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Conserved domains on  [gi|71987364|ref|NP_001022113|]
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putative 26S proteasome regulatory subunit 10B [Caenorhabditis elegans]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
21-391 2.50e-166

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 471.62  E-value: 2.50e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   21 ERTKALNSYRRKLAE-CRDIEQKLKDLRKKESEMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKFIVKATNGPRYVVG 99
Cdd:PRK03992   1 ERLEALEERNSELEEqIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  100 CRRSINKEELKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRV 179
Cdd:PRK03992  81 VSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  180 GITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRR 259
Cdd:PRK03992 161 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  260 FSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITK 339
Cdd:PRK03992 241 TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71987364  340 HGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:PRK03992 321 ADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKV 372
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
21-391 2.50e-166

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 471.62  E-value: 2.50e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   21 ERTKALNSYRRKLAE-CRDIEQKLKDLRKKESEMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKFIVKATNGPRYVVG 99
Cdd:PRK03992   1 ERLEALEERNSELEEqIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  100 CRRSINKEELKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRV 179
Cdd:PRK03992  81 VSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  180 GITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRR 259
Cdd:PRK03992 161 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  260 FSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITK 339
Cdd:PRK03992 241 TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71987364  340 HGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:PRK03992 321 ADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKV 372
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
29-391 6.87e-147

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: 421.13  E-value: 6.87e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364    29 YRRKLAECRDIEQKLKDLRKKESEMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKFIVKATNGPRYVVGCRRSINKEE 108
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   109 LKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCL 188
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   189 LFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADR 268
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   269 EIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAV 348
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 71987364   349 VKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
110-391 1.18e-133

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 386.28  E-value: 1.18e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 110 KQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLL 189
Cdd:COG1222  38 ALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 190 FGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSAdrE 269
Cdd:COG1222 118 YGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--E 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 270 IQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVV 349
Cdd:COG1222 196 VQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLA 275
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71987364 350 KLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:COG1222 276 KLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKV 317
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
148-318 1.64e-112

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: 326.60  E-value: 1.64e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 148 SYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGE 227
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 228 SARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALL 307
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 71987364 308 RPGRLDRKIEI 318
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
188-320 2.95e-52

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 170.85  E-value: 2.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   188 LLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGtsaD 267
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG---D 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71987364   268 REIQRTLMELLNQLDGFDSL-GKVKVIMATNRPDTLDPALLrpGRLDRKIEIGL 320
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
183-322 3.26e-19

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: 83.58  E-value: 3.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364    183 PPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVS-----------------SAIVDKYIGESARMIREMFNYARDHQPC 245
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987364    246 IVFMDEIDAIggrrfsegTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPgRLDRKIEIGLPN 322
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
21-391 2.50e-166

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 471.62  E-value: 2.50e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   21 ERTKALNSYRRKLAE-CRDIEQKLKDLRKKESEMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKFIVKATNGPRYVVG 99
Cdd:PRK03992   1 ERLEALEERNSELEEqIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  100 CRRSINKEELKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRV 179
Cdd:PRK03992  81 VSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  180 GITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRR 259
Cdd:PRK03992 161 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  260 FSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITK 339
Cdd:PRK03992 241 TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71987364  340 HGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:PRK03992 321 ADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKV 372
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
29-391 6.87e-147

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: 421.13  E-value: 6.87e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364    29 YRRKLAECRDIEQKLKDLRKKESEMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKFIVKATNGPRYVVGCRRSINKEE 108
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   109 LKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCL 188
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   189 LFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADR 268
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   269 EIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAV 348
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 71987364   349 VKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
110-391 1.18e-133

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 386.28  E-value: 1.18e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 110 KQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLL 189
Cdd:COG1222  38 ALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 190 FGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSAdrE 269
Cdd:COG1222 118 YGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--E 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 270 IQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVV 349
Cdd:COG1222 196 VQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLA 275
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71987364 350 KLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:COG1222 276 KLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKV 317
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
7-391 1.13e-118

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 350.60  E-value: 1.13e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364    7 SNMVEPTGPAIVEDERTKALNSYRRKLAECRDIEQKLKDLRKKeseMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKF 86
Cdd:PTZ00454   5 AAAAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKN---LKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   87 IVKATNGPRYVVGCRRSINKEELKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVV 166
Cdd:PTZ00454  82 IVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  167 ELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCI 246
Cdd:PTZ00454 162 ELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  247 VFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSR 326
Cdd:PTZ00454 242 IFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQK 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71987364  327 LEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:PTZ00454 322 RLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTV 386
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
32-391 3.17e-114

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 340.60  E-value: 3.17e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   32 KLAECRD---IEQKLKDLRKKESEMTKQFDKSENDIKSLQSVGQIVGEVLKQLSEEKFIVKATNGPRYVVGCRRSINKEE 108
Cdd:PTZ00361  62 KLERIKDyllLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  109 LKQGTRVSLDMTTLTIMRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCL 188
Cdd:PTZ00361 142 LEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVI 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  189 LFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADR 268
Cdd:PTZ00361 222 LYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEK 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  269 EIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAV 348
Cdd:PTZ00361 302 EIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEF 381
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 71987364  349 VKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:PTZ00361 382 IMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKV 424
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
148-318 1.64e-112

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: 326.60  E-value: 1.64e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 148 SYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGE 227
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 228 SARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALL 307
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 71987364 308 RPGRLDRKIEI 318
Cdd:cd19502 161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
125-396 3.25e-84

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: 262.54  E-value: 3.25e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 125 MRQLPREVDPLVYKMSHEDPGNISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAV 204
Cdd:COG0464 132 AAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARAL 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 205 ASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRfseGTSADREIQRTLMELLNQLDGF 284
Cdd:COG0464 212 AGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL 288
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 285 DSlgKVKVIMATNRPDTLDPALLRpgRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVC 364
Cdd:COG0464 289 RS--DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVV 364
                       250       260       270
                ....*....|....*....|....*....|..
gi 71987364 365 TEAGMFAIRAEREFVIDEDFMKAVRKVGDAKR 396
Cdd:COG0464 365 RRAALQALRLGREPVTTEDLLEALEREDIFLK 396
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
138-396 2.64e-77

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: 247.58  E-value: 2.64e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   138 KMSHEDPGNISYSDVGGLAEQIRELREVVELpLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVS 217
Cdd:TIGR01241  43 KLLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   218 SAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATN 297
Cdd:TIGR01241 122 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATN 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   298 RPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAERE 377
Cdd:TIGR01241 202 RPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKT 281
                         250       260
                  ....*....|....*....|.
gi 71987364   378 FVIDEDFMKAVRKV--GDAKR 396
Cdd:TIGR01241 282 EITMNDIEEAIDRViaGPEKK 302
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
138-396 4.34e-76

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 246.87  E-value: 4.34e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 138 KMSHEDPGNISYSDVGGLAEQIRELREVVELpLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVS 217
Cdd:COG0465 130 KLYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 218 SAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFS--EGTSADREiqRTLMELLNQLDGFDSLGKVKVIMA 295
Cdd:COG0465 209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglGGGHDERE--QTLNQLLVEMDGFEGNEGVIVIAA 286
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 296 TNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAE 375
Cdd:COG0465 287 TNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRN 366
                       250       260
                ....*....|....*....|...
gi 71987364 376 REFVIDEDFMKAVRKV--GDAKR 396
Cdd:COG0465 367 KKAVTMEDFEEAIDRViaGPERK 389
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
146-391 1.31e-74

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: 246.36  E-value: 1.31e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   146 NISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYI 225
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   226 GESARMIREMFNYARDHQPCIVFMDEIDAIG---GRRFSEGTSadreiQRTLMELLNQLDGFDSLGKVKVIMATNRPDTL 302
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAparGARFDTSVT-----DRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   303 DPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIR--------- 373
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALResigspake 683
                         250       260
                  ....*....|....*....|....*..
gi 71987364   374 ----AEREFVID-----EDFMKAVRKV 391
Cdd:TIGR01243 684 klevGEEEFLKDlkvemRHFLEALKKV 710
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
151-318 1.13e-70

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: 219.47  E-value: 1.13e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESAR 230
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 231 MIREMFNYARDHQPCIVFMDEIDAIGGRRfsegTSADREI-QRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRP 309
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVeRRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 71987364 310 GRLDRKIEI 318
Cdd:cd19503 157 GRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
147-373 2.76e-68

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: 229.41  E-value: 2.76e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   147 ISYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIG 226
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   227 ESARMIREMFNYARDHQPCIVFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPAL 306
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987364   307 LRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIR 373
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
147-318 3.37e-66

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: 208.24  E-value: 3.37e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 147 ISYSDVGGLAEQIRELREVVELpLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIG 226
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 227 ESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPAL 306
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 71987364 307 LRPGRLDRKIEI 318
Cdd:cd19501 160 LRPGRFDRQVYV 171
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
160-316 7.38e-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: 204.44  E-value: 7.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 160 RELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYA 239
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987364 240 RDHQPCIVFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKI 316
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
ftsH CHL00176
cell division protein; Validated
147-391 1.58e-64

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 217.61  E-value: 1.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  147 ISYSDVGGLAEQIRELREVVELpLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIG 226
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  227 ESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPAL 306
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  307 LRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMK 386
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418

                 ....*
gi 71987364  387 AVRKV 391
Cdd:CHL00176 419 AIDRV 423
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
160-318 8.47e-64

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: 201.57  E-value: 8.47e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 160 RELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYA 239
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71987364 240 RDHQPCIVFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEI 318
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
138-391 8.73e-64

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 215.67  E-value: 8.73e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  138 KMSHEDPGNISYSDVGGLAEQIRELREVVELpLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVS 217
Cdd:PRK10733 140 RMLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISG 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  218 SAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATN 297
Cdd:PRK10733 219 SDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATN 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  298 RPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAERE 377
Cdd:PRK10733 299 RPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKR 378
                        250
                 ....*....|....
gi 71987364  378 FVIDEDFMKAVRKV 391
Cdd:PRK10733 379 VVSMVEFEKAKDKI 392
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
158-318 5.22e-63

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: 199.43  E-value: 5.22e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 158 QIRELREVVELPLINPELFKRvGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFN 237
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 238 YARDHQPCIVFMDEIDAIGGRRFSEGTSADReiQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIE 317
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDSSGESGEL--RRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 71987364 318 I 318
Cdd:cd19481 158 F 158
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
70-379 3.11e-62

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: 208.79  E-value: 3.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364    70 VGQIVgeVLKQLSEE-KFIVKATNGPRYVVGCRRSINKEELKQGTRVSLDMTTLTIMRQLPR-EVDPLVYkmshEDPGNI 147
Cdd:TIGR03689 106 TGEIV--TLKEVLDDgRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGYAFEAIPRtEVEDLVL----EEVPDV 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   148 SYSDVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLdCN-----------FLKVV 216
Cdd:TIGR03689 180 TYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSL-AArigaegggksyFLNIK 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   217 SSAIVDKYIGESARMIREMFNYAR----DHQPCIVFMDEIDAIGGRRFSeGTSADREiqRTLM-ELLNQLDGFDSLGKVK 291
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRARekasEGRPVIVFFDEMDSLFRTRGS-GVSSDVE--TTVVpQLLAEIDGVESLDNVI 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   292 VIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHsnkITKHGEIDFE-AVVKLSDGFSAADLRNVCTEAgMF 370
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY---LTDDLPLPEDlAAHDGDREATAAALIQRVVDA-LY 411

                  ....*....
gi 71987364   371 AIRAEREFV 379
Cdd:TIGR03689 412 ARSEANRYV 420
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
151-319 1.49e-60

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: 193.42  E-value: 1.49e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESAR 230
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 231 MIREMFNYARDHQPCIVFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPG 310
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 71987364 311 RLDRKIEIG 319
Cdd:cd19519 158 RFDREIDIG 166
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
150-402 1.08e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 188.94  E-value: 1.08e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 150 SDVGGLAEQIRELREVVElPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESA 229
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 230 RMIREMFNYARDHqPCIVFMDEIDAIGGRRFSegTSADREIQRTLMELLNQLDGFDSlgKVKVIMATNRPDTLDPALLRp 309
Cdd:COG1223  81 RNLRKLFDFARRA-PCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 310 gRLDRKIEIGLPNEQSRLEILKIHSNKITKHGEIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMKAVR 389
Cdd:COG1223 155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233
                       250
                ....*....|...
gi 71987364 390 KVGDAKRLETKLD 402
Cdd:COG1223 234 QRKERKKEPKKEG 246
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
160-318 1.83e-52

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: 172.69  E-value: 1.83e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 160 RELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYA 239
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71987364 240 RDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEI 318
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
188-320 2.95e-52

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 170.85  E-value: 2.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   188 LLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGtsaD 267
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG---D 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71987364   268 REIQRTLMELLNQLDGFDSL-GKVKVIMATNRPDTLDPALLrpGRLDRKIEIGL 320
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
151-316 5.84e-52

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: 171.43  E-value: 5.84e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESAR 230
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 231 MIREMFNYARDHQPCIVFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQLDGF----DSLGKVKVIMATNRPDTLDPAL 306
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 71987364 307 LRPGRLDRKI 316
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
151-315 1.61e-49

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: 165.38  E-value: 1.61e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVV-----SSAIVDKYI 225
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 226 GESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqLDGFDSLGKVKVIMATNRPDTLDPA 305
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157
                       170
                ....*....|
gi 71987364 306 LLRPGRLDRK 315
Cdd:cd19517 158 LRRPGRFDRE 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
157-314 1.33e-48

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: 162.66  E-value: 1.33e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 157 EQIR-ELREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREM 235
Cdd:cd19530   2 DHVReELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71987364 236 FNYARDHQPCIVFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDR 314
Cdd:cd19530  82 FQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
152-318 2.21e-48

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: 162.14  E-value: 2.21e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 152 VGGLAEQIRELREVVELPLINPELFKRvGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARM 231
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPG-LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 232 IREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIqRTlmELLNQLDGF--DSLGKVKVIMATNRPDTLDPALLRp 309
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155

                ....*....
gi 71987364 310 gRLDRKIEI 318
Cdd:cd19509 156 -RFEKRIYI 163
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
162-317 6.49e-47

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: 157.98  E-value: 6.49e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 162 LREVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARD 241
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71987364 242 HQPCIVFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIE 317
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTGV---TDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
161-314 5.84e-45

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: 153.05  E-value: 5.84e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 161 ELREVVELPLINPELFKRvGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYAR 240
Cdd:cd19527   4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71987364 241 DHQPCIVFMDEIDAIGGRRFSEGTSADrEIQRTLMELLNQLDGFDSLGK-VKVIMATNRPDTLDPALLRPGRLDR 314
Cdd:cd19527  83 DAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
151-318 3.62e-43

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: 148.34  E-value: 3.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKRVGIT-PPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESA 229
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 230 RMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqLDGFDSLGKVKVIM--ATNRPDTLDPALL 307
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSL---WDGLSTDGNCRVIVmgATNRPQDLDEAIL 157
                       170
                ....*....|.
gi 71987364 308 RpgRLDRKIEI 318
Cdd:cd19520 158 R--RMPKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
151-318 4.88e-42

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: 145.51  E-value: 4.88e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKrvGITPP-KGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESA 229
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 230 RMIREMFNYARDHQPCIVFMDEIDAIGGRRfseGTSADREIQRTLM-ELLNQLDGF-------DSLGKVKVIMATNRPDT 301
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEASRRVKsELLVQMDGVggasendDPSKMVMVLAATNFPWD 155
                       170
                ....*....|....*..
gi 71987364 302 LDPALLRpgRLDRKIEI 318
Cdd:cd19522 156 IDEALRR--RLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
146-318 2.02e-39

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: 138.84  E-value: 2.02e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 146 NISYSDVGGLAEQIRELREVVELPLINPELFKRvGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYI 225
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 226 GESARMIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADREIQrtlMELLNQLDGF--DSLGkVKVIMATNRPDTLD 303
Cdd:cd19521  82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIK---TELLVQMNGVgnDSQG-VLVLGATNIPWQLD 157
                       170
                ....*....|....*
gi 71987364 304 PALLRpgRLDRKIEI 318
Cdd:cd19521 158 SAIRR--RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
139-318 2.25e-39

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: 139.35  E-value: 2.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 139 MSHEDPgnISYSDVGGLAEQIRELREVVELPLINPELFkrVGI-TPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVS 217
Cdd:cd19525  13 MDHGPP--INWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLrGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 218 SAIVDKYIGESARMIREMFNYARDHQPCIVFMDEIDAIGGRRfseGTSADREIQRTLMELLNQLDGFDSLG--KVKVIMA 295
Cdd:cd19525  89 SSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATTSSedRILVVGA 165
                       170       180
                ....*....|....*....|...
gi 71987364 296 TNRPDTLDPALLRpgRLDRKIEI 318
Cdd:cd19525 166 TNRPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
151-316 9.97e-37

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: 131.51  E-value: 9.97e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFkrVGI-TPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESA 229
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELF--TGLrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 230 RMIREMFNYARDHQPCIVFMDEIDAIggrrFSEGTSADREIQRTL-MELLNQLDGFDSLG--KVKVIMATNRPDTLDPAL 306
Cdd:cd19524  79 KLVRALFAVARELQPSIIFIDEVDSL----LSERSEGEHEASRRLkTEFLIEFDGVQSNGddRVLVMGATNRPQELDDAV 154
                       170
                ....*....|
gi 71987364 307 LRpgRLDRKI 316
Cdd:cd19524 155 LR--RFTKRV 162
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
152-318 1.71e-32

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: 120.67  E-value: 1.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 152 VGGLAEQIREL-REVVELPLINPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSS-AIVDKYIGESA 229
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGpEILNKYVGESE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 230 RMIREMFNYARDHQPC--------IVFMDEIDAIGGRRFSEGTSADREiQRTLMELLNQLDGFDSLGKVKVIMATNRPDT 301
Cdd:cd19504  82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGSTGVH-DTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                       170
                ....*....|....*..
gi 71987364 302 LDPALLRPGRLDRKIEI 318
Cdd:cd19504 161 IDEALLRPGRLEVQMEI 177
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
151-308 2.93e-29

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: 111.51  E-value: 2.93e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 151 DVGGLAEQIRELREVVELPLINPELFKRVgITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESAR 230
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 231 MIREMFNYARDHQPCIVFMDEIDAIGGRRFSEGTSADReIQrtlMELLNQLDGFDSLGK--VKVIMATNRPDTLDPALLR 308
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGR-LQ---VELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
153-320 2.30e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 100.68  E-value: 2.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 153 GGLAEQIRELREVVELPlinpelfkrvgitPPKGCLLFGPPGTGKTLLARAVASQL---DCNFLKVVSSAIVDKYIGESA 229
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 230 R---MIREMFNYARDHQPCIVFMDEIDAIGgrrfsegtsadREIQRTLMELLNQL-DGFDSLGKVKVIMATNRPDTLDPA 305
Cdd:cd00009  68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136
                       170
                ....*....|....*
gi 71987364 306 LLRPGRLDRKIEIGL 320
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
180-391 3.79e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 107.03  E-value: 3.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  180 GITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEID-AIGGR 258
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  259 RFS--EGTSAdreiqRTLMELLNQLDGFDSlgKVKVIMATNRPDTLDPALLRPGRLDRKIEIGLPNEQSRLEILKIHSNK 336
Cdd:CHL00195 335 ESKgdSGTTN-----RVLATFITWLSEKKS--PVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQK 407
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71987364  337 ITKHG--EIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDeDFMKAVRKV 391
Cdd:CHL00195 408 FRPKSwkKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTD-DILLALKQF 463
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
177-314 3.90e-22

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: 92.05  E-value: 3.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 177 KRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESARMIREMFNYARDHQPCIVFMDEID-AI 255
Cdd:cd19507  24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGF 103
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987364 256 GGRRFS--EGTSAdreiqRTLMELLNQLDgfDSLGKVKVIMATNRPDTLDPALLRPGRLDR 314
Cdd:cd19507 104 SNADSKgdSGTSS-----RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
172-318 5.84e-21

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: 88.56  E-value: 5.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 172 NPELFKRVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDkyigeSARMIREMFNYARdhQPCIVFMDE 251
Cdd:cd19510  11 NEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTAP--KQSIILLED 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 252 IDA---IGGRRFSEGTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPGRLDRKIEI 318
Cdd:cd19510  84 IDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
183-322 3.26e-19

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: 83.58  E-value: 3.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364    183 PPKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVS-----------------SAIVDKYIGESARMIREMFNYARDHQPC 245
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71987364    246 IVFMDEIDAIggrrfsegTSADREIQRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPALLRPgRLDRKIEIGLPN 322
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
342-386 1.27e-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: 59.09  E-value: 1.27e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 71987364   342 EIDFEAVVKLSDGFSAADLRNVCTEAGMFAIRAEREFVIDEDFMK 386
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
178-318 1.54e-11

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: 62.39  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 178 RVGITPPKGCLLFGPPGTGKTLLARAVASQLDCNFLKV--------------VSSAIVDKYIGESARMIREMFNYARDHQ 243
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRIslnkllynkpdfgnDDWIDGMLILKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71987364 244 PCIVFMDEIDAIGGRRFSEGTSADReiqRTLMELLNQLDGFDSLGKVK----VIMATNRPDTLDPALLRPGRLDRKIEI 318
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
188-306 2.35e-11

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 62.46  E-value: 2.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 188 LLFGPPGTGKTLLARAVASQLD---------CNFLKVVSSAIVDKYIGESARMIREMFNYAR---DHQPCIVF--MDEID 253
Cdd:cd19508  56 LLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQeliDDKDALVFvlIDEVE 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71987364 254 AIGGRR--FSEGTSADREIqRTLMELLNQLDGFDSLGKVKVIMATNRPDTLDPAL 306
Cdd:cd19508 136 SLAAARsaSSSGTEPSDAI-RVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
74-129 2.80e-11

Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 58.29  E-value: 2.80e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 71987364    74 VGEVLKQLSEEKFIVKATNGPRYVVGCRRSINKEELKQGTRVSLDMTTLTIMRQLP 129
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
187-252 4.61e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.87  E-value: 4.61e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  187 CLLFGPPGTGKTLLARAVASQLDCNFLKVvsSAIVDKyIGEsarmIREMFNYARDH----QPCIVFMDEI 252
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAL--SAVTSG-VKD----LREVIEEARQRrsagRRTILFIDEI 101
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
155-317 5.29e-10

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: 57.54  E-value: 5.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 155 LAEQIRELREVVELPLINPELFKRVgitppkgcLLFGPPGTGKTLLARAVA--SQLDcnfLKVVSSAIVDKYIGESARMI 232
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNI--------LFYGPPGTGKTLFAKKLAlhSGMD---YAIMTGGDVAPMGREGVTAI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 233 REMFNYA-RDHQPCIVFMDEIDAIGGRRFSEGTSADreIQRTLMELLNQLDgfDSLGKVKVIMATNRPDTLDPALlrPGR 311
Cdd:cd19512  70 HKVFDWAnTSRRGLLLFVDEADAFLRKRSTEKISED--LRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDR 143

                ....*.
gi 71987364 312 LDRKIE 317
Cdd:cd19512 144 IDEMVE 149
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
184-278 4.89e-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: 55.46  E-value: 4.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 184 PKGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVD-KYIGesarmiREMFNYARDHQPCIVFMDEIDAIGGRRFSE 262
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119
                        90
                ....*....|....*..
gi 71987364 263 GTSADRE-IQRTLMELL 278
Cdd:cd19498 120 GPDVSREgVQRDLLPIV 136
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
188-261 6.73e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 57.37  E-value: 6.73e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987364 188 LLFGPPGTGKTLLARAVASQLDCNFLKVvsSAIVDKyIGEsarmIREMFNYARDH----QPCIVFMDEIDaiggrRFS 261
Cdd:COG2256  53 ILWGPPGTGKTTLARLIANATDAEFVAL--SAVTSG-VKD----IREVIEEARERraygRRTILFVDEIH-----RFN 118
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
188-278 9.60e-08

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 52.60  E-value: 9.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 188 LLFGPPGTGKTLLARAVASQLDCNFlkvvssAIVDK-------YIGES-----ARMIRE-MFNYARdHQPCIVFMDEIDA 254
Cdd:cd19497  54 LLIGPTGSGKTLLAQTLAKILDVPF------AIADAttlteagYVGEDvenilLKLLQAaDYDVER-AQRGIVYIDEIDK 126
                        90       100
                ....*....|....*....|....*....
gi 71987364 255 IGgrRFSEGTSADRE-----IQRTLMELL 278
Cdd:cd19497 127 IA--RKSENPSITRDvsgegVQQALLKIL 153
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
157-307 1.03e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 53.70  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 157 EQIRELREVVElPLINPElfkrvgitPPKGCLLFGPPGTGKTLLARAVASQL---------DCNFLKV----------VS 217
Cdd:COG1474  33 EEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEELeeeaeergvDVRVVYVncrqastryrVL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 218 SAIVDKYIGE---------SARMIREMFNYARDH-QPCIVFMDEIDAIGgrrfsegtsaDREIQRTLMELLNQLDGFDSl 287
Cdd:COG1474 104 SRILEELGSGedipstglsTDELFDRLYEALDERdGVLVVVLDEIDYLV----------DDEGDDLLYQLLRANEELEG- 172
                       170       180
                ....*....|....*....|...
gi 71987364 288 GKVKVIMATNRP---DTLDPALL 307
Cdd:COG1474 173 ARVGVIGISNDLeflENLDPRVK 195
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
154-317 1.82e-07

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: 52.92  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   154 GLAE---QIRELREVVELPLINPELFKRVGITPpKGCLLFGPPGTGKTLLARAVASQLdC--------NFLKVVSSAIVD 222
Cdd:TIGR03922 280 GLERvkrQVAALKSSTAMALARAERGLPVAQTS-NHMLFAGPPGTGKTTIARVVAKIY-CglgvlrkpLVREVSRADLIG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   223 KYIGESARMIREMFNYARDHqpcIVFMDEIDAIGGRRFSEGTSADREIQRTL---MEllNQLDGFdslgkvKVIMATNRP 299
Cdd:TIGR03922 358 QYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEAIDTLlarME--NDRDRL------VVIGAGYRK 426
                         170       180
                  ....*....|....*....|...
gi 71987364   300 DtLDPAL-----LRpGRLDRKIE 317
Cdd:TIGR03922 427 D-LDKFLevnegLR-SRFTRVIE 447
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
185-299 1.42e-06

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 47.91  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 185 KGCLLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIGESA--RMIREMFNYARDHQPCIVFMDEIDAIGGRRF-- 260
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGlqMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVpk 106
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71987364 261 SEGTSADREIQRTLMELLNQLDGFDslgKVKVIMATNRP 299
Cdd:cd19506 107 TEKQLDPKRLKKDLPKILKSLKPED---RVLIVGTTSRP 142
PRK04195 PRK04195
replication factor C large subunit; Provisional
183-299 7.16e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.99  E-value: 7.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  183 PPKGCLLFGPPGTGKTLLARAVASQLDcnfLKVV--------SSAIVDKYIGESARMiREMFNYARDhqpcIVFMDEIDA 254
Cdd:PRK04195  38 PKKALLLYGPPGVGKTSLAHALANDYG---WEVIelnasdqrTADVIERVAGEAATS-GSLFGARRK----LILLDEVDG 109
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 71987364  255 IGGRrfsegtsADREIQRTLMELLNQldgfdslGKVKVIMATNRP 299
Cdd:PRK04195 110 IHGN-------EDRGGARAILELIKK-------AKQPIILTANDP 140
44 PHA02544
clamp loader, small subunit; Provisional
184-382 8.95e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 47.29  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  184 PKGCLLFGPPGTGKTLLARAVASQLDCNFLKVvssaivdkyIGESARM--IR-EMFNYA----RDHQPCIVFMDEIDaig 256
Cdd:PHA02544  43 PNMLLHSPSPGTGKTTVAKALCNEVGAEVLFV---------NGSDCRIdfVRnRLTRFAstvsLTGGGKVIIIDEFD--- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  257 grrfSEGTSADREIQRTLMELLNqldgfdslGKVKVIMATNRPDTLDPALLrpGRLdRKIEIGLPNEQSRLEILK--IH- 333
Cdd:PHA02544 111 ----RLGLADAQRHLRSFMEAYS--------KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMMKqmIVr 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71987364  334 SNKITKHGEIDFE-----AVVKlsDGFsaADLRNVCTEAGMFAIRAErefvIDE 382
Cdd:PHA02544 176 CKGILEAEGVEVDmkvlaALVK--KNF--PDFRRTINELQRYASTGK----IDA 221
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
188-307 1.97e-05

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: 44.86  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 188 LLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDK---------YIGE-SARMIREMFNyARDHQPciVFM-DEIDAIG 256
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmPGRIIQALKK-AGTNNP--VFLlDEIDKIG 117
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71987364 257 GRRFSEGTSAdreiqrtLMELL----------NQLD-GFDsLGKVKVIMATNRPDTLDPALL 307
Cdd:cd19500 118 SSFRGDPASA-------LLEVLdpeqnstfsdHYLDvPFD-LSKVLFIATANSLDTIPGPLL 171
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
184-297 3.33e-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: 44.11  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   184 PKGCLLF-GPPGTGKTLLARAVASQLD---CNFLKVVSSA-----IVDKYIGESARMIR-----EMFNYARDHQPCIVFM 249
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELLFgdeRALIRIDMSEymeehSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 71987364   250 DEIDaiggrrfsegtSADREIQRTlmeLLNQLDG---FDSLG-KVK-----VIMATN 297
Cdd:pfam07724  82 DEIE-----------KAHPGVQND---LLQILEGgtlTDKQGrTVDfkntlFIMTGN 124
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
188-303 5.09e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 42.49  E-value: 5.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 188 LLFGPPGTGKTLLARAVASQLDCNFLKVVSSAIVDKYIgesaRMIREmfnYARDHQPCIVFMDEIDAIGGRRFSEGTSAD 267
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARASQGDRSSEL 74
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71987364 268 REIQRTLMELLNQLDgfdslgkvKVIMATNRPDTLD 303
Cdd:cd01120  75 LEDLAKLLRAARNTG--------ITVIATIHSDKFD 102
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
188-270 6.84e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.76  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  188 LLFGPPGTGKTLLARAVASQLDCNFlkvvssAIVD-------KYIGESARMIREMFNYARDH-----QPCIVFMDEIDAI 255
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPF------AIADattlteaGYVGEDVENILLKLLQAADYdvekaQRGIVYIDEIDKI 185
                         90
                 ....*....|....*
gi 71987364  256 GgrRFSEGTSADREI 270
Cdd:PRK05342 186 A--RKSENPSITRDV 198
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
169-276 1.23e-04

ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213250 [Multi-domain]  Cd Length: 199  Bit Score: 42.67  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 169 PLINPElfKRVG----ITPPKGCLLFGPPGTGKTLLARAV--------------ASQLDCNFLKVVSSAIV--DKYIGES 228
Cdd:cd03283   8 PLIGRE--KRVAndidMEKKNGILITGSNMSGKSTFLRTIgvnvilaqagapvcASSFELPPVKIFTSIRVsdDLRDGIS 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 71987364 229 -----ARMIREMFNYARDHQPCIVFMDEIdaIGGRRFSEGTSADREIQRTLME 276
Cdd:cd03283  86 yfyaeLRRLKEIVEKAKKGEPVLFLLDEI--FKGTNSRERQAASAAVLKFLKN 136
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
187-212 1.80e-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: 42.85  E-value: 1.80e-04
                        10        20
                ....*....|....*....|....*.
gi 71987364 187 CLLFGPPGTGKTLLARAVASQLDCNF 212
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPF 59
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
188-265 2.27e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 43.11  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 188 LLFGPPGTGKTLLARAVASQLDCNFlkvvssAIVDK-------YIGES-----ARMIRemfnyARDH-----QPCIVFMD 250
Cdd:COG1219 113 LLIGPTGSGKTLLAQTLARILDVPF------AIADAttlteagYVGEDvenilLKLLQ-----AADYdvekaERGIIYID 181
                        90
                ....*....|....*
gi 71987364 251 EIDAIGgrRFSEGTS 265
Cdd:COG1219 182 EIDKIA--RKSENPS 194
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
187-217 5.19e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 5.19e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 71987364  187 CLLFGPPGTGKTLLARAVASQLDCNfLKVVS 217
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITS 83
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
187-223 9.31e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 40.75  E-value: 9.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 71987364   187 CLLFGPPGTGKTLLARAVASQLDCNfLKVVSSAIVDK 223
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK 68
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
157-391 1.44e-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: 40.31  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   157 EQIRELREvvelpLINPELFkrvGITPPKgCLLFGPPGTGKTLLARAVASQL----------------DCNFLKVVSSAI 220
Cdd:TIGR02928  22 EQIEELAK-----ALRPILR---GSRPSN-VFIYGKTGTGKTAVTKYVMKELeeaaedrdvrvvtvyvNCQILDTLYQVL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   221 VdkYIGESARMI---------------REMFNYARDHQPCIVF-MDEIDAIGGrrfsegtsadrEIQRTLMELL-----N 279
Cdd:TIGR02928  93 V--ELANQLRGSgeevpttglstsevfRRLYKELNERGDSLIIvLDEIDYLVG-----------DDDDLLYQLSrarsnG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   280 QLDGfdslGKVKVIMATNRPDTLDpallrpgRLDRKI-------EIGLP--NEQSRLEILKIHSNKITKHGEIDfEAVVK 350
Cdd:TIGR02928 160 DLDN----AKVGVIGISNDLKFRE-------NLDPRVksslceeEIIFPpyDAEELRDILENRAEKAFYDGVLD-DGVIP 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71987364   351 LSDGFSAAD----------LRnvctEAGMFAIRAEREFVIDEDFMKAVRKV 391
Cdd:TIGR02928 228 LCAALAAQEhgdarkaidlLR----VAGEIAEREGAERVTEDHVEKAQEKI 274
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
154-208 4.63e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.87  E-value: 4.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71987364   154 GLAEQIRELREvvelplinpeLFKRVGITPPKGCLLFGPPGTGKTLLARAVASQL 208
Cdd:pfam13191   4 GREEELEQLLD----------ALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRAL 48
PRK13341 PRK13341
AAA family ATPase;
188-252 4.66e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 4.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987364  188 LLFGPPGTGKTLLARAVASQLDCNF--LKVVSSAIVD-KYIGESARMIREMFNyardhQPCIVFMDEI 252
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFssLNAVLAGVKDlRAEVDRAKERLERHG-----KRTILFIDEV 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
187-212 4.75e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.91  E-value: 4.75e-03
                        10        20
                ....*....|....*....|....*.
gi 71987364 187 CLLFGPPGTGKTLLARAVASQLDCNF 212
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
PLN00020 PLN00020
ribulose bisphosphate carboxylase/oxygenase activase -RuBisCO activase (RCA); Provisional
166-392 5.74e-03

ribulose bisphosphate carboxylase/oxygenase activase -RuBisCO activase (RCA); Provisional


Pssm-ID: 215031 [Multi-domain]  Cd Length: 413  Bit Score: 38.54  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  166 VELPLInpelfkrVGITPPKGCllfgppgtGKTLLARAVASQLDCNflKVVSSA--IVDKYIGESARMIREMFNYARDH- 242
Cdd:PLN00020 145 IKVPLI-------LGIWGGKGQ--------GKSFQCELVFKKMGIE--PIVMSAgeLESENAGEPGKLIRQRYREAADIi 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  243 ----QPCIVFMDEIDAIGGR-RFSEGTSADREIQRTLMELLN-----QLDGF----DSLGKVKVIMATNRPDTLDPALLR 308
Cdd:PLN00020 208 kkkgKMSCLFINDLDAGAGRfGTTQYTVNNQMVNGTLMNIADnptnvSLGGDwrekEEIPRVPIIVTGNDFSTLYAPLIR 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364  309 PGRLDRKieIGLPNEQSRLEILKihsnKITKHGEIDFEAVVKLSDGFSAADLRnvcteagmF--AIRAErefVIDEDFMK 386
Cdd:PLN00020 288 DGRMEKF--YWAPTREDRIGVVH----GIFRDDGVSREDVVKLVDTFPGQPLD--------FfgALRAR---VYDDEVRK 350

                 ....*.
gi 71987364  387 AVRKVG 392
Cdd:PLN00020 351 WIAEVG 356
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
187-255 5.77e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.04  E-value: 5.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364   187 CLLFGPPGTGKTLLARAVASQLdCNFLKVVSSAIvdkYIGESArmiREMFN-YarDHQPCIVfMDEIDAI 255
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSV---YSRNPD---DDFWDgY--TGQPVVI-IDDFGQN 60
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
189-293 6.87e-03

RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410897 [Multi-domain]  Cd Length: 209  Bit Score: 37.62  E-value: 6.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987364 189 LFGPPGTGKTLL----ARAVASQLDCNFLkvvssaIVDKYIGESARMIREMFNYARDHQpcivfmDEIDAIGGR-RFSEG 263
Cdd:cd19489  12 LVGESSSGKTQLcltaAANVASRSGQNVL------YIDTKSSFSARRLAQILKSRAQDA------EEIDKALQRiRVVRV 79
                        90       100       110
                ....*....|....*....|....*....|..
gi 71987364 264 TSAdREIQRTLMELLNQL--DGFDSLGKVKVI 293
Cdd:cd19489  80 FDP-YELLDLLEELRNTLsqQQENLYSRLKLV 110
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
188-223 7.19e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.09  E-value: 7.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 71987364   188 LLFGPPGTGKTLLARAVASQLDCNFlKVVSSAIVDK 223
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER 71
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
188-210 8.39e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 37.65  E-value: 8.39e-03
                        10        20
                ....*....|....*....|...
gi 71987364 188 LLFGPPGTGKTLLARAVASQLDC 210
Cdd:COG0470  22 LLHGPPGIGKTTLALALARDLLC 44
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
185-208 8.85e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 38.03  E-value: 8.85e-03
                        10        20
                ....*....|....*....|....
gi 71987364 185 KGCLLFGPPGTGKTLLARAVASQL 208
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIAREL 88
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
188-208 9.76e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.21  E-value: 9.76e-03
                        10        20
                ....*....|....*....|.
gi 71987364 188 LLFGPPGTGKTLLARAVASQL 208
Cdd:COG1401 225 ILAGPPGTGKTYLARRLAEAL 245
 
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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