 DASRRLKTEFL--IEF-------DGVQSaGDDRVLVMgATNRPQELDEAVLRR 466
Cdd:cd19510    94 NKKNPSAYGGLsrVTFsgllnalDGVAS-SEERIVFM-TTNHIERLDPALIRP 144
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 309-414 1.54e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 309 DDIAGQD--LAKQALqeivilpsLRpelftglRAPARG----LLLFGPPGNGKTMLAKAVAAESNATFFNISAasltsky 382
Cdd:COG2256    25 DEVVGQEhlLGPGKP--------LR-------RAIEAGrlssMILWGPPGTGKTTLARLIANATDAEFVALSA------- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1393630394 383 VGEGEKLVRALFAVAREL----QPSIIFIDEV--------DSLL 414
Cdd:COG2256    83 VTSGVKDIREVIEEARERraygRRTILFVDEIhrfnkaqqDALL 126
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 343-473 4.76e-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: 59.38  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 343 RGLLLFGPPGNGKTMLAKAVAAE---------SNATFFNISAASLTSKYVGEGEKLVRALFAVAREL---QPSIIF--ID 408
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlID 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 409 EVDSLLCER-----REGEHDASRRLKTeFLIEFDGVQSAgdDRVLVMGATNRPQELDEAVLRRFIKRVYV 473
Cdd:cd19508   133 EVESLAAARsasssGTEPSDAIRVVNA-VLTQIDRIKRY--HNNVILLTSNLLEKIDVAFVDRADIKQYI 199
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 345-538 9.87e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.87  E-value: 9.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 345 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASltskyvgEGEKLVRALFAVAREL----QPSIIFIDEV--------DS 412
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEIhrfnkaqqDA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 413 LLcerregEHdasrrlkteflIEfdgvqsagDDRVLVMGAT--------NRP----------QELDEAVLRRFIKRVyvs 474
Cdd:PRK13342  112 LL------PH-----------VE--------DGTITLIGATtenpsfevNPAllsraqvfelKPLSEEDIEQLLKRA--- 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393630394 475 LPNEEtrllllknllcKQGSPLTQKELAQLARMTDGysgsD----LTALakDAALGPIRELKPEQVKN 538
Cdd:PRK13342  164 LEDKE-----------RGLVELDDEALDALARLANG----DarraLNLL--ELAALGVDSITLELLEE 214
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 344-467 5.49e-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: 51.91  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 344 GLLLFGPPGNGKTMLAKAVAAE-SNATFF------NISAASLTSKYVGEGEKLVRALFAVARELQPS-IIFIDEVD---- 411
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFyvqltrDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEINranp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393630394 412 -------SLLCERREGehdasrrlktefLIEFDGVQSAGDDRVLVMGATNRP----QELDEAVLRRF 467
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 ...
 311-426 1.22e-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: 52.00  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 311 IAGQDLAKQALQEIVILPSLRPELFTGLRAPA--RGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVGege 387
Cdd:cd19498    13 IIGQDEAKRAVAIALRNRWRRMQLPEELRDEVtpKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG--- 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1393630394 388 klvRALFAVARELQPSIIFIDEVDSLLCERREGEHDASR 426
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 ...
 500-554 4.26e-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: 46.76  E-value: 4.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394 500 ELAQLARMTDGYSGSDLTALAKDAALGPIRElkpeqvknmsasEMRNIRLSDFTE 554
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 ...
 311-411 1.97e-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: 49.52  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 311 IAGQDLAKQALQEIVILPSLRpeLFTGLRAPARGL-------LLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKY 382
Cdd:cd19497    14 VIGQERAKKVLSVAVYNHYKR--IRNNLKQKDDDVeleksniLLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1393630394 383 VGEG-----EKLVR-ALFAVARElQPSIIFIDEVD 411
Cdd:cd19497    92 VGEDvenilLKLLQaADYDVERA-QRGIVYIDEID 125
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 307-410 2.69e-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: 47.49  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 307 KFDDIAGQDLAKQALqEIVILPslrpelftglrAPARG-----LLLFGPPGNGKTMLAKAVAAESNAtffNISAASltsk 381
Cdd:pfam05496   5 TLDEYIGQEKVKENL-KIFIEA-----------AKQRGealdhVLLYGPPGLGKTTLANIIANEMGV---NIRITS---- 65

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1393630394 382 yvgeGEKLVRA--LFAVARELQP-SIIFIDEV 410
Cdd:pfam05496  66 ----GPAIERPgdLAAILTNLEPgDVLFIDEI 93
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 334-480 3.14e-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: 49.01  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 334 LFTGLRApaRG-LLLFGPPGNGKTMLAKAVAAESNATFFNIS------AASLT--SKYVGEGEKLV---RALFAvarelq 401
Cdd:COG0714    24 VLIALLA--GGhLLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILgtYIYDQQTGEFEfrpGPLFA------ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 402 pSIIFIDEVDsllceRregehdASRrlKTE-FLIEF--------DGVQSAGDDRVLVMgATNRPQE------LDEAVLRR 466
Cdd:COG0714    96 -NVLLADEIN-----R------APP--KTQsALLEAmeerqvtiPGGTYKLPEPFLVI-ATQNPIEqegtypLPEAQLDR 160

                         170
                  ....*....|....
gi 1393630394 467 FIKRVYVSLPNEET 480
Cdd:COG0714   161 FLLKLYIGYPDAEE 174
PRK04195 PRK04195
replication factor C large subunit; Provisional
 307-413 5.15e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.15  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 307 KFDDIAGQDLAKQALQEIVilpslrpELFTGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA-----ASLTSK 381
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWI-------ESWLKGK-PKKALLLYGPPGVGKTSLAHALANDYGWEVIELNAsdqrtADVIER 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1393630394 382 YVGEGEKlVRALFAVARELqpsiIFIDEVDSL 413
Cdd:PRK04195   84 VAGEAAT-SGSLFGARRKL----ILLDEVDGI 110
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 308-364 6.90e-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: 47.14  E-value: 6.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1393630394 308 FDDIAGQDLAKQALqEIvilpslrpelftglrAPARG--LLLFGPPGNGKTMLAKAVAA 364
Cdd:pfam01078   2 LADVKGQEQAKRAL-EI---------------AAAGGhnLLMIGPPGSGKTMLAKRLPG 44
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 311-411 9.86e-06

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: 46.40  E-value: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 311 IAGQDLAKQALQEIVILPSlrpelfTGLRAPARG---LLLFGPPGNGKTMLAKAVAA-----ESNATFFNISAAS----- 377
Cdd:cd19499    13 VVGQDEAVKAVSDAIRRAR------AGLSDPNRPigsFLFLGPTGVGKTELAKALAEllfgdEDNLIRIDMSEYMekhsv 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1393630394 378 -----LTSKYVG--EGEKLVRALfavaRELQPSIIFIDEVD 411
Cdd:cd19499    87 srligAPPGYVGytEGGQLTEAV----RRKPYSVVLLDEIE 123
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 547-579 1.18e-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: 1.18e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1393630394 547 IRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFG 579
Cdd:pfam09336  29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 308-360 1.52e-05

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 47.73  E-value: 1.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393630394 308 FDDIAGQDLAKQALqEIvilpslrpelftglrAPARG--LLLFGPPGNGKTMLAK 360
Cdd:COG0606   191 LADVKGQEQAKRAL-EI---------------AAAGGhnLLMIGPPGSGKTMLAR 229
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
307-413 2.88e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.28  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 307 KFDDIAGQDLAKQALqEIVILPSLRpelftglrapaRG-----LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLtsk 381
Cdd:PRK00080   23 SLDEFIGQEKVKENL-KIFIEAAKK-----------RGealdhVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL--- 87

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1393630394 382 yvgegEK---LVrALFAvarELQP-SIIFIDEVDSL 413
Cdd:PRK00080   88 -----EKpgdLA-AILT---NLEEgDVLFIDEIHRL 114
44 PHA02544
clamp loader, small subunit; Provisional
 325-435 3.38e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 46.14  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 325 VILPSLRPELFTGL----RAPArgLLLFGP-PGNGKTMLAKAVAAESNATFFNISAASLTSKYVgeGEKLVRALFAVARE 399
Cdd:PHA02544   23 CILPAADKETFKSIvkkgRIPN--MLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFV--RNRLTRFASTVSLT 98

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1393630394 400 LQPSIIFIDEVDsllcerREGEHDASRRLKTefLIE 435
Cdd:PHA02544   99 GGGKVIIIDEFD------RLGLADAQRHLRS--FME 126
PRK13341 PRK13341
AAA family ATPase;
345-410 5.32e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.20  E-value: 5.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393630394 345 LLLFGPPGNGKTMLAKAVAAESNATFFNISAasltskyVGEGEKLVRALFAVAREL-----QPSIIFIDEV 410
Cdd:PRK13341   55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERlerhgKRTILFIDEV 118
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
346-411 9.31e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.15  E-value: 9.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393630394 346 LLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEG-EK-LVRALFA----VARElQPSIIFIDEVD 411
Cdd:PRK05342  112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEDvENiLLKLLQAadydVEKA-QRGIVYIDEID 183
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
301-393 1.45e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 301 DNGTAvKF--DDIAGQDLAKQALQEIVilpslrpELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAE--SNATFFNISAA 376
Cdd:COG1224    29 ENGKA-KFvaDGLVGQVEAREAAGIVV-------KMIKEGKMAGKGILIVGPPGTGKTALAVAIARElgEDTPFVAISGS 100

                          90
                  ....*....|....*..
gi 1393630394 377 SLTSKYVGEGEKLVRAL 393
Cdd:COG1224   101 EIYSAELKKTEFLMQAL 117
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 345-475 1.57e-04

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: 41.72  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 345 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTskyvgegEKLVRALFAVARELQPSIIFIDEVDSLLcerREGEHDA 424
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFL-------DTILEAIEDLIEEKKLDIIIIDSLSSLA---RASQGDR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1393630394 425 SRRLKTEFLIEfdgVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSL 475
Cdd:cd01120    71 SSELLEDLAKL---LRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSL 118
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 346-411 2.07e-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: 42.18  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 346 LLFGPPGNGKTMLAKAVAA-----ESNATFFNISA---ASLTSK-------YVG--EGEKLVRALfavaRELQPSIIFID 408
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAEllfgdERALIRIDMSEymeEHSVSRligappgYVGyeEGGQLTEAV----RRKPYSIVLID 82


                  ...
gi 1393630394 409 EVD 411
Cdd:pfam07724  83 EIE 85
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 345-413 3.03e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.78  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 345 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK---------YVGE--GeKLVRALfAVARELQPsIIFIDEVDSL 413
Cdd:cd19500    40 LCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmpG-RIIQAL-KKAGTNNP-VFLLDEIDKI 116
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
 305-391 4.62e-04

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 42.67  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 305 AVKFDDIAGQDLAKQALQEIVILPSLRpelftglraparGLLLFGPPGNGKTMLAKAVA-------AESNATFFNISAA- 376
Cdd:PRK12402   11 PALLEDILGQDEVVERLSRAVDSPNLP------------HLLVQGPPGSGKTAAVRALArelygdpWENNFTEFNVADFf 78

                          90
                  ....*....|....*
gi 1393630394 377 SLTSKYVGEGEKLVR 391
Cdd:PRK12402   79 DQGKKYLVEDPRFAH 93
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 301-393 7.88e-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: 41.91  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 301 DNGTAVKFDD-IAGQDLAKQALQEIVilpslrpELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNAT--FFNISAAS 377
Cdd:pfam06068  15 EDGEARYVSGgLVGQEKAREAAGVIV-------EMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSE 87

                          90
                  ....*....|....*.
gi 1393630394 378 LTSKYVGEGEKLVRAL 393
Cdd:pfam06068  88 VYSLEMKKTEALTQAF 103
PRK09862 PRK09862
ATP-dependent protease;
310-382 9.66e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 41.89  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 310 DIAGQDLAKQALqEIVIlpslrpelftglrAPARGLLLFGPPGNGKTMLAKAV-----------AAESNATFFNISAASL 378
Cdd:PRK09862  192 DVIGQEQGKRGL-EITA-------------AGGHNLLLIGPPGTGKTMLASRIngllpdlsneeALESAAILSLVNAESV 257


                  ....
gi 1393630394 379 TSKY 382
Cdd:PRK09862  258 QKQW 261
TIGR00368 TIGR00368
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ...
 308-360 1.12e-03

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: 41.75  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393630394 308 FDDIAGQDLAKQALqEIVIlpslrpelftglrAPARGLLLFGPPGNGKTMLAK 360
Cdd:TIGR00368 191 LKDIKGQQHAKRAL-EIAA-------------AGGHNLLLFGPPGSGKTMLAS 229
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 307-409 1.49e-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: 40.83  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 307 KFDDIAGQDLAKQALqEIVILPslrpelftglrAPARG-----LLLFGPPGNGKTMLAKAVAAESNATFFNIS------- 374
Cdd:COG2255    26 RLDEYIGQEKVKENL-KIFIEA-----------AKKRGealdhVLLYGPPGLGKTTLAHIIANEMGVNIRITSgpaiekp 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1393630394 375 ---AASLTSkyvgegeklvralfavareLQP-SIIFIDE 409
Cdd:COG2255    94 gdlAAILTN-------------------LEEgDVLFIDE 113
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 337-423 1.54e-03

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 41.37  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 337 GLRAP--ARGLLLFGPPGNGKTMLAKAVAAE-------SNATFFNISAASLTSKYVGEGEKLVRALFAVARElqpSIIFI 407
Cdd:TIGR03922 305 GLPVAqtSNHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFL 381

                          90
                  ....*....|....*.
gi 1393630394 408 DEVDSLLcERREGEHD 423
Cdd:TIGR03922 382 DEAYTLV-ETGYGQKD 396
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 307-413 1.74e-03

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: 40.75  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 307 KFDDIAGQDLAKQALQEIVILPSLRPElftglraPARGLLLFGPPGNGKTMLAKAVAAESNAtffNISAASltskyvgeG 386
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQE-------ALDHLLLYGPPGLGKTTLAHIIANEMGV---NLKITS--------G 63

                          90       100       110
                  ....*....|....*....|....*....|
gi 1393630394 387 EKLVRA--LFAVARELQP-SIIFIDEVDSL 413
Cdd:TIGR00635  64 PALEKPgdLAAILTNLEEgDVLFIDEIHRL 93
PRK08116 PRK08116
hypothetical protein; Validated
 335-365 2.47e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.00  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1393630394 335 FTGLRAPARGLLLFGPPGNGKTMLAKAVAAE 365
Cdd:PRK08116  107 FEEMKKENVGLLLWGSVGTGKTYLAACIANE 137
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 122-184 5.84e-03

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 35.59  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393630394 122 QAFEYISIAlrIDEDEKGQKEQAVEWYKKGIEELEKGIavivtgQGEQCERARR-LQAKMMTNL 184
Cdd:pfam04212   3 KALELVKKA--VEEDNAGNYEEALELYKEALDYLLLAL------KETKNEERRElLRAKIAEYL 58
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 346-469 7.07e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.43  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393630394 346 LLFGPPGNGKTMLAKAVAAE----------SNATFFNISAASLT--SKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 413
Cdd:PRK11034  211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393630394 414 L--CERREGEHDASRRLKTefliefdgVQSAGddRVLVMGATNRPQ-----ELDEAVLRRFIK 469
Cdd:PRK11034  291 IgaGAASGGQVDAANLIKP--------LLSSG--KIRVIGSTTYQEfsnifEKDRALARRFQK 343
 
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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