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Conserved domains on  [gi|15220930|ref|NP_175778|]
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regulatory particle triple-A 1A [Arabidopsis thaliana]

Protein Classification

26S proteasome regulatory subunit family protein( domain architecture ID 1001539)

26S proteasome regulatory subunit family protein may act as a component of the 26S proteasome, a multiprotein complex facilitating the ATP-dependent degradation of ubiquitinated proteins

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887|GO:0036402|GO:0043161|GO:0000502
PubMed:  27428775|10417703|9927482

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
 113-423 5.80e-159

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 453.52  E-value: 5.80e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  113 KFVVGLGDKVSPTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPE 192
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  193 KFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDA 272
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  273 IGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHT 352
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220930  353 RTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVI-KGYQKFSATPKYM 423
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 113-423 5.80e-159

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 453.52  E-value: 5.80e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  113 KFVVGLGDKVSPTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPE 192
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  193 KFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDA 272
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  273 IGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHT 352
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220930  353 RTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVI-KGYQKFSATPKYM 423
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 85-410 9.39e-136

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 393.78  E-value: 9.39e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930    85 PLQVARCTKIIspntEDAKYVINVKQIAKFVVGLGDKVSPTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPD 164
Cdd:TIGR01242  43 PLIVGTVLEVL----DDNRVVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   165 VTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVG 244
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   245 EGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPAL 324
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   325 LRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLD 404
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358


                  ....*.
gi 15220930   405 AVNKVI 410
Cdd:TIGR01242 359 AVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 121-411 1.70e-135

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 391.68  E-value: 1.70e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 121 KVSPTDIEEGMRVGVDRNKYQIQIPLPPKIdpsvtmMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGID 200
Cdd:COG1222  37 KALELLEEAPALLLNDANLTQKRLGTPRGT------AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIE 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 201 PPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDD 280
Cdd:COG1222 111 PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 281 GVGGdnEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERD 360
Cdd:COG1222 191 GTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADD 268

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220930 361 IRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVIK 411
Cdd:COG1222 269 VDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKVKK 319
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 166-336 6.34e-122

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: 351.25  E-value: 6.34e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 166 TYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGE 245
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 246 GARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALL 325
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 15220930 326 RPGRLDRKVEF 336
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 205-338 1.22e-48

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: 161.99  E-value: 1.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   205 VLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDdgvGG 284
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15220930   285 DNEVQRTMLEIVNQLDGFDAR-GNIKVLMATNRPDTLDPALLrpGRLDRKVEFGL 338
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 201-340 1.31e-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: 82.04  E-value: 1.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930    201 PPKGVLCYGPPGTGKTLLARAVAN---RTDACFIRVIGSEL--------------VQKYVGEGARMVRELFQMARSKKAC 263
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220930    264 IVFFDEVDAIGGARFddgvggdnEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPgRLDRKVEFGLPD 340
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 113-423 5.80e-159

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 453.52  E-value: 5.80e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  113 KFVVGLGDKVSPTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPE 192
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  193 KFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDA 272
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  273 IGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHT 352
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220930  353 RTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVI-KGYQKFSATPKYM 423
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 85-410 9.39e-136

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 393.78  E-value: 9.39e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930    85 PLQVARCTKIIspntEDAKYVINVKQIAKFVVGLGDKVSPTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPD 164
Cdd:TIGR01242  43 PLIVGTVLEVL----DDNRVVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   165 VTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVG 244
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   245 EGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPAL 324
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   325 LRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLD 404
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358


                  ....*.
gi 15220930   405 AVNKVI 410
Cdd:TIGR01242 359 AVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 121-411 1.70e-135

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 391.68  E-value: 1.70e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 121 KVSPTDIEEGMRVGVDRNKYQIQIPLPPKIdpsvtmMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGID 200
Cdd:COG1222  37 KALELLEEAPALLLNDANLTQKRLGTPRGT------AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIE 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 201 PPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDD 280
Cdd:COG1222 111 PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 281 GVGGdnEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERD 360
Cdd:COG1222 191 GTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADD 268

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220930 361 IRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVIK 411
Cdd:COG1222 269 VDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKVKK 319
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 166-336 6.34e-122

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: 351.25  E-value: 6.34e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 166 TYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGE 245
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 246 GARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALL 325
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 15220930 326 RPGRLDRKVEF 336
Cdd:cd19502 161 RPGRFDRKIEF 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 126-411 1.97e-118

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 350.99  E-value: 1.97e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  126 DIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGV 205
Cdd:PTZ00454 103 LLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGV 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  206 LCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGD 285
Cdd:PTZ00454 183 LLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGAD 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  286 NEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFEL 365
Cdd:PTZ00454 263 REVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLED 342

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15220930  366 LARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVIK 411
Cdd:PTZ00454 343 FVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVR 388
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 85-423 4.40e-114

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 341.37  E-value: 4.40e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   85 PLQVARCTKIISPN------TEDAKYVINvkqIAKFVvglgDKvspTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMT 158
Cdd:PTZ00361 104 PLSVGTLEEIIDENhaivssSVGPEYYVN---ILSFV----DK---EQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMK 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  159 VEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSEL 238
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEL 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  239 VQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPD 318
Cdd:PTZ00361 254 IQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIE 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  319 TLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVT 398
Cdd:PTZ00361 334 SLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVT 413

                        330       340
                 ....*....|....*....|....*
gi 15220930  399 EKDFLDAVNKVIkgYQKFSATPKYM 423
Cdd:PTZ00361 414 QADFRKAKEKVL--YRKKGNIPEGL 436
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 160-417 5.96e-87

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: 273.39  E-value: 5.96e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   160 EEKPDVTYNDVGGCKEQIEKMREVVELpMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELV 239
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   240 QKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDT 319
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   320 LDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTE 399
Cdd:TIGR01241 206 LDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITM 285

                         250
                  ....*....|....*...
gi 15220930   400 KDFLDAVNKVIKGYQKFS 417
Cdd:TIGR01241 286 NDIEEAIDRVIAGPEKKS 303
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
157-415 2.58e-86

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 274.22  E-value: 2.58e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 157 MTVEEKPDVTYNDVGGCKEQIEKMREVVElpMLH-PEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIG 235
Cdd:COG0465 131 LYDEDKPKVTFDDVAGVDEAKEELQEIVD--FLKdPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 236 SELVQKYVGEGARMVRELFQMARsKKA-CIVFFDEVDAIGGARfDDGVGGDN-EVQRTMleivNQL----DGFDARGNIK 309
Cdd:COG0465 209 SDFVEMFVGVGASRVRDLFEQAK-KNApCIIFIDEIDAVGRQR-GAGLGGGHdEREQTL----NQLlvemDGFEGNEGVI 282

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 310 VLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYA 389
Cdd:COG0465 283 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLA 362

                       250       260
                ....*....|....*....|....*.
gi 15220930 390 IRARRKTVTEKDFLDAVNKVIKGYQK 415
Cdd:COG0465 363 ARRNKKAVTMEDFEEAIDRVIAGPER 388
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 167-409 6.95e-79

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: 249.44  E-value: 6.95e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 167 YNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEG 246
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 247 ARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEivnQLDGFdaRGNIKVLMATNRPDTLDPALLR 326
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLT---EMEEL--RSDVVVIAATNRPDLLDPALLR 310

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 327 pgRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAV 406
Cdd:COG0464 311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388


                ...
gi 15220930 407 NKV 409
Cdd:COG0464 389 ERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 150-409 1.25e-75

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: 249.82  E-value: 1.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   150 IDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDAC 229
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGAN 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   230 FIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIG---GARFDDGVggdneVQRTMLEIVNQLDGFDARG 306
Cdd:TIGR01243 515 FIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAparGARFDTSV-----TDRIVNQLLTEMDGIQELS 589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   307 NIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAG 386
Cdd:TIGR01243 590 NVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAA 669

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 15220930   387 MYAIRARRKT------------------VTEKDFLDAVNKV 409
Cdd:TIGR01243 670 MAALRESIGSpakeklevgeeeflkdlkVEMRHFLEALKKV 710
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 163-391 1.70e-72

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: 241.35  E-value: 1.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   163 PDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKY 242
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   243 VGEGARMVRELFQMARSKKACIVFFDEVDAIGGARfdDGVGGDNEvQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDP 322
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220930   323 ALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIR 391
Cdd:TIGR01243 330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
ftsH CHL00176
cell division protein; Validated
 160-412 3.01e-71

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 236.10  E-value: 3.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  160 EEKPDVTYNDVGGCKEQIEKMREVVELpMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELV 239
Cdd:CHL00176 175 EADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFV 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  240 QKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARfDDGVGGDN-EVQRTMLEIVNQLDGFDARGNIKVLMATNRPD 318
Cdd:CHL00176 254 EMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQR-GAGIGGGNdEREQTLNQLLTEMDGFKGNKGVIVIAATNRVD 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  319 TLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVT 398
Cdd:CHL00176 333 ILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATIT 412

                        250
                 ....*....|....
gi 15220930  399 EKDFLDAVNKVIKG 412
Cdd:CHL00176 413 MKEIDTAIDRVIAG 426
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
153-417 2.64e-70

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 233.77  E-value: 2.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  153 SVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELpMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIR 232
Cdd:PRK10733 137 SKARMLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFT 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  233 VIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLM 312
Cdd:PRK10733 216 ISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  313 ATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRA 392
Cdd:PRK10733 296 ATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARG 375

                        250       260
                 ....*....|....*....|....*
gi 15220930  393 RRKTVTEKDFLDAVNKVIKGYQKFS 417
Cdd:PRK10733 376 NKRVVSMVEFEKAKDKIMMGAERRS 400
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 165-334 5.96e-70

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: 218.64  E-value: 5.96e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 165 VTYNDVGGCKEQIEKMREVVELpMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVG 244
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 245 EGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPAL 324
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159

                       170
                ....*....|
gi 15220930 325 LRPGRLDRKV 334
Cdd:cd19501 160 LRPGRFDRQV 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 178-332 3.59e-65

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: 205.60  E-value: 3.59e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 178 EKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMA 257
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220930 258 RSKKACIVFFDEVDAIGGARFDDGVGGDNEvqRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDR 332
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 169-336 3.61e-65

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: 205.99  E-value: 3.61e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGAR 248
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 249 MVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLeivNQLDGFDARGNIKVLMATNRPDTLDPALLRPG 328
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLL---TLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                ....*...
gi 15220930 329 RLDRKVEF 336
Cdd:cd19503 158 RFDREVEI 165
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 169-337 1.94e-61

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: 196.50  E-value: 1.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGAR 248
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 249 MVRELFQMARSKKACIVFFDEVDAIGGARFDdgvgGDNEVQRtmlEIVNQL----DGFDARGNIKVLMATNRPDTLDPAL 324
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVER---RIVSQLltlmDGLKQRAHVIVMAATNRPNSIDPAL 153

                       170
                ....*....|...
gi 15220930 325 LRPGRLDRKVEFG 337
Cdd:cd19519 154 RRFGRFDREIDIG 166
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 121-401 2.02e-60

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 204.56  E-value: 2.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   121 KVSPTDIEEGMRVG----VDRnKYQIQIPLPPKidPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVK 196
Cdd:TIGR03689 134 KLAGALADEGLRPGdtllVDP-RAGYAFEAIPR--TEVEDLVLEEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYRE 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   197 LGIDPPKGVLCYGPPGTGKTLLARAVAN----------RTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKA---- 262
Cdd:TIGR03689 211 YGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNKYVGETERQIRLIFQRAREKASegrp 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   263 CIVFFDEVDAIGGARfddGVGGDNEVQRTML-EIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDL 341
Cdd:TIGR03689 291 VIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDA 367

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220930   342 ESRTQIFkihTRTMNCERDIRFELLARLCPNS-TGADIRSVCTEAgMYAIRARRK--TVTEKD 401
Cdd:TIGR03689 368 EAAADIF---AKYLTDDLPLPEDLAAHDGDREaTAAALIQRVVDA-LYARSEANRyvEVTYAN 426
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 176-336 1.25e-58

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: 189.03  E-value: 1.25e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 176 QIEKMREVVELPMLHPEKFvKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQ 255
Cdd:cd19481   1 LKASLREAVEAPRRGSRLR-RYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 256 MARSKKACIVFFDEVDAIGGARfdDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVE 335
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                .
gi 15220930 336 F 336
Cdd:cd19481 158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 178-334 7.28e-58

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: 186.93  E-value: 7.28e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 178 EKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMA 257
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220930 258 RSKKACIVFFDEVDAIGGARfddGVGGDNEV-QRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKV 334
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRR---GTTGDSGVtERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 178-334 2.81e-55

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: 180.40  E-value: 2.81e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 178 EKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMA 257
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220930 258 RSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKV 334
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
168-411 2.29e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 178.15  E-value: 2.29e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 168 NDVGGCKEQIEKMREVVE--LPMLHPEKFvklGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGE 245
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIKelRRRENLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 246 GARMVRELFQMARSKKaCIVFFDEVDAIGGARFDDGVGGDnevqrtMLEIVN----QLDGFdaRGNIKVLMATNRPDTLD 321
Cdd:COG1223  79 TARNLRKLFDFARRAP-CVIFFDEFDAIAKDRGDQNDVGE------VKRVVNallqELDGL--PSGSVVIAATNHPELLD 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 322 PALLRpgRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKD 401
Cdd:COG1223 150 SALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKED 227

                       250
                ....*....|
gi 15220930 402 FLDAVNKVIK 411
Cdd:COG1223 228 LEEALKQRKE 237
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 187-332 2.86e-50

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: 167.28  E-value: 2.86e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 187 PMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVF 266
Cdd:cd19530  15 PIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIF 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220930 267 FDEVDAIGGARFDDGVGGdneVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDR 332
Cdd:cd19530  95 FDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 205-338 1.22e-48

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: 161.99  E-value: 1.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   205 VLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDdgvGG 284
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15220930   285 DNEVQRTMLEIVNQLDGFDAR-GNIKVLMATNRPDTLDPALLrpGRLDRKVEFGL 338
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 169-336 1.61e-47

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: 160.37  E-value: 1.61e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVAN------RTDACFIRViGSELVQKY 242
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAecskggQKVSFFMRK-GADCLSKW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 243 VGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIvnqLDGFDARGNIKVLMATNRPDTLDP 322
Cdd:cd19517  80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDP 156

                       170
                ....*....|....
gi 15220930 323 ALLRPGRLDRKVEF 336
Cdd:cd19517 157 ALRRPGRFDREFYF 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 170-334 7.70e-45

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: 153.28  E-value: 7.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 170 VGGCKEQIEKMREVVELPMLHPEKFvKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARM 249
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 250 VRELFQMARSKKACIVFFDEVDAIGGARfddgVGGDNEVQRTM-LEIVNQLDGF--DARGNIKVLMATNRPDTLDPALLR 326
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSER----GSGEHEASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155


                ....*...
gi 15220930 327 pgRLDRKV 334
Cdd:cd19509 156 --RFEKRI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 169-334 1.07e-44

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: 152.94  E-value: 1.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGAR 248
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 249 MVRELFQMARSKKACIVFFDEVDAIGGARfddgvggdNEVQRTM-LEIVNQL----DGF----DARGNIKVLMATNRPDT 319
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR--------ESAQREMeRRIVSQLltcmDELnnekTAGGPVLVIGATNRPDS 152

                       170
                ....*....|....*
gi 15220930 320 LDPALLRPGRLDRKV 334
Cdd:cd19518 153 LDPALRRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 180-335 3.55e-44

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: 151.43  E-value: 3.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 180 MREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARS 259
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220930 260 KKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLeivNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVE 335
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLL---TQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 182-332 3.24e-42

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: 146.12  E-value: 3.24e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 182 EVVELPMLHPEKFVKlGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKK 261
Cdd:cd19527   7 DTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAK 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220930 262 ACIVFFDEVDAIGGARfddGVGGDNE--VQRTMLEIVNQLDGF-DARGNIKVLMATNRPDTLDPALLRPGRLDR 332
Cdd:cd19527  86 PCVIFFDELDSLAPSR---GNSGDSGgvMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 162-334 1.81e-37

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: 134.22  E-value: 1.81e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 162 KPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKlGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQK 241
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 242 YVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDdgvgGDNE-VQRTMLEIVNQLDGF--DARGnIKVLMATNRPD 318
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEaSRRIKTELLVQMNGVgnDSQG-VLVLGATNIPW 154

                       170
                ....*....|....*.
gi 15220930 319 TLDPALLRpgRLDRKV 334
Cdd:cd19521 155 QLDSAIRR--RFEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 148-326 2.25e-37

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: 134.35  E-value: 2.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 148 PKIDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGiDPPKGVLCYGPPGTGKTLLARAVANRTD 227
Cdd:cd19525   2 PKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 228 ACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDdgvgGDNEVQRTM-LEIVNQLDGFDARG 306
Cdd:cd19525  81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE----GEHESSRRIkTEFLVQLDGATTSS 156

                       170       180
                ....*....|....*....|..
gi 15220930 307 N--IKVLMATNRPDTLDPALLR 326
Cdd:cd19525 157 EdrILVVGATNRPQEIDEAARR 178
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 169-326 1.11e-36

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: 131.78  E-value: 1.11e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLGI-DPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGA 247
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 248 RMVRELFQMARSKKACIVFFDEVDAIGGARfddgVGGDNEVQRTM-LEIVNQLDGFDARGNIKVLM--ATNRPDTLDPAL 324
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156


                ..
gi 15220930 325 LR 326
Cdd:cd19520 157 LR 158
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 169-334 1.95e-34

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: 125.73  E-value: 1.95e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLGIdPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGAR 248
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 249 MVRELFQMARSKKACIVFFDEVDAIGGARFDdgvgGDNEVQRTM-LEIVNQLDGFDARGNIKVLM--ATNRPDTLDPALL 325
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVL 155


                ....*....
gi 15220930 326 RpgRLDRKV 334
Cdd:cd19524 156 R--RFTKRV 162
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 169-334 3.01e-34

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: 125.48  E-value: 3.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVklGIDPP-KGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGA 247
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 248 RMVRELFQMARSKKACIVFFDEVDAIGGARfddGVGGDNEV-QRTMLEIVNQLDGF-------DARGNIKVLMATNRPDT 319
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155

                       170
                ....*....|....*
gi 15220930 320 LDPALLRpgRLDRKV 334
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 191-335 1.76e-30

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: 115.66  E-value: 1.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 191 PEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVI-GSELVQKYVGEGARMVRELFQMA-RSKKAC----- 263
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESEANIRKLFADAeEEQRRLgansg 103

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220930 264 --IVFFDEVDAIGGARfdDGVGGDNEVQRTmleIVNQL----DGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVE 335
Cdd:cd19504 104 lhIIIFDEIDAICKQR--GSMAGSTGVHDT---VVNQLlskiDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 171-338 6.02e-26

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 102.61  E-value: 6.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 171 GGCKEQIEKMREVVELPmlhpekfvklgidPPKGVLCYGPPGTGKTLLARAVAN---RTDACFIRVIGSELVQKYVGEGA 247
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAEL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 248 R---MVRELFQMARSKKACIVFFDEVDAIGGarfddgvGGDNEVQRTMLEIvnqLDGFDARGNIKVLMATNRPDTLDPAL 324
Cdd:cd00009  68 FghfLVRLLFELAEKAKPGVLFIDEIDSLSR-------GAQNALLRVLETL---NDLRIDRENVRVIGATNRPLLGDLDR 137

                       170
                ....*....|....
gi 15220930 325 LRPGRLDRKVEFGL 338
Cdd:cd00009 138 ALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 169-326 3.01e-25

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: 101.11  E-value: 3.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 169 DVGGCKEQIEKMREVVELPMLHPEKFVKLgIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGAR 248
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 249 MVRELFQMARSKKACIVFFDEVDAIGGARFDdgvgGDNEVQRTMLEIVNQLDGF--DARGNIKVLMATNRPDTLDPALLR 326
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
ycf46 CHL00195
Ycf46; Provisional
 163-410 5.26e-21

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 95.09  E-value: 5.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  163 PDVTYNDVGGC---KEQIEKMREVVElpmlhpEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELV 239
Cdd:CHL00195 223 VNEKISDIGGLdnlKDWLKKRSTSFS------KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  240 QKYVGEGARMVRELFQMARSKKACIVFFDEVD-AIGGARFDDGVGGDNEVQRTMLEIVNQldgfdARGNIKVLMATNRPD 318
Cdd:CHL00195 297 GGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNID 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  319 TLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTM--NCERDIRFELLARLCPNSTGADIRSVCTEAgMYAIRARRKT 396
Cdd:CHL00195 372 LLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGAEIEQSIIEA-MYIAFYEKRE 450

                        250
                 ....*....|....
gi 15220930  397 VTEKDFLDAVNKVI 410
Cdd:CHL00195 451 FTTDDILLALKQFI 464
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 201-340 1.31e-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: 82.04  E-value: 1.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930    201 PPKGVLCYGPPGTGKTLLARAVAN---RTDACFIRVIGSEL--------------VQKYVGEGARMVRELFQMARSKKAC 263
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220930    264 IVFFDEVDAIGGARFddgvggdnEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPgRLDRKVEFGLPD 340
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 198-332 1.04e-16

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 77.02  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 198 GIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVD-AIGGA 276
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15220930 277 RFDDGVGGDNEVQRTMLEIVNQldgfdARGNIKVLMATNRPDTLDPALLRPGRLDR 332
Cdd:cd19507 107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 196-336 3.36e-14

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: 69.69  E-value: 3.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 196 KLGIDPPKGVLCYGPPGTGKTLLARAVAN--RTDACFIrvigsELVQkyVGEGARMVRELfqMARSKKACIVFFDEVDA- 272
Cdd:cd19510  17 DRGIPYRRGYLLYGPPGTGKSSFIAALAGelDYDICDL-----NLSE--VVLTDDRLNHL--LNTAPKQSIILLEDIDAa 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220930 273 --IGGARFDDGVGGDNEVQRTMLEIVNQLDGF---DARgniKVLMATNRPDTLDPALLRPGRLDRKVEF 336
Cdd:cd19510  88 feSREHNKKNPSAYGGLSRVTFSGLLNALDGVassEER---IVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 203-336 2.58e-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: 61.39  E-value: 2.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 203 KGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSElVQKYVGEGARMVRELFQMA-RSKKACIVFFDEVDAIGGARFDDG 281
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15220930 282 VggdNEVQRTMLEIVNQLDGFDARgNIKVLMATNRPDTLDPALlrPGRLDRKVEF 336
Cdd:cd19512 102 I---SEDLRAALNAFLYRTGEQSN-KFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 360-404 2.82e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 57.93  E-value: 2.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15220930   360 DIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLD 404
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 205-324 3.91e-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: 56.30  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 205 VLCYGPPGTGKTLLARAVANRTD---------ACFIRVIGSELVQKYVGEGARMVRELFQ----MARSKKACI-VFFDEV 270
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqeLIDDKDALVfVLIDEV 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15220930 271 DAIGGARFDDGVGGD-NEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPAL 324
Cdd:cd19508 135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 202-296 6.69e-09

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 55.08  E-value: 6.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 202 PKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQ-KYVGegarmvRELFQMARSKKACIVFFDEVDAIggARFDD 280
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKI--AKRGG 117

                        90
                ....*....|....*....
gi 15220930 281 GVGGD---NEVQRTMLEIV 296
Cdd:cd19498 118 SSGPDvsrEGVQRDLLPIV 136
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 208-270 9.56e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.91  E-value: 9.56e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 208 YGPPGTGKTLLARAVANRTDACFIR---VIGSelvqkyVGEgarmVRELFQMARSKKA----CIVFFDEV 270
Cdd:COG2256  55 WGPPGTGKTTLARLIANATDAEFVAlsaVTSG------VKD----IREVIEEARERRAygrrTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
 166-277 1.02e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 53.77  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  166 TYNDVGGCKEQIEKMREVVElpmlhpeKFVKlGIdPPKGVLCYGPPGTGKTLLARAVANRtdacfirvIGSELV------ 239
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE-------SWLK-GK-PKKALLLYGPPGVGKTSLAHALAND--------YGWEVIelnasd 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15220930  240 -------QKYVGEGARMvRELFQMARSkkacIVFFDEVDAI------GGAR 277
Cdd:PRK04195  75 qrtadviERVAGEAATS-GSLFGARRK----LILLDEVDGIhgnedrGGAR 120
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 196-332 2.18e-07

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 50.45  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 196 KLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQK--------------YVGEGARMVRELFQMARSKK 261
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMS 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220930 262 ACIVFFDEVDAIGGARFDDGVGGDNevqRTMLEIVNQLDGFDARG----NIKVLMATNRPDTLDPALLRPGRLDR 332
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKsstrNILVIASTHIPQKVDPALIAPNRLDT 157
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 208-270 3.09e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 3.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  208 YGPPGTGKTLLARAVANRTDACFIR---VIGSelvqkyVGEgarmVRELFQMARSKKA----CIVFFDEV 270
Cdd:PRK13342  42 WGPPGTGKTTLARIIAGATDAPFEAlsaVTSG------VKD----LREVIEEARQRRSagrrTILFIDEI 101
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 174-368 4.86e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 48.69  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   174 KEQIEKMREVVELPMLHPEKFVKLGIDPpKGVLCYGPPGTGKTLLARAVANR-------TDACFIRVIGSELVQKYVGEG 246
Cdd:TIGR03922 285 KRQVAALKSSTAMALARAERGLPVAQTS-NHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGES 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   247 ARMVRELFQMARSKkacIVFFDE----VDAIGGARFDDGvggdnevqrtmLEIVNQLDGF--DARGNIKVLMATNRPDtL 320
Cdd:TIGR03922 364 EAKTNEIIDSALGG---VLFLDEaytlVETGYGQKDPFG-----------LEAIDTLLARmeNDRDRLVVIGAGYRKD-L 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15220930   321 DPAL-----LRpGRLDRKVEFglpDLESRTQIFKIhTRTMNCERDIRFELLAR 368
Cdd:TIGR03922 429 DKFLevnegLR-SRFTRVIEF---PSYSPDELVEI-ARRMATERDSVLDDAAA 476
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 196-336 1.30e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 45.25  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 196 KLGIDPPK---GVLCY-GPPGTGKTLLARAVA---NRTDACFIRVIGSELVQK------------YVGEGARMVreLFQM 256
Cdd:cd19499  31 RAGLSDPNrpiGSFLFlGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGGQ--LTEA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 257 ARSKKACIVFFDEVDAiggarfddgvgGDNEVQRTMLEIVNqlDGF--DARG------NIKVLMATNrpdTLDPALLrpG 328
Cdd:cd19499 109 VRRKPYSVVLLDEIEK-----------AHPDVQNLLLQVLD--DGRltDSHGrtvdfkNTIIIMTSN---HFRPEFL--N 170


                ....*...
gi 15220930 329 RLDRKVEF 336
Cdd:cd19499 171 RIDEIVVF 178
44 PHA02544
clamp loader, small subunit; Provisional
 202-349 1.62e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 46.52  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930  202 PKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGS----ELVQKYVGEGARmvrelfQMARSKKACIVFFDEVDAIGGAr 277
Cdd:PHA02544  43 PNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFAS------TVSLTGGGKVIIIDEFDRLGLA- 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220930  278 fddgvggdnEVQRTMLEIVNQLDgfdarGNIKVLMATNRPDTLDPALLrpGRLdRKVEFGLPDLESRTQIFK 349
Cdd:PHA02544 116 ---------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMMK 170
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 204-326 1.93e-05

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: 44.21  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   204 GVLCYGPPGTGKTLLARAVANRTDAC--FIRVIG-----SELVQKYV--GEGARMV-RELfqMARSKKACIVFFDEVDAI 273
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRpvFYVQLTrdtteEDLFGRRNidPGGASWVdGPL--VRAAREGEIAVLDEINRA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220930   274 GGarfddgvggdnEVQRTMLEIVN-----QLDGF----DARGNIKVLMATNRPDT----LDPALLR 326
Cdd:pfam07728  79 NP-----------DVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 209-296 2.31e-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: 44.49  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   209 GPPGTGKTLLARAVANR---TDACFIRVIGSELVQK------------YVG--EGArmvrELFQMARSKKACIVFFDEVD 271
Cdd:pfam07724  10 GPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEhsvsrligappgYVGyeEGG----QLTEAVRRKPYSIVLIDEIE 85

                          90       100
                  ....*....|....*....|....*
gi 15220930   272 AIggarfddgvggDNEVQRTMLEIV 296
Cdd:pfam07724  86 KA-----------HPGVQNDLLQIL 99
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
175-280 2.90e-05

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 45.99  E-value: 2.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 175 EQIEKMREVVElPMLHPEkfvklgidPPKGVLCYGPPGTGKTLLARAVANR---------TDACFIRV----------IG 235
Cdd:COG1474  33 EEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrVL 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15220930 236 SELVQKyVGEG----------ARMVRELFQ-MARSKKACIVFFDEVDAIGGARFDD 280
Cdd:COG1474 104 SRILEE-LGSGedipstglstDELFDRLYEaLDERDGVLVVVLDEIDYLVDDEGDD 158
PRK13341 PRK13341
AAA family ATPase;
208-270 9.75e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 44.66  E-value: 9.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220930  208 YGPPGTGKTLLARAVANRTDACFIrVIGSELvqkyvgEGARMVRELF-----QMARSKKACIVFFDEV 270
Cdd:PRK13341  58 YGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVdrakeRLERHGKRTILFIDEV 118
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 205-233 1.53e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 43.23  E-value: 1.53e-04
                        10        20
                ....*....|....*....|....*....
gi 15220930 205 VLCYGPPGTGKTLLARAVANRTDACFIRV 233
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 209-326 2.20e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 41.46  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 209 GPPGTGKTLLARAVANRTDACFIRVI--GSELVQKYVGEGARMVRELFQM----------ARS--KKACIVFFDEVDAig 274
Cdd:cd00267  32 GPNGSGKSTLLRAIAGLLKPTSGEILidGKDIAKLPLEELRRRIGYVPQLsggqrqrvalARAllLNPDLLLLDEPTS-- 109

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15220930 275 garfddgvGGDNEVQRTMLEIVNQLdgfdARGNIKVLMATNRPDTLDPALLR 326
Cdd:cd00267 110 --------GLDPASRERLLELLREL----AEEGRTVIIVTHDPELAELAADR 149
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 205-296 5.09e-04

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: 41.43  E-value: 5.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 205 VLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQK-YVGEGARMVRE-LFQMA-----RSKKAcIVFFDEVDAIggAR 277
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGEDVENILLkLLQAAdydveRAQRG-IVYIDEIDKI--AR 129

                        90       100
                ....*....|....*....|....*
gi 15220930 278 FDDG------VGGDNeVQRTMLEIV 296
Cdd:cd19497 130 KSENpsitrdVSGEG-VQQALLKIL 153
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
199-241 5.29e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 41.30  E-value: 5.29e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15220930 199 IDPPKGVLCYGPPGTGKTLLARAVANRtdAC-------FIRVigSELVQK 241
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALGHE--ACragyrvrFTTA--PDLVNE 141
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
208-410 7.78e-04

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 41.33  E-value: 7.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 208 YGPPGTGKTLLARAVANRtdacfIRVIGSELVQKYVgEGARMVRELFQMARSKK--ACIVFFDEVDA--IggarfDD--G 281
Cdd:COG0593  40 YGGVGLGKTHLLHAIGNE-----ALENNPGARVVYL-TAEEFTNDFINAIRNNTieEFKEKYRSVDVllI-----DDiqF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 282 VGGDNEVQRTMLEIVNQLdgfdARGNIKVLMATNRPdtldPALLrPGRLDR---KVEFGL------PDLESRTQIF--KI 350
Cdd:COG0593 109 LAGKEATQEEFFHTFNAL----REAGKQIVLTSDRP----PKEL-PGLEERlrsRLEWGLvvdiqpPDLETRIAILrkKA 179

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220930 351 HTRTMNCERDIRFELLARLcpNSTGADIRSVCTEAGMYAiRARRKTVTE-------KDFLDAVNKVI 410
Cdd:COG0593 180 ADRGLELPDEVLEYLARRI--ERNVRELEGALNRLDAYA-LLTGRPITLelarevlKDLLRAQKKEI 243
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
205-258 9.97e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.51  E-value: 9.97e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220930 205 VLCyGPPGTGKTLLARAVANRTDACFIR--VIGSELVQKYVGEGARMV-------RELFQMAR 258
Cdd:COG0645   3 LVC-GLPGSGKSTLARALAERLGAVRLRsdVVRKRLFGAGLAPLERSPeatartyARLLALAR 64
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 205-321 1.14e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 38.64  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 205 VLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKyvgegarMVRELFQMARSKKACIVFFDEVDAIGGARfddgvgg 284
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDT-------ILEAIEDLIEEKKLDIIIIDSLSSLARAS------- 66

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15220930 285 DNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLD 321
Cdd:cd01120  67 QGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDI 103
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 175-275 1.31e-03

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 40.69  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   175 EQIEKMREVVElPMLHPEkfvklgidPPKGVLCYGPPGTGKTLLARAVANR----TDACFIRV---------------IG 235
Cdd:TIGR02928  22 EQIEELAKALR-PILRGS--------RPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15220930   236 SELVQKYVGEG----------ARMVRELFQ-MARSKKACIVFFDEVDAIGG 275
Cdd:TIGR02928  93 VELANQLRGSGeevpttglstSEVFRRLYKeLNERGDSLIIVLDEIDYLVG 143
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
203-238 3.08e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.57  E-value: 3.08e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15220930 203 KGVLCYGPPGTGKTLLARAVANR--TDACFIRVIGSEL 238
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 205-233 4.20e-03

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 38.78  E-value: 4.20e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 15220930 205 VLCYGPPGTGKTLLARAVANRT-DACFIRV 233
Cdd:COG2842  53 GVVYGESGVGKTTAAREYANRNpNVIYVTA 82
Sigma54_activat pfam00158
Sigma-54 interaction domain;
178-238 4.32e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.77  E-value: 4.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220930   178 EKMREVVELpmlhpekfVKLGIDPPKGVLCYGPPGTGKTLLARAV---ANRTDACFIRV---------IGSEL 238
Cdd:pfam00158   6 PAMQEVLEQ--------AKRVAPTDAPVLITGESGTGKELFARAIhqlSPRADGPFVAVncaaipeelLESEL 70
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 205-274 5.87e-03

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: 37.54  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930 205 VLC-YGPPGTGKTLLARAVANRTDACFIRV-IG-----SELV---QKYVGEgarMVRELFQ-MARSKKACIVF-FDEVDA 272
Cdd:cd19500  39 ILClVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGA---MPGRIIQaLKKAGTNNPVFlLDEIDK 115


                ..
gi 15220930 273 IG 274
Cdd:cd19500 116 IG 117
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 203-233 6.78e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 38.84  E-value: 6.78e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 15220930 203 KG-VLC-YGPPGTGKTLLARAVANRTDACFIRV 233
Cdd:COG0466 351 KGpILClVGPPGVGKTSLGKSIARALGRKFVRI 383
AAA_22 pfam13401
AAA domain;
205-278 7.40e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.55  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220930   205 VLCYGPPGTGKTLLARAVANRTDAC-----------------FIRVIGSELVQKYVGEG-ARMVRELFQ--MARSKKACI 264
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPEVrdsvvfvdlpsgtspkdLLRALLRALGLPLSGRLsKEELLAALQqlLLALAVAVV 87

                          90
                  ....*....|....
gi 15220930   265 VFFDEVDAIGGARF 278
Cdd:pfam13401  88 LIIDEAQHLSLEAL 101
PRK08116 PRK08116
hypothetical protein; Validated
 204-224 8.07e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.08  E-value: 8.07e-03
                         10        20
                 ....*....|....*....|.
gi 15220930  204 GVLCYGPPGTGKTLLARAVAN 224
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIAN 136
PRK06835 PRK06835
DNA replication protein DnaC; Validated
 172-225 9.54e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 37.96  E-value: 9.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15220930  172 GCKEQIEKMREVVElpmlhpeKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANR 225
Cdd:PRK06835 160 SPRKNMEKILEKCK-------NFIENFDKNNENLLFYGNTGTGKTFLSNCIAKE 206
 
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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