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Conserved domains on  [gi|392919885|ref|NP_001256115|]
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Spastin homolog [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 240-401 1.91e-84

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


The actual alignment was detected with superfamily member cd19524:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 164  Bit Score: 258.24  E-value: 1.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKT 319
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 320 IRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRFPK 399
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                 ..
gi 392919885 400 RI 401
Cdd:cd19524  161 RV 162
cell_div_CdvC super family cl49147
cell division protein CdvC;
175-510 4.26e-62

cell division protein CdvC;


The actual alignment was detected with superfamily member NF041006:

Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 207.66  E-value: 4.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 175 TVHPEPPVQASNRKM--ETVKRVKVDKASLPMHQNPvnraallNGVDKVIGERLLdeVLDNTGVRMDDVAGCHSAKAALE 252
Cdd:NF041006  46 RLYPDSPLRHAYEQMinEYKKRIEVLEELVPAEPAG-------PDVEKESDEELV--VKEKPKVTFSDIVGLEDVKEALK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 253 EAVILPALNPNLFKgLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNA-- 330
Cdd:NF041006 117 EAIVYPSKRPDLFP-LGWP-RGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKsk 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 331 ---QPSIIFIDEIDSIL-CERSEKDAEVsrRMKTEFLVQFDG-ATSSADDRILVIGATNRPHELDDAVLRRFPKRIMLNL 405
Cdd:NF041006 195 eegKPAIIFIDEIDALLgVYSSEVGGEV--RVRNQFLKEMDGlQDKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 406 PDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPIREIDRSKLSMTdgekiRKIRASDFD 485
Cdd:NF041006 273 PDREQRLELLKYYTSKIKLENDV---DLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGEP-----RPITMEDFK 344

                        330       340
                 ....*....|....*....|....*
gi 392919885 486 TALRTIRPSTSQKIMSKLSDFSRSF 510
Cdd:NF041006 345 EVLKIRKPSVNQEMLKAYEAWHEKF 369
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 240-401 1.91e-84

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: 258.24  E-value: 1.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKT 319
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 320 IRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRFPK 399
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                 ..
gi 392919885 400 RI 401
Cdd:cd19524  161 RV 162
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 223-500 4.46e-81

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 255.32  E-value: 4.46e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 223 GERLLDEVLDNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLRqPVKGILLFGPPGNGKTLLAKAVAGESKQMF 300
Cdd:COG1222   62 TPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 301 FNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSE-KDAEVSRRMKTEFLVQFDGATSsaDDRILV 379
Cdd:COG1222  141 IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFES--RGDVLI 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 380 IGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAM 457
Cdd:COG1222  219 IAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDV---DLDKLAKLTEGFSGADLKAIVTEAGM 295

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 392919885 458 VPIReidrsklsmtdgEKIRKIRASDFDTALRTIRPSTSQKIM 500
Cdd:COG1222  296 FAIR------------EGRDTVTMEDLEKAIEKVKKKTETATN 326
cell_div_CdvC NF041006
cell division protein CdvC;
175-510 4.26e-62

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 207.66  E-value: 4.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 175 TVHPEPPVQASNRKM--ETVKRVKVDKASLPMHQNPvnraallNGVDKVIGERLLdeVLDNTGVRMDDVAGCHSAKAALE 252
Cdd:NF041006  46 RLYPDSPLRHAYEQMinEYKKRIEVLEELVPAEPAG-------PDVEKESDEELV--VKEKPKVTFSDIVGLEDVKEALK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 253 EAVILPALNPNLFKgLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNA-- 330
Cdd:NF041006 117 EAIVYPSKRPDLFP-LGWP-RGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKsk 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 331 ---QPSIIFIDEIDSIL-CERSEKDAEVsrRMKTEFLVQFDG-ATSSADDRILVIGATNRPHELDDAVLRRFPKRIMLNL 405
Cdd:NF041006 195 eegKPAIIFIDEIDALLgVYSSEVGGEV--RVRNQFLKEMDGlQDKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 406 PDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPIREIDRSKLSMTdgekiRKIRASDFD 485
Cdd:NF041006 273 PDREQRLELLKYYTSKIKLENDV---DLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGEP-----RPITMEDFK 344

                        330       340
                 ....*....|....*....|....*
gi 392919885 486 TALRTIRPSTSQKIMSKLSDFSRSF 510
Cdd:NF041006 345 EVLKIRKPSVNQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 220-511 3.91e-59

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: 208.22  E-value: 3.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  220 KVIGERLLDEVL-DNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGES 296
Cdd:TIGR01243 433 KMVEPSAIREVLvEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATES 511

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  297 KQMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCER-SEKDAEVSRRMKTEFLVQFDGATSSADd 375
Cdd:TIGR01243 512 GANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDRIVNQLLTEMDGIQELSN- 590

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  376 rILVIGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCK 453
Cdd:TIGR01243 591 -VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDV---DLEELAEMTEGYTGADIEAVCR 666

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392919885  454 EAAMVPIREIDRS----KLSMTDGE--KIRKIRASDFDTALRTIRPSTSQKIMSKLSDFSRSFG 511
Cdd:TIGR01243 667 EAAMAALRESIGSpakeKLEVGEEEflKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 229-483 1.88e-58

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 198.52  E-value: 1.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 229 EVLDNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLrQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISAS 306
Cdd:PRK03992 121 EVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 307 SLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEK----DAEVSRRMkTEFLVQFDGATSSADDRIlvIGA 382
Cdd:PRK03992 200 ELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSgtsgDREVQRTL-MQLLAEMDGFDPRGNVKI--IAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 383 TNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPI 460
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDV---DLEELAELTEGASGADLKAICTEAGMFAI 353

                        250       260
                 ....*....|....*....|....
gi 392919885 461 REiDRSKLSMTDGEK-IRKIRASD 483
Cdd:PRK03992 354 RD-DRTEVTMEDFLKaIEKVMGKE 376
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 275-405 2.07e-50

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: 168.54  E-value: 2.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  275 ILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEV 354
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392919885  355 SRRMKTEFLVQFDGATSSaDDRILVIGATNRPHELDDAVLRRFPKRIMLNL 405
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSS-NSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 273-407 4.89e-18

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: 80.88  E-value: 4.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885   273 KGILLFGPPGNGKTLLAKAVAGESKQM---FFNISASSLTS--------------KWVGDSEKTIRGLFQIARNAQPSII 335
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDVL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392919885   336 FIDEIDSILCERSEKDAEVSRRMKTEFLVQfdgatssADDRILVIGATNRPHELDDAVLR-RFPKRIMLNLPD 407
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 432-475 5.87e-08

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: 49.07  E-value: 5.87e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 392919885  432 DIRYIASNTSGFSNSDLVALCKEAAMVPIREiDRSKLSMTDGEK 475
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRR-GLEAVTQEDLEE 45
flhF PRK05703
flagellar biosynthesis protein FlhF;
105-298 3.37e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 42.96  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 105 VDPNVKQSRSATVGPSRPASAARVTPRPT----RATAPEKKNAAKAKENDENRHVCSRGDRCGAHHQPVTKKSDTVHPEP 180
Cdd:PRK05703  51 VDEDETPKKNPVLREEKRKPAKSILSLQAllekRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 181 PVQASNRKMETVKR-VKVDKASL-PMHQNPVNRAALLN-----GVDKVIGERLLDEVLDNTGVRMDdvagchSAKAALEE 253
Cdd:PRK05703 131 ELDELRDELKELKNlLEDQLSGLrQVERIPPEFAELYKrlkrsGLSPEIAEKLLKLLLEHMPPRER------TAWRYLLE 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392919885 254 AV--ILPALNPNLFKGlrqpvKGIL-LFGPPGNGKT-----LLAKAVAGESKQ 298
Cdd:PRK05703 205 LLanMIPVRVEDILKQ-----GGVVaLVGPTGVGKTttlakLAARYALLYGKK 252
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 240-401 1.91e-84

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: 258.24  E-value: 1.91e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKT 319
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 320 IRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRFPK 399
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                 ..
gi 392919885 400 RI 401
Cdd:cd19524  161 RV 162
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 241-401 3.58e-84

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: 257.28  E-value: 3.58e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 241 VAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTI 320
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 321 RGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRFPKR 400
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                 .
gi 392919885 401 I 401
Cdd:cd19509  161 I 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 223-500 4.46e-81

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 255.32  E-value: 4.46e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 223 GERLLDEVLDNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLRqPVKGILLFGPPGNGKTLLAKAVAGESKQMF 300
Cdd:COG1222   62 TPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 301 FNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSE-KDAEVSRRMKTEFLVQFDGATSsaDDRILV 379
Cdd:COG1222  141 IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFES--RGDVLI 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 380 IGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAM 457
Cdd:COG1222  219 IAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDV---DLDKLAKLTEGFSGADLKAIVTEAGM 295

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 392919885 458 VPIReidrsklsmtdgEKIRKIRASDFDTALRTIRPSTSQKIM 500
Cdd:COG1222  296 FAIR------------EGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 219-403 4.21e-78

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: 242.59  E-value: 4.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 219 DKVIGERLLDEVLD-NTGVRMDDVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESK 297
Cdd:cd19525    1 EPKMIELIMSEIMDhGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 298 QMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRI 377
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 392919885 378 LVIGATNRPHELDDAVLRRFPKRIML 403
Cdd:cd19525  161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 236-401 1.89e-67

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: 214.73  E-value: 1.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 236 VRMDDVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGD 315
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 316 SEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSaDDRILVIGATNRPHELDDAVLR 395
Cdd:cd19521   84 SEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGND-SQGVLVLGATNIPWQLDSAIRR 162


                 ....*.
gi 392919885 396 RFPKRI 401
Cdd:cd19521  163 RFEKRI 168
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 198-472 4.68e-65

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: 216.32  E-value: 4.68e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 198 DKASLPMHQNPVNRAALLNGVDKVIGERLLDEVLDNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLRQPvKGI 275
Cdd:COG0464  116 RALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 276 LLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVS 355
Cdd:COG0464  195 LLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVG 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 356 RRMKTEFLVQFDGATssadDRILVIGATNRPHELDDAVLRRFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRY 435
Cdd:COG0464  275 RRVVNTLLTEMEELR----SDVVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDV---DLEE 347

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 392919885 436 IASNTSGFSNSDLVALCKEAAMVPIReIDRSKLSMTD 472
Cdd:COG0464  348 LAEATEGLSGADIRNVVRRAALQALR-LGREPVTTED 383
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 240-403 3.76e-64

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: 205.74  E-value: 3.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFK--GLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSE 317
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDnsRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 318 KTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRF 397
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 392919885 398 PKRIML 403
Cdd:cd19520  161 PKRFHI 166
cell_div_CdvC NF041006
cell division protein CdvC;
175-510 4.26e-62

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 207.66  E-value: 4.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 175 TVHPEPPVQASNRKM--ETVKRVKVDKASLPMHQNPvnraallNGVDKVIGERLLdeVLDNTGVRMDDVAGCHSAKAALE 252
Cdd:NF041006  46 RLYPDSPLRHAYEQMinEYKKRIEVLEELVPAEPAG-------PDVEKESDEELV--VKEKPKVTFSDIVGLEDVKEALK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 253 EAVILPALNPNLFKgLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNA-- 330
Cdd:NF041006 117 EAIVYPSKRPDLFP-LGWP-RGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKsk 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 331 ---QPSIIFIDEIDSIL-CERSEKDAEVsrRMKTEFLVQFDG-ATSSADDRILVIGATNRPHELDDAVLRRFPKRIMLNL 405
Cdd:NF041006 195 eegKPAIIFIDEIDALLgVYSSEVGGEV--RVRNQFLKEMDGlQDKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 406 PDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPIREIDRSKLSMTdgekiRKIRASDFD 485
Cdd:NF041006 273 PDREQRLELLKYYTSKIKLENDV---DLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGEP-----RPITMEDFK 344

                        330       340
                 ....*....|....*....|....*
gi 392919885 486 TALRTIRPSTSQKIMSKLSDFSRSF 510
Cdd:NF041006 345 EVLKIRKPSVNQEMLKAYEAWHEKF 369
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 240-403 1.33e-61

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: 199.44  E-value: 1.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKT 319
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 320 IRGLFQIARNAQPSIIFIDEIDSILCER-SEKDAEVSRRMKTEFLVQFDGATSSADDR-----ILVIGATNRPHELDDAV 393
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 392919885 394 LRRFPKRIML 403
Cdd:cd19522  161 RRRLEKRIYI 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 220-511 3.91e-59

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: 208.22  E-value: 3.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  220 KVIGERLLDEVL-DNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGES 296
Cdd:TIGR01243 433 KMVEPSAIREVLvEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATES 511

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  297 KQMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCER-SEKDAEVSRRMKTEFLVQFDGATSSADd 375
Cdd:TIGR01243 512 GANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDRIVNQLLTEMDGIQELSN- 590

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  376 rILVIGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCK 453
Cdd:TIGR01243 591 -VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDV---DLEELAEMTEGYTGADIEAVCR 666

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392919885  454 EAAMVPIREIDRS----KLSMTDGE--KIRKIRASDFDTALRTIRPSTSQKIMSKLSDFSRSFG 511
Cdd:TIGR01243 667 EAAMAALRESIGSpakeKLEVGEEEflKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 229-483 1.88e-58

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 198.52  E-value: 1.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 229 EVLDNTGVRMDDVAGCHSAKAALEEAVILPALNPNLFK--GLrQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISAS 306
Cdd:PRK03992 121 EVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 307 SLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEK----DAEVSRRMkTEFLVQFDGATSSADDRIlvIGA 382
Cdd:PRK03992 200 ELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSgtsgDREVQRTL-MQLLAEMDGFDPRGNVKI--IAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 383 TNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPI 460
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDV---DLEELAELTEGASGADLKAICTEAGMFAI 353

                        250       260
                 ....*....|....*....|....
gi 392919885 461 REiDRSKLSMTDGEK-IRKIRASD 483
Cdd:PRK03992 354 RD-DRTEVTMEDFLKaIEKVMGKE 376
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 236-500 1.57e-53

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: 192.43  E-value: 1.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  236 VRMDDVAGCHSAKAALEEAVILPALNPNLFKGLR-QPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVG 314
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  315 DSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSAddRILVIGATNRPHELDDAVL 394
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRG--RVIVIGATNRPDALDPALR 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  395 R--RFPKRIMLNLPDEEARKELitktLKKH--NMmdgLISSDI--RYIASNTSGFSNSDLVALCKEAAMVPIREIDRSKL 468
Cdd:TIGR01243 333 RpgRFDREIVIRVPDKRARKEI----LKVHtrNM---PLAEDVdlDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGK 405

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 392919885  469 SMTDGEKIR-------KIRASDFDTALRTIRPSTSQKIM 500
Cdd:TIGR01243 406 INFEAEEIPaevlkelKVTMKDFMEALKMVEPSAIREVL 444
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 247-401 2.55e-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: 172.08  E-value: 2.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 247 AKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLF 324
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 325 QIARNAQPSIIFIDEIDSILCERS-EKDAEVSRRMKTEFLVQFDGATSSadDRILVIGATNRPHELDDAVLR--RFPKRI 401
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGqSDSSGVTDRVVSQLLTELDGIESL--KGVVVIAATNRPDMIDPALLRpgRLDKLI 157
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 240-401 6.27e-51

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 171.32  E-value: 6.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFK--GLRqPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSE 317
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 318 KTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGAtsSADDRILVIGATNRPHELDDAVLR-- 395
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM--SSRGKVVVIAATNRPDAIDPALRRpg 157


                 ....*.
gi 392919885 396 RFPKRI 401
Cdd:cd19503  158 RFDREV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 275-405 2.07e-50

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: 168.54  E-value: 2.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  275 ILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEV 354
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392919885  355 SRRMKTEFLVQFDGATSSaDDRILVIGATNRPHELDDAVLRRFPKRIMLNL 405
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSS-NSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 225-475 1.41e-49

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: 177.48  E-value: 1.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  225 RLLDEvlDNTGVRMDDVAGCHSAKAALEEAV-ILPalNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFF 301
Cdd:TIGR01241  43 KLLNE--EKPKVTFKDVAGIDEAKEELMEIVdFLK--NPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  302 NISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSekdAEVS----RRMKT--EFLVQFDGATSSadD 375
Cdd:TIGR01241 118 SISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG---AGLGggndEREQTlnQLLVEMDGFGTN--T 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  376 RILVIGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCK 453
Cdd:TIGR01241 193 GVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDV---DLKAVARRTPGFSGADLANLLN 269

                         250       260
                  ....*....|....*....|..
gi 392919885  454 EAAMVPIREiDRSKLSMTDGEK 475
Cdd:TIGR01241 270 EAALLAARK-NKTEITMNDIEE 290
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 247-403 3.50e-49

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 166.30  E-value: 3.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 247 AKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQI 326
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 327 ARNAQPSIIFIDEIDSILCERSE-KDAEVSRRMKTEFLVQFDGATSsaDDRILVIGATNRPHELDDAVLR--RFPKRIML 403
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSsGESGELRRVLNQLLTELDGVNS--RSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 240-403 1.68e-48

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: 164.67  E-value: 1.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKT 319
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 320 IRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSrRMKTEFLVQFDGATSSADDRILVIGATNRPHELDDAVLRRFPK 399
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                 ....
gi 392919885 400 RIML 403
Cdd:cd19523  160 RLLV 163
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
238-497 6.06e-48

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 166.21  E-value: 6.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 238 MDDVAGCHSAKAALEEAVILPALNPNLFKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSE 317
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 318 KTIRGLFQIARNAqPSIIFIDEIDSILCERSEKD--AEVsRRMKTEFLVQFDGATSsaddRILVIGATNRPHELDDAVLR 395
Cdd:COG1223   81 RNLRKLFDFARRA-PCVIFFDEFDAIAKDRGDQNdvGEV-KRVVNALLQELDGLPS----GSVVIAATNHPELLDSALWR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 396 RFPKRIMLNLPDEEARKELITKTLKKhnmMDGLISSDIRYIASNTSGFSNSDLVALCKEAamvpireidRSKLSMTDGEK 475
Cdd:COG1223  155 RFDEVIEFPLPDKEERKEILELNLKK---FPLPFELDLKKLAKKLEGLSGADIEKVLKTA---------LKKAILEDREK 222

                        250       260
                 ....*....|....*....|..
gi 392919885 476 IRKiraSDFDTALRTIRPSTSQ 497
Cdd:COG1223  223 VTK---EDLEEALKQRKERKKE 241
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 239-401 1.88e-45

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: 157.11  E-value: 1.88e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 239 DDVAGCHSAKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDS 316
Cdd:cd19502    3 EDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 317 EKTIRGLFQIARNAQPSIIFIDEIDSILCERSEK----DAEVSRRMkTEFLVQFDGATSSadDRILVIGATNRPHELDDA 392
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSgtggDREVQRTM-LELLNQLDGFDPR--GNIKVIMATNRPDILDPA 158

                        170
                 ....*....|.
gi 392919885 393 VLR--RFPKRI 401
Cdd:cd19502  159 LLRpgRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 247-401 1.73e-43

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 151.49  E-value: 1.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 247 AKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLF 324
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 325 QIARNAQPSIIFIDEIDSILCER-SEKDAEVSRRMKTEFLVQFDGATSSADdrILVIGATNRPHELDDAVLR--RFPKRI 401
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLI 157
ftsH CHL00176
cell division protein; Validated
 233-488 2.19e-42

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 159.83  E-value: 2.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 233 NTGVRMDDVAGCHSAKAALEEAVILPAlNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTS 310
Cdd:CHL00176 177 DTGITFRDIAGIEEAKEEFEEVVSFLK-KPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 311 KWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEK---DAEVSRRMKTEFLVQFDGATSSADdrILVIGATNRPH 387
Cdd:CHL00176 255 MFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKG--VIVIAATNRVD 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 388 ELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDgliSSDIRYIASNTSGFSNSDLVALCKEAAMVPIReidr 465
Cdd:CHL00176 333 ILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSP---DVSLELIARRTPGFSGADLANLLNEAAILTAR---- 405

                        250       260
                 ....*....|....*....|...
gi 392919885 466 sklsmtdgEKIRKIRASDFDTAL 488
Cdd:CHL00176 406 --------RKKATITMKEIDTAI 420
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 240-397 4.55e-42

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 147.97  E-value: 4.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLR-QPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEK 318
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392919885 319 TIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSAddRILVIGATNRPHELDDAvLRRF 397
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPA-LRRF 156
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 236-401 1.52e-41

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 146.61  E-value: 1.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 236 VRMDDVAGCHSAKAALEEAV-ILpaLNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKW 312
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVeFL--KNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 313 VGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEK---DAEVSRRMKTEFLVQFDGATSsaDDRILVIGATNRPHEL 389
Cdd:cd19501   78 VGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGFES--NTGVIVIAATNRPDVL 155

                        170
                 ....*....|....
gi 392919885 390 DDAVLR--RFPKRI 401
Cdd:cd19501  156 DPALLRpgRFDRQV 169
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
225-472 6.29e-40

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 152.11  E-value: 6.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 225 RLLDEvlDNTGVRMDDVAGCHSAKAALEEAV-ILPalNPNLFKGL--RQPvKGILLFGPPGNGKTLLAKAVAGESKQMFF 301
Cdd:COG0465  130 KLYDE--DKPKVTFDDVAGVDEAKEELQEIVdFLK--DPEKFTRLgaKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFF 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 302 NISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSIlcERsekdaevSR----------RMKT--EFLVQFDGA 369
Cdd:COG0465  205 SISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV--GR-------QRgaglggghdeREQTlnQLLVEMDGF 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 370 tsSADDRILVIGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELitktLKKHnmMDGL-ISSDI--RYIASNTSGFS 444
Cdd:COG0465  276 --EGNEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAI----LKVH--ARKKpLAPDVdlEVIARRTPGFS 347

                        250       260
                 ....*....|....*....|....*...
gi 392919885 445 NSDLVALCKEAAMVPIREiDRSKLSMTD 472
Cdd:COG0465  348 GADLANLVNEAALLAARR-NKKAVTMED 374
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
225-477 2.29e-39

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 151.34  E-value: 2.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 225 RLLDEvlDNTGVRMDDVAGCHSAKAALEEAVILpALNPNLFKGLRQPV-KGILLFGPPGNGKTLLAKAVAGESKQMFFNI 303
Cdd:PRK10733 140 RMLTE--DQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIpKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTI 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 304 SASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSE---KDAEVSRRMKTEFLVQFDGAtsSADDRILVI 380
Cdd:PRK10733 217 SGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGF--EGNEGIIVI 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 381 GATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMV 458
Cdd:PRK10733 295 AATNRPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDI---DAAIIARGTPGFSGADLANLVNEAALF 371

                        250
                 ....*....|....*....
gi 392919885 459 PIREiDRSKLSMTDGEKIR 477
Cdd:PRK10733 372 AARG-NKRVVSMVEFEKAK 389
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 239-477 2.89e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 148.00  E-value: 2.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 239 DDVAGCHSAKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDS 316
Cdd:PTZ00361 183 ADIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 317 EKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDA----EVSRRMkTEFLVQFDGATSSADdrILVIGATNRPHELDDA 392
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSggekEIQRTM-LELLNQLDGFDSRGD--VKVIMATNRIESLDPA 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 393 VLR--RFPKRIMLNLPDEEARKELITKTLKKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPIREiDRSKLSM 470
Cdd:PTZ00361 339 LIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDV---DLEEFIMAKDELSGADIKAICTEAGLLALRE-RRMKVTQ 414


                 ....*..
gi 392919885 471 TDGEKIR 477
Cdd:PTZ00361 415 ADFRKAK 421
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 240-403 4.64e-39

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: 139.85  E-value: 4.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLR-QPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEK 318
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGvEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 319 TIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADD--RILVIGATNRPHELDDAVLR- 395
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAggPVLVIGATNRPDSLDPALRRa 160


                 ....*....
gi 392919885 396 -RFPKRIML 403
Cdd:cd19518  161 gRFDREICL 169
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 248-401 3.31e-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: 137.26  E-value: 3.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 248 KAALEEAVILPALNPNLF-KGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQI 326
Cdd:cd19528    2 KRELQELVQYPVEHPDKFlKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392919885 327 ARNAQPSIIFIDEIDSILCERSEKDAE---VSRRMKTEFLVQFDGATSSADdrILVIGATNRPHELDDAVLRrfPKRI 401
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNTKKN--VFIIGATNRPDIIDPAILR--PGRL 155
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 236-461 4.29e-38

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 143.75  E-value: 4.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 236 VRMDDVAGCHSAKAALEEAVILPALNPNLFKGLR-QPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVG 314
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 315 DSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSE----KDAEVsRRMKTEFLVQFDGATSSADdrILVIGATNRPHELD 390
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDaqtgADREV-QRILLELLNQMDGFDQTTN--VKVIMATNRADTLD 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392919885 391 DAVLR--RFPKRIMLNLPDEEaRKELITKTL-KKHNMMDGLissDIRYIASNTSGFSNSDLVALCKEAAMVPIR 461
Cdd:PTZ00454 299 PALLRpgRLDRKIEFPLPDRR-QKRLIFQTItSKMNLSEEV---DLEDFVSRPEKISAADIAAICQEAGMQAVR 368
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 251-399 2.40e-37

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: 134.92  E-value: 2.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 251 LEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIAR 328
Cdd:cd19530    8 LTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRAR 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392919885 329 NAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGAtsSADDRILVIGATNRPHELDDAVLR--RFPK 399
Cdd:cd19530   87 ASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGL--EERSNVFVIAATNRPDIIDPAMLRpgRLDK 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 247-401 2.32e-36

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: 132.17  E-value: 2.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 247 AKAALEEAVILPALNPNLFK--GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLF 324
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFAssPLRLR-SGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392919885 325 QIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSadDRILVIGATNRPHELDDAVLRrfPKRI 401
Cdd:cd19526   80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGL--DGVYVLAATSRPDLIDPALLR--PGRL 152
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 248-403 4.99e-35

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 128.78  E-value: 4.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 248 KAALEEAVILPALNPNLF-KGLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQI 326
Cdd:cd19527    2 KKEILDTIQLPLEHPELFsSGLRKR-SGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 327 ARNAQPSIIFIDEIDSILCER--SEKDAEVSRRMKTEFLVQFDGATSSADDrILVIGATNRPHELDDAVLR--RFPKRIM 402
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLY 159


                 .
gi 392919885 403 L 403
Cdd:cd19527  160 L 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 240-400 3.14e-33

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 124.16  E-value: 3.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEEAVILPALNPNLFKGLR-QPVKGILLFGPPGNGKTLLAKAVA-----GESKQMFFNISASSLTSKWV 313
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 314 GDSEKTIRGLFQIARNAQPSIIFIDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSAddRILVIGATNRPHELDDAv 393
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRG--QVVVIGATNRPDALDPA- 157


                 ....*..
gi 392919885 394 LRRfPKR 400
Cdd:cd19517  158 LRR-PGR 163
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 242-405 3.55e-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: 98.37  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 242 AGCHSAKAALEEAVILPalnpnlfkglrqPVKGILLFGPPGNGKTLLAKAVAGESKQM---FFNISASSLTSKWVGDSEK 318
Cdd:cd00009    1 VGQEEAIEALREALELP------------PPKNLLLYGPPGTGKTTLARAIANELFRPgapFLYLNASDLLEGLVVAELF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 319 ---TIRGLFQIARNAQPSIIFIDEIDSIlcersekdaevSRRMKTEFLVQFDGATSSAD--DRILVIGATNRP--HELDD 391
Cdd:cd00009   69 ghfLVRLLFELAEKAKPGVLFIDEIDSL-----------SRGAQNALLRVLETLNDLRIdrENVRVIGATNRPllGDLDR 137

                        170
                 ....*....|....
gi 392919885 392 AVLRRFPKRIMLNL 405
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 272-401 1.93e-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: 85.62  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 272 VKGILLFGPPGNGKTLLAKAV-----AGESKQmffnISASSLTSKWVGDSEKTIRGLFQIAR--------NAQPSIIFID 338
Cdd:cd19504   35 VKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEeeqrrlgaNSGLHIIIFD 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392919885 339 EIDSILCER--SEKDAEVSRRMKTEFLVQFDGATSSadDRILVIGATNRPHELDDAVLRrfPKRI 401
Cdd:cd19504  111 EIDAICKQRgsMAGSTGVHDTVVNQLLSKIDGVEQL--NNILVIGMTNRKDLIDEALLR--PGRL 171
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 273-407 4.89e-18

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: 80.88  E-value: 4.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885   273 KGILLFGPPGNGKTLLAKAVAGESKQM---FFNISASSLTS--------------KWVGDSEKTIRGLFQIARNAQPSII 335
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDVL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392919885   336 FIDEIDSILCERSEKDAEVSRRMKTEFLVQfdgatssADDRILVIGATNRPHELDDAVLR-RFPKRIMLNLPD 407
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 272-403 3.03e-15

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: 73.33  E-value: 3.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 272 VKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDS--EKTIRGLFQIARNAQPSIIFIDEIDSILCERSE 349
Cdd:cd19506   26 VKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVP 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392919885 350 KDAEVS--RRMKTEfLVQFDGATsSADDRILVIGATNRPHELDDAVLRRFPKRIML 403
Cdd:cd19506  106 KTEKQLdpKRLKKD-LPKILKSL-KPEDRVLIVGTTSRPFEADLKSFCKVYNKIIL 159
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 240-397 3.57e-15

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: 73.17  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 240 DVAGCHSAKAALEE---AVILPALNPNLfkglrQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDS 316
Cdd:cd19507    1 DVGGLDNLKDWLKKrkaAFSKQASAYGL-----PTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 317 EKTIRGLFQIARNAQPSIIFIDEIDSILCERSEK-DAEVSRRMKTEFLVQFDGATSSaddrILVIGATNRPHELDDAVLR 395
Cdd:cd19507   76 ESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKgDSGTSSRVLGTFLTWLQEKKKP----VFVVATANNVQSLPPELLR 151


                 ....
gi 392919885 396 --RF 397
Cdd:cd19507  152 kgRF 155
ycf46 CHL00195
Ycf46; Provisional
 267-444 1.71e-12

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 69.28  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 267 GLRQPvKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEIDSILCE 346
Cdd:CHL00195 255 GLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSN 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 347 -RSEKDAEVSRRMKTEFLVQFDGATSSaddrILVIGATNRPHELDDAVLR--RFPKRIMLNLPDEEARKELITKTLKKHN 423
Cdd:CHL00195 334 sESKGDSGTTNRVLATFITWLSEKKSP----VFVVATANNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKFR 409

                        170       180
                 ....*....|....*....|.
gi 392919885 424 mMDGLISSDIRYIASNTSGFS 444
Cdd:CHL00195 410 -PKSWKKYDIKKLSKLSNKFS 429
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 269-397 1.24e-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: 62.54  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 269 RQPVKGILLFGPPGNGKTLLAKAVAGESKqMFFNISASSLTSKWVGDSEKTIRGLFQIARNAQPS-IIFIDEIDSILCER 347
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSG-MDYAIMTGGDVAPMGREGVTAIHKVFDWANTSRRGlLLFVDEADAFLRKR 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392919885 348 S-EKDAEVSRRMKTEFLVQfdgaTSSADDRILVIGATNRPHELDDAVLRRF 397
Cdd:cd19512   98 StEKISEDLRAALNAFLYR----TGEQSNKFMLVLASNQPEQFDWAINDRI 144
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 273-401 6.74e-10

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: 57.75  E-value: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 273 KGILLFGPPGNGKTLLAKAVAGEskqMFFNISASSLTSkwVGDSEKTIRGLFQIArnAQPSIIFIDEIDSILcerSEKDA 352
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGE---LDYDICDLNLSE--VVLTDDRLNHLLNTA--PKQSIILLEDIDAAF---ESREH 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392919885 353 EVSRRMKTEFL--VQF-------DGATSSaDDRILVIgATNRPHELDDAVLRrfPKRI 401
Cdd:cd19510   94 NKKNPSAYGGLsrVTFsgllnalDGVASS-EERIVFM-TTNHIERLDPALIR--PGRV 147
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 263-403 2.94e-09

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 56.62  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 263 NLFKGLRQPV--KGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTS-KWVG-DSEKTIRGLFQiarnaqpSIIFID 338
Cdd:cd19498   35 QLPEELRDEVtpKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFID 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392919885 339 EIDSILCERSEKDAEVSRR-MKTEFLVQFDGATSSAD------DRILVIGA----TNRPHELDDAVLRRFPKRIML 403
Cdd:cd19498  108 EIDKIAKRGGSSGPDVSREgVQRDLLPIVEGSTVSTKygpvktDHILFIAAgafhVAKPSDLIPELQGRFPIRVEL 183
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 266-488 3.76e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.56  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 266 KGLRQPVKG-----ILLFGPPGNGKTLLAKAVAGESKQMFFNISASSltskwvgDSEKTIRGLFQIARNA----QPSIIF 336
Cdd:PRK13342  25 KPLRRMIEAgrlssMILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 337 IDEIdsilcERSEKDaevsrrmKTEFLVQF--DGatssaddRILVIGAT--NRPHELDDAVLRRfpKRIM-LNLPDEEAR 411
Cdd:PRK13342  98 IDEI-----HRFNKA-------QQDALLPHveDG-------TITLIGATteNPSFEVNPALLSR--AQVFeLKPLSEEDI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 412 KELITKTLKKHNMMDGLISSDIR-YIASntsgFSNSD----LVALckEAAMVPIREIDRSKLSMT----------DGEK- 475
Cdd:PRK13342 157 EQLLKRALEDKERGLVELDDEALdALAR----LANGDarraLNLL--ELAALGVDSITLELLEEAlqkraarydkDGDEh 230

                        250       260
                 ....*....|....*....|
gi 392919885 476 -------IRKIRASDFDTAL 488
Cdd:PRK13342 231 ydlisalHKSIRGSDPDAAL 250
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 275-396 8.43e-09

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: 55.53  E-value: 8.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 275 ILLFGPPGNGKTLLAKAVAGE---------SKQMFFNISASSLTSKWVGDSEKTIRGLFQ-IAR--NAQPSIIF--IDEI 340
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFQkIQEliDDKDALVFvlIDEV 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 341 DSILCERSEKDA--EVSR--RMKTEFLVQFDGATSSadDRILVIGATNRPHELDDAVLRR 396
Cdd:cd19508  135 ESLAAARSASSSgtEPSDaiRVVNAVLTQIDRIKRY--HNNVILLTSNLLEKIDVAFVDR 192
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 275-340 2.79e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 55.83  E-value: 2.79e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 275 ILLFGPPGNGKTLLAKAVAGESKQMFFNISAssltskwVGDSEKTIRGLFQIARNA----QPSIIFIDEI 340
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERraygRRTILFVDEI 114
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 432-475 5.87e-08

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: 49.07  E-value: 5.87e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 392919885  432 DIRYIASNTSGFSNSDLVALCKEAAMVPIREiDRSKLSMTDGEK 475
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRR-GLEAVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 271-392 1.22e-07

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 51.22  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 271 PVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKWV-----------GDSEKTIRGL---FQIARNAQPSIIF 336
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPdfgnddwidgmLILKESLHRLnlqFELAKAMSPCIIW 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392919885 337 IDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSADD--RILVIGATNRPHELDDA 392
Cdd:cd19505   91 IPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSStrNILVIASTHIPQKVDPA 148
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 275-343 1.26e-07

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: 52.99  E-value: 1.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392919885 275 ILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLT-SKWVG-DSEKTIRGLFQIA----RNAQPSIIFIDEIDSI 343
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGeDVENILLKLLQAAdydvERAQRGIVYIDEIDKI 127
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
275-343 2.94e-07

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 52.85  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 275 ILLFGPPGNGKTLLAKAVAgeskQMF---FNIS-ASSLT-SKWVG-DSEKTIRGLFQ-----IARnAQPSIIFIDEIDSI 343
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLA----RILdvpFAIAdATTLTeAGYVGeDVENILLKLLQaadydVEK-AQRGIVYIDEIDKI 185
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 274-397 1.33e-06

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: 47.67  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  274 GILLFGPPGNGKTLLAKAVAG-------ESKQMFFNISASSLTSKW---VGDSEKTIRGLFQIARNAQpsIIFIDEIDsi 343
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAalsnrpvFYVQLTRDTTEEDLFGRRnidPGGASWVDGPLVRAAREGE--IAVLDEIN-- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392919885  344 lceRSEKDAEVS-------RRMKTE---FLVQFdgatssADDRILVIGATNRP----HELDDAVLRRF 397
Cdd:pfam07728  77 ---RANPDVLNSllslldeRRLLLPdggELVKA------APDGFRLIATMNPLdrglNELSPALRSRF 135
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 275-422 2.09e-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: 49.40  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 275 ILLFGPPGNGKTLLAKAVA----GESKQMFFNIS--ASSLTSKWV---GDSEKTIR-G-LFQiarnaqpSIIFIDEIDsi 343
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALAralgLPFIRIQFTPDllPSDILGTYIydqQTGEFEFRpGpLFA-------NVLLADEIN-- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 344 lceRSekDAEV--------SRRmkteflvQF--DGATSSADDRILVIgATNRPHE------LDDAVLRRFPKRIMLNLPD 407
Cdd:COG0714  105 ---RA--PPKTqsalleamEER-------QVtiPGGTYKLPEPFLVI-ATQNPIEqegtypLPEAQLDRFLLKLYIGYPD 171

                        170
                 ....*....|....*
gi 392919885 408 EEARKELITKTLKKH 422
Cdd:COG0714  172 AEEEREILRRHTGRH 186
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 275-343 4.55e-06

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 48.89  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 275 ILLFGPPGNGKTLLAKAVAgeskQMF---FNIS-ASSLT-SKWVG-DSEKTIRGLFQ-----IARnAQPSIIFIDEIDSI 343
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLA----RILdvpFAIAdATTLTeAGYVGeDVENILLKLLQaadydVEK-AERGIIYIDEIDKI 186
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 275-422 1.92e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.88  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  275 ILLFGPPGNGKTLLAKAVAGE---SKQMFFNISASSLTSKW------------VGDSEKTIrgLFQIARNAQPSIIFIDE 339
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHsvsrligappgyVGYEEGGQ--LTEAVRRKPYSIVLIDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  340 IDSIlcersekDAEVSRrmktEFLVQFDGAT-SSADDR------ILVIGATNRpHELDDAVLRRFPKRimlnlPDEEARK 412
Cdd:pfam07724  84 IEKA-------HPGVQN----DLLQILEGGTlTDKQGRtvdfknTLFIMTGNF-GSEKISDASRLGDS-----PDYELLK 146

                         170
                  ....*....|
gi 392919885  413 ELITKTLKKH 422
Cdd:pfam07724 147 EEVMDLLKKG 156
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 268-343 1.70e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 42.55  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 268 LRQPVKG-ILLF-GPPGNGKTLLAKAVAGESKQMFFNISASSLTskwvgdSEKTIRG------------LFQIARNAQPS 333
Cdd:cd19500   31 LKGSMKGpILCLvGPPGVGKTSLGKSIARALGRKFVRISLGGVR------DEAEIRGhrrtyvgampgrIIQALKKAGTN 104

                         90
                 ....*....|..
gi 392919885 334 --IIFIDEIDSI 343
Cdd:cd19500  105 npVFLLDEIDKI 116
flhF PRK05703
flagellar biosynthesis protein FlhF;
105-298 3.37e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 42.96  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 105 VDPNVKQSRSATVGPSRPASAARVTPRPT----RATAPEKKNAAKAKENDENRHVCSRGDRCGAHHQPVTKKSDTVHPEP 180
Cdd:PRK05703  51 VDEDETPKKNPVLREEKRKPAKSILSLQAllekRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 181 PVQASNRKMETVKR-VKVDKASL-PMHQNPVNRAALLN-----GVDKVIGERLLDEVLDNTGVRMDdvagchSAKAALEE 253
Cdd:PRK05703 131 ELDELRDELKELKNlLEDQLSGLrQVERIPPEFAELYKrlkrsGLSPEIAEKLLKLLLEHMPPRER------TAWRYLLE 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392919885 254 AV--ILPALNPNLFKGlrqpvKGIL-LFGPPGNGKT-----LLAKAVAGESKQ 298
Cdd:PRK05703 205 LLanMIPVRVEDILKQ-----GGVVaLVGPTGVGKTttlakLAARYALLYGKK 252
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 467-511 6.18e-04

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: 37.86  E-value: 6.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392919885  467 KLSMTD--GEKI--RKIRASDFDTALRTIRPSTSQKIMSKLSDFSRSFG 511
Cdd:pfam09336  13 EMTWMDipSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 275-340 6.81e-04

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: 40.18  E-value: 6.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  275 ILLFGPPGNGKTLLAKAVAGEskqMFFNI---SASSLTSKwvGDsektirgLFQIARNAQP-SIIFIDEI 340
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANE---MGVNIritSGPAIERP--GD-------LAAILTNLEPgDVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
275-340 1.43e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.88  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392919885 275 ILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLTSKwvGDsektirgLFQIARNAQP-SIIFIDEI 340
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GD-------LAAILTNLEEgDVLFIDEI 111
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 238-294 1.45e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.21  E-value: 1.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392919885  238 MDDVAGCHSAKAALEEAVilpALNPNLfkglrqpvkgiLLFGPPGNGKTLLAKAVAG 294
Cdd:pfam01078   2 LADVKGQEQAKRALEIAA---AGGHNL-----------LMIGPPGSGKTMLAKRLPG 44
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 241-341 4.21e-03

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: 38.31  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 241 VAGCHSAKAALEEAVILPALnpnlfkGLRQPVKGI---LLFGPPGNGKTLLAKAVA-----GESKQMFFNISA------- 305
Cdd:cd19499   13 VVGQDEAVKAVSDAIRRARA------GLSDPNRPIgsfLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEymekhsv 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 392919885 306 SSLTSKWVGDSEKTIRGLF--QIARNAqPSIIFIDEID 341
Cdd:cd19499   87 SRLIGAPPGYVGYTEGGQLteAVRRKP-YSVVLLDEIE 123
PRK04195 PRK04195
replication factor C large subunit; Provisional
 237-343 4.42e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 39.52  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885 237 RMDDVAGCHSAKAALEEAVIlpalnpNLFKGlrQPVKGILLFGPPGNGKTLLAKAVAGEskqMFF-----NIS----ASS 307
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE------SWLKG--KPKKALLLYGPPGVGKTSLAHALAND---YGWevielNASdqrtADV 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 392919885 308 LtSKWVGDSEKTiRGLFQIARnaqpSIIFIDEIDSI 343
Cdd:PRK04195  81 I-ERVAGEAATS-GSLFGARR----KLILLDEVDGI 110
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
273-310 4.45e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.57  E-value: 4.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 392919885 273 KGILLFGPPGNGKTLLAKAVAGE--SKQMFFNISASSLTS 310
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYS 104
PRK13341 PRK13341
AAA family ATPase;
276-340 6.15e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 6.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392919885 276 LLFGPPGNGKTLLAKAVAGESKQMFFNISAsslTSKWVGDSEKTI-RGLFQIARNAQPSIIFIDEI 340
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA---VLAGVKDLRAEVdRAKERLERHGKRTILFIDEV 118
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 275-340 6.58e-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: 38.82  E-value: 6.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392919885  275 ILLFGPPGNGKTLLAKAVAGESKQMFFNISASSLtskwvgdsEKTiRGLFQIARNAQP-SIIFIDEI 340
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL--------EKP-GDLAAILTNLEEgDVLFIDEI 90
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 270-422 7.33e-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: 39.06  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  270 QPVKGILLFGPPGNGKTLLAKAVAGE-------SKQMFFNISASSLTSKWVGDSEKTIRglfQIARNAQPSIIFIDEIDS 342
Cdd:TIGR03922 310 QTSNHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTN---EIIDSALGGVLFLDEAYT 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919885  343 ILCERSEKDAEVSRRMKTEFLVQFDgatsSADDRILVIGATNRPH-----ELDDAVLRRFPKRIMLN--LPDE------- 408
Cdd:TIGR03922 387 LVETGYGQKDPFGLEAIDTLLARME----NDRDRLVVIGAGYRKDldkflEVNEGLRSRFTRVIEFPsySPDElveiarr 462

                         170
                  ....*....|....*.
gi 392919885  409 --EARKELITKTLKKH 422
Cdd:TIGR03922 463 maTERDSVLDDAAADA 478
 
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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