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Conserved domains on  [gi|63054416|ref|NP_587809|]
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proteasome regulatory subunit Rpt4 [Schizosaccharomyces pombe]

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
3-373 1.75e-165

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 468.54  E-value: 1.75e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    3 ERDTALEKYKSYL-LQHREWDSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQIIGEVLKQLDSERFIVKASSGPRYVVG 81
Cdd:PRK03992   1 ERLEALEERNSELeEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   82 CRNNVDQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRV 161
Cdd:PRK03992  81 VSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  162 GIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRR 241
Cdd:PRK03992 161 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  242 FSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSK 321
Cdd:PRK03992 241 TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054416  322 QGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:PRK03992 321 ADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKV 372
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
3-373 1.75e-165

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 468.54  E-value: 1.75e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    3 ERDTALEKYKSYL-LQHREWDSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQIIGEVLKQLDSERFIVKASSGPRYVVG 81
Cdd:PRK03992   1 ERLEALEERNSELeEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   82 CRNNVDQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRV 161
Cdd:PRK03992  81 VSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  162 GIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRR 241
Cdd:PRK03992 161 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  242 FSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSK 321
Cdd:PRK03992 241 TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054416  322 QGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:PRK03992 321 ADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKV 372
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
18-373 2.99e-140

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: 403.80  E-value: 2.99e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    18 HREWDSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQ-------IIGEVLKQLDSERFIVKASSGPRYVVGCRNNVDQSH 90
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIErlrspplIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    91 LVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVL 170
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   171 LYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADR 250
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   251 EIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEAL 330
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 63054416   331 VKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
87-373 4.15e-134

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 386.67  E-value: 4.15e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  87 DQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPP 166
Cdd:COG1222  33 LQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 167 KGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGT 246
Cdd:COG1222 113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGT 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 247 SAdrEIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEID 326
Cdd:COG1222 193 SG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVD 270
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 63054416 327 YEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:COG1222 271 LDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKV 317
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
130-300 4.84e-106

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: 309.27  E-value: 4.84e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 130 SFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGE 209
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 210 SARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALL 289
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 63054416 290 RPGRLDRKIEI 300
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
169-302 1.84e-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: 1.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   169 VLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGtsa 248
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG--- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63054416   249 DREIQRTLMELLNQMDGFDYL-GQTKIIMATNRPDTLDPALLrpGRLDRKIEIPL 302
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
165-304 3.17e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 80.88  E-value: 3.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    165 PPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVS-----------------SAIVDKYIGESARIIREMFGYAKEHEPC 227
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054416    228 VIFMDEIDAIggrrfsegTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPgRLDRKIEIPLPN 304
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
3-373 1.75e-165

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 468.54  E-value: 1.75e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    3 ERDTALEKYKSYL-LQHREWDSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQIIGEVLKQLDSERFIVKASSGPRYVVG 81
Cdd:PRK03992   1 ERLEALEERNSELeEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   82 CRNNVDQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRV 161
Cdd:PRK03992  81 VSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  162 GIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRR 241
Cdd:PRK03992 161 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  242 FSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSK 321
Cdd:PRK03992 241 TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 63054416  322 QGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:PRK03992 321 ADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKV 372
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
18-373 2.99e-140

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: 403.80  E-value: 2.99e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    18 HREWDSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQ-------IIGEVLKQLDSERFIVKASSGPRYVVGCRNNVDQSH 90
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIErlrspplIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    91 LVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVL 170
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   171 LYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADR 250
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   251 EIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEAL 330
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 63054416   331 VKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
87-373 4.15e-134

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 386.67  E-value: 4.15e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  87 DQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPP 166
Cdd:COG1222  33 LQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 167 KGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGT 246
Cdd:COG1222 113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGT 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 247 SAdrEIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEID 326
Cdd:COG1222 193 SG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVD 270
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 63054416 327 YEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKV 373
Cdd:COG1222 271 LDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKV 317
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
8-378 2.16e-112

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 335.59  E-value: 2.16e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    8 LEKYKSYLLQHREW---DSKLKDLRFGNRDLVKKYDKTEDDIKSLQSVGQIIgevlkqlDSERFIVKASSGPRYVVGCRN 84
Cdd:PTZ00361  63 LERIKDYLLLEEEFitnQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEII-------DENHAIVSSSVGPEYYVNILS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   85 NVDQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIK 164
Cdd:PTZ00361 136 FVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIK 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  165 PPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSE 244
Cdd:PTZ00361 216 PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDA 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  245 GTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGE 324
Cdd:PTZ00361 296 TSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAED 375
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 63054416  325 IDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKVADLKK 378
Cdd:PTZ00361 376 VDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKK 429
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
33-385 7.84e-110

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 327.49  E-value: 7.84e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   33 RDLVKKYDKTEDDIKSLQSVGQIIGEVLKQLDSERFIVKASSGPRYVVGCRNNVDQSHLVQGVRVSLDMTTLTIMRILPR 112
Cdd:PTZ00454  46 KNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPP 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  113 EVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGV 192
Cdd:PTZ00454 126 EADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  193 NFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQT 272
Cdd:PTZ00454 206 TFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNV 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  273 KIIMATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFI 352
Cdd:PTZ00454 286 KVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQ 365
                        330       340       350
                 ....*....|....*....|....*....|...
gi 63054416  353 AIKEDRDYVIQSDLMSAARKVadLKKLEGTIDY 385
Cdd:PTZ00454 366 AVRKNRYVILPKDFEKGYKTV--VRKTDRDYDF 396
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
130-300 4.84e-106

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: 309.27  E-value: 4.84e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 130 SFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGE 209
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 210 SARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALL 289
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 63054416 290 RPGRLDRKIEI 300
Cdd:cd19502 161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
86-378 1.19e-82

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: 257.92  E-value: 1.19e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  86 VDQSHLVQGVRVSLDMTTLTIMRILPREVDPLVYNMSIEDPGDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKP 165
Cdd:COG0464 111 LLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPP 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 166 PKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRfseG 245
Cdd:COG0464 191 PRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---G 267
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 246 TSADREIQRTLMELLNQMDGFDYlgQTKIIMATNRPDTLDPALLRpgRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEI 325
Cdd:COG0464 268 EVGDGVGRRVVNTLLTEMEELRS--DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDV 343
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 63054416 326 DYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKVADLKK 378
Cdd:COG0464 344 DLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALEREDIFLK 396
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
121-373 5.18e-81

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: 256.44  E-value: 5.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   121 MSIEDPGDISFAGVGGLNEQIRELREVIELpLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSS 200
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   201 AIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNR 280
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   281 PDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDY 360
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282
                         250
                  ....*....|...
gi 63054416   361 VIQSDLMSAARKV 373
Cdd:TIGR01241 283 ITMNDIEEAIDRV 295
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
124-373 3.91e-79

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 254.19  E-value: 3.91e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 124 EDPGDISFAGVGGLNEQIRELREVIELpLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIV 203
Cdd:COG0465 134 EDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 204 DKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFS--EGTSADREiqRTLMELLNQMDGFDylGQTKIIM--ATN 279
Cdd:COG0465 213 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglGGGHDERE--QTLNQLLVEMDGFE--GNEGVIViaATN 288
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 280 RPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRD 359
Cdd:COG0465 289 RPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKK 368
                       250
                ....*....|....
gi 63054416 360 YVIQSDLMSAARKV 373
Cdd:COG0465 369 AVTMEDFEEAIDRV 382
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
133-300 3.51e-71

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: 220.24  E-value: 3.51e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 133 GVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESAR 212
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 213 IIREMFGYAKEHEPCVIFMDEIDAIGGRRfsegTSADREI-QRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRP 291
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVeRRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 63054416 292 GRLDRKIEI 300
Cdd:cd19503 157 GRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
123-380 1.26e-70

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: 235.19  E-value: 1.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   123 IEDPgDISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAI 202
Cdd:TIGR01243 445 VEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEI 523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   203 VDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIG---GRRFSEGTSadreiQRTLMELLNQMDGFDYLGQTKIIMATN 279
Cdd:TIGR01243 524 LSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAparGARFDTSVT-----DRIVNQLLTEMDGIQELSNVVVIAATN 598
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   280 RPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRD 359
Cdd:TIGR01243 599 RPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIG 678
                         250       260
                  ....*....|....*....|.
gi 63054416   360 YVIQSDLMSAARKVADLKKLE 380
Cdd:TIGR01243 679 SPAKEKLEVGEEEFLKDLKVE 699
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
129-300 1.75e-68

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: 213.63  E-value: 1.75e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 129 ISFAGVGGLNEQIRELREVIELpLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIG 208
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 209 ESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPAL 288
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 63054416 289 LRPGRLDRKIEI 300
Cdd:cd19501 160 LRPGRFDRQVYV 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
128-355 9.55e-67

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: 224.79  E-value: 9.55e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   128 DISFAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYI 207
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   208 GESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPA 287
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054416   288 LLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIK 355
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
142-298 7.15e-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: 203.67  E-value: 7.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 142 RELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYA 221
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054416 222 KEHEPCVIFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKI 298
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
ftsH CHL00176
cell division protein; Validated
128-382 3.54e-64

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 216.07  E-value: 3.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  128 DISFAGVGGLNEQIRELREVIELpLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYI 207
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  208 GESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPA 287
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAA 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  288 LLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLM 367
Cdd:CHL00176 338 LLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEID 417
                        250
                 ....*....|....*
gi 63054416  368 SAARKVadLKKLEGT 382
Cdd:CHL00176 418 TAIDRV--IAGLEGT 430
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
121-373 6.46e-63

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 212.97  E-value: 6.46e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  121 MSIEDPGDISFAGVGGLNEQIRELREVIELpLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSS 200
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  201 AIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNR 280
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  281 PDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDY 360
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                        250
                 ....*....|...
gi 63054416  361 VIQSDLMSAARKV 373
Cdd:PRK10733 380 VSMVEFEKAKDKI 392
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
142-300 1.75e-62

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: 197.72  E-value: 1.75e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 142 RELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYA 221
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054416 222 KEHEPCVIFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEI 300
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
134-301 1.16e-61

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 195.73  E-value: 1.16e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARI 213
Cdd:cd19519   2 IGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 214 IREMFGYAKEHEPCVIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGR 293
Cdd:cd19519  82 LRKAFEEAEKNAPAIIFIDEIDAIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGR 158

                ....*...
gi 63054416 294 LDRKIEIP 301
Cdd:cd19519 159 FDREIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
140-300 2.37e-60

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: 192.11  E-value: 2.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 140 QIRELREVIELPLKNPELfLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFG 219
Cdd:cd19481   1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 220 YAKEHEPCVIFMDEIDAIGGRRFSEGTSADReiQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIE 299
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDSSGESGEL--RRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 63054416 300 I 300
Cdd:cd19481 158 F 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
137-381 4.48e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 194.72  E-value: 4.48e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 137 LNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIRE 216
Cdd:COG1223   6 GQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 217 MFGYAKEhEPCVIFMDEIDAIGGRRFSegTSADREIQRTLMELLNQMDGFDylGQTKIIMATNRPDTLDPALLRpgRLDR 296
Cdd:COG1223  86 LFDFARR-APCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR--RFDE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 297 KIEIPLPNEVGRMEILKIHLEKVSKQGEIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSAARKVADL 376
Cdd:COG1223 159 VIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKER 238

                ....*
gi 63054416 377 KKLEG 381
Cdd:COG1223 239 KKEPK 243
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
52-361 4.18e-59

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: 199.94  E-value: 4.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    52 VGQIIgEVLKQLDSERFIVKASSGPRYVVGCRNNVDQSHLVQGVRVSLDMTTLTIMRILPR-EVDPLVynmsIEDPGDIS 130
Cdd:TIGR03689 106 TGEIV-TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGYAFEAIPRtEVEDLV----LEEVPDVT 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   131 FAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVN----------FLKVVSS 200
Cdd:TIGR03689 181 YADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARigaegggksyFLNIKGP 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   201 AIVDKYIGESARIIREMFGYAKEH----EPCVIFMDEIDAIGGRRFSeGTSADREiqRTLM-ELLNQMDGFDYLGQTKII 275
Cdd:TIGR03689 261 ELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGS-GVSSDVE--TTVVpQLLAEIDGVESLDNVIVI 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   276 MATNRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKIHLEKvskqgEIDYEALVKLTDGTNGAD---LRNVVTEAGFi 352
Cdd:TIGR03689 338 GASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTD-----DLPLPEDLAAHDGDREATaaaLIQRVVDALY- 411

                  ....*....
gi 63054416   353 AIKEDRDYV 361
Cdd:TIGR03689 412 ARSEANRYV 420
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
134-298 4.39e-54

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: 176.44  E-value: 4.39e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARI 213
Cdd:cd19518   2 IGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 214 IREMFGYAKEHEPCVIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQMDGFDYLGQTK----IIMATNRPDTLDPALL 289
Cdd:cd19518  82 IRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELNNEKTAGgpvlVIGATNRPDSLDPALR 158

                ....*....
gi 63054416 290 RPGRLDRKI 298
Cdd:cd19518 159 RAGRFDREI 167
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
169-302 1.84e-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: 1.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   169 VLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGtsa 248
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG--- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63054416   249 DREIQRTLMELLNQMDGFDYL-GQTKIIMATNRPDTLDPALLrpGRLDRKIEIPL 302
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
142-300 5.39e-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: 170.77  E-value: 5.39e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 142 RELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYA 221
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054416 222 KEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEI 300
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
139-296 3.64e-50

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 166.12  E-value: 3.64e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 139 EQIR-ELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREM 217
Cdd:cd19530   2 DHVReELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054416 218 FGYAKEHEPCVIFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDR 296
Cdd:cd19530  82 FQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
144-299 3.77e-48

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: 160.67  E-value: 3.77e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 144 LREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKE 223
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416 224 HEPCVIFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIE 299
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTGV---TDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
134-297 6.28e-48

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 160.75  E-value: 6.28e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLG-----VNFLKVVSSAIVDKYIG 208
Cdd:cd19517   2 IGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWVG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 209 ESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqMDGFDYLGQTKIIMATNRPDTLDPAL 288
Cdd:cd19517  82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPAL 158

                ....*....
gi 63054416 289 LRPGRLDRK 297
Cdd:cd19517 159 RRPGRFDRE 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
134-300 1.31e-47

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: 159.44  E-value: 1.31e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELFlRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARI 213
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 214 IREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIqRTlmELLNQMDGF--DYLGQTKIIMATNRPDTLDPALLRp 291
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155

                ....*....
gi 63054416 292 gRLDRKIEI 300
Cdd:cd19509 156 -RFEKRIYI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
143-296 3.26e-44

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: 150.74  E-value: 3.26e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 143 ELREVIELPLKNPELFlRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAK 222
Cdd:cd19527   4 EILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054416 223 EHEPCVIFMDEIDAIGGRRFSEGTSADrEIQRTLMELLNQMDGFDYLGQ-TKIIMATNRPDTLDPALLRPGRLDR 296
Cdd:cd19527  83 DAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
134-300 1.64e-42

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: 146.42  E-value: 1.64e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELFLRVGI-KPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESAR 212
Cdd:cd19520   2 IGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 213 IIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqMDGFDYLGQTKIIM--ATNRPDTLDPALLR 290
Cdd:cd19520  82 LVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSL---WDGLSTDGNCRVIVmgATNRPQDLDEAILR 158
                       170
                ....*....|
gi 63054416 291 pgRLDRKIEI 300
Cdd:cd19520 159 --RMPKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
134-300 5.37e-41

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: 142.43  E-value: 5.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELFlrVGIKPP-KGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESAR 212
Cdd:cd19522   2 IADLEEAKKLLEEAVVLPMWMPEFF--KGIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 213 IIREMFGYAKEHEPCVIFMDEIDAIGGRRfseGTSADREIQRTL-MELLNQMDGF----DYLGQTKIIM---ATNRPDTL 284
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEASRRVkSELLVQMDGVggasENDDPSKMVMvlaATNFPWDI 156
                       170
                ....*....|....*.
gi 63054416 285 DPALLRpgRLDRKIEI 300
Cdd:cd19522 157 DEALRR--RLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
128-300 1.56e-37

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 133.45  E-value: 1.56e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 128 DISFAGVGGLNEQIRELREVIELPLKNPELFLRvGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYI 207
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 208 GESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADREIQrtlMELLNQMDGFDYLGQTKIIM-ATNRPDTLDP 286
Cdd:cd19521  82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIK---TELLVQMNGVGNDSQGVLVLgATNIPWQLDS 158
                       170
                ....*....|....
gi 63054416 287 ALLRpgRLDRKIEI 300
Cdd:cd19521 159 AIRR--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; ...
121-300 7.00e-37

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 132.42  E-value: 7.00e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 121 MSIEDPgdISFAGVGGLNEQIRELREVIELPLKNPELFlrVGIK-PPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVS 199
Cdd:cd19525  13 MDHGPP--INWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 200 SAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEIDAIGGRRfseGTSADREIQRTLMELLNQMDGFDYLGQTKIIM--A 277
Cdd:cd19525  89 SSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATTSSEDRILVvgA 165
                       170       180
                ....*....|....*....|...
gi 63054416 278 TNRPDTLDPALLRpgRLDRKIEI 300
Cdd:cd19525 166 TNRPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
134-298 1.37e-34

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 125.35  E-value: 1.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 134 VGGLNEQIRELREVIELPLKNPELF--LRvgiKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESA 211
Cdd:cd19524   2 IAGQDLAKQALQEMVILPSLRPELFtgLR---APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 212 RIIREMFGYAKEHEPCVIFMDEIDAIggrrFSEGTSADREIQRTL-MELLNQMDGFDYLGQTKIIM--ATNRPDTLDPAL 288
Cdd:cd19524  79 KLVRALFAVARELQPSIIFIDEVDSL----LSERSEGEHEASRRLkTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAV 154
                       170
                ....*....|
gi 63054416 289 LRpgRLDRKI 298
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; ...
133-300 2.74e-33

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: 122.60  E-value: 2.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 133 GVGGLNEQIREL-REVIELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSS-AIVDKYIGES 210
Cdd:cd19504   1 GIGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGpEILNKYVGES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 211 ARIIREMFGYAKEHEPC--------VIFMDEIDAIGGRRFSEGTSADREiQRTLMELLNQMDGFDYLGQTKIIMATNRPD 282
Cdd:cd19504  81 EANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGSTGVH-DTVVNQLLSKIDGVEQLNNILVIGMTNRKD 159
                       170
                ....*....|....*...
gi 63054416 283 TLDPALLRPGRLDRKIEI 300
Cdd:cd19504 160 LIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
135-302 6.35e-28

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: 107.23  E-value: 6.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 135 GGLNEQIRELREVIELPlknpelflrvgikPPKGVLLYGPPGTGKTLLARAVAASL---GVNFLKVVSSAIVDKYIGESA 211
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 212 R---IIREMFGYAKEHEPCVIFMDEIDAIGgrrfsegtsadREIQRTLMELLNQ-MDGFDYLGQTKIIMATNRPDTLDPA 287
Cdd:cd00009  68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETlNDLRIDRENVRVIGATNRPLLGDLD 136
                       170
                ....*....|....*
gi 63054416 288 LLRPGRLDRKIEIPL 302
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
132-290 3.45e-25

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 100.34  E-value: 3.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 132 AGVGGLNEQIRElrEVIeLPLKNPELFLRVgIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESA 211
Cdd:cd19523   3 AGLGALKAAIKE--EVL-WPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 212 RIIREMFGYAKEHEPCVIFMDEIDAIGGRRFSEGTSADReIQrtlMELLNQMDGFDYLGQTKIIM--ATNRPDTLDPALL 289
Cdd:cd19523  79 KILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGR-LQ---VELLAQLDGVLGSGEDGVLVvcTTSKPEEIDESLR 154

                .
gi 63054416 290 R 290
Cdd:cd19523 155 R 155
ycf46 CHL00195
Ycf46; Provisional
162-381 3.80e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 100.86  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  162 GIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEID-AIGGR 240
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  241 RFS--EGTSAdreiqRTLMELLNqmdgfdYLGQTK---IIMAT-NRPDTLDPALLRPGRLDRKIEIPLPNEVGRMEILKI 314
Cdd:CHL00195 335 ESKgdSGTTN-----RVLATFIT------WLSEKKspvFVVATaNNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKI 403
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054416  315 HLEKVSKQG--EIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQsDLMSAARKVADLKKLEG 381
Cdd:CHL00195 404 HLQKFRPKSwkKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTD-DILLALKQFIPLAQTEK 471
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
160-296 4.13e-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: 91.66  E-value: 4.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 160 RVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARIIREMFGYAKEHEPCVIFMDEID-AIG 238
Cdd:cd19507  25 AYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFS 104
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054416 239 GRRFS--EGTSAdreiqRTLMELLNQMdgfdylgQTKI----IMAT-NRPDTLDPALLRPGRLDR 296
Cdd:cd19507 105 NADSKgdSGTSS-----RVLGTFLTWL-------QEKKkpvfVVATaNNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
148-300 2.89e-18

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: 80.86  E-value: 2.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 148 IELPLKNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDkyigeSARIIREMFGYAKEHEpc 227
Cdd:cd19510   5 LKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTAPKQS-- 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416 228 VIFMDEIDA---IGGRRFSEGTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPGRLDRKIEI 300
Cdd:cd19510  78 IILLEDIDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
165-304 3.17e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 80.88  E-value: 3.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416    165 PPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVS-----------------SAIVDKYIGESARIIREMFGYAKEHEPC 227
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054416    228 VIFMDEIDAIggrrfsegTSADREIQRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPALLRPgRLDRKIEIPLPN 304
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
159-300 1.95e-13

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: 67.40  E-value: 1.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 159 LRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKV--------------VSSAIVDKYIGESARIIREMFGYAKEH 224
Cdd:cd19505   5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRIslnkllynkpdfgnDDWIDGMLILKESLHRLNLQFELAKAM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 225 EPCVIFMDEIDAIGGRRFSEGTSADReiqRTLMELLNQMDGFDYLGQTK----IIMATNRPDTLDPALLRPGRLDRKIEI 300
Cdd:cd19505  85 SPCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
167-299 1.11e-11

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 62.16  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 167 KGVLLYGPPGTGKTLLARAVAASLGVNFlKVVSSAIVDKYIGESARIIREMFGYA-KEHEPCVIFMDEIDAIGGRRFSEG 245
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDY-AIMTGGDVAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 63054416 246 TSADreIQRTLMELLNQMDgfDYLGQTKIIMATNRPDTLDPALlrPGRLDRKIE 299
Cdd:cd19512 102 ISED--LRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMVE 149
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
169-288 1.77e-10

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 59.77  E-value: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVN---------FLKVVSSAIVDKYIGESARIIREMFGYAKE---HEPCVIF--MDEI 234
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKIQElidDKDALVFvlIDEV 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416 235 DAIGGRR--FSEGTSADREIqRTLMELLNQMDGFDYLGQTKIIMATNRPDTLDPAL 288
Cdd:cd19508 135 ESLAAARsaSSSGTEPSDAI-RVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
PRK04195 PRK04195
replication factor C large subunit; Provisional
130-343 4.47e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 61.09  E-value: 4.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  130 SFAGVGGLNEQIRELREVIELPLKNpelflrvgiKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSS-----AIVD 204
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIESWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  205 KYIGESARiIREMFGYAKEhepcVIFMDEIDAIGGRrfsegtsADREIQRTLMELLNqmdgfdylgQTK--IIMATNRPD 282
Cdd:PRK04195  83 RVAGEAAT-SGSLFGARRK----LILLDEVDGIHGN-------EDRGGARAILELIK---------KAKqpIILTANDPY 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054416  283 TLDPALLRpgrlDRKIEIPLpNEVGRMEILKIhLEKV-SKQG-EIDYEALVKLTDGTNGaDLR 343
Cdd:PRK04195 142 DPSLRELR----NACLMIEF-KRLSTRSIVPV-LKRIcRKEGiECDDEALKEIAERSGG-DLR 197
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
56-111 1.94e-09

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: 52.89  E-value: 1.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416    56 IGEVLKQLDSERFIVKASSGPRYVVGCRNNVDQSHLVQGVRVSLDMTTLTIMRILP 111
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
324-368 3.73e-09

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: 51.77  E-value: 3.73e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 63054416   324 EIDYEALVKLTDGTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMS 368
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
169-234 2.64e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 55.48  E-value: 2.64e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  169 VLLYGPPGTGKTLLARAVAASLGVNFLKVvsSAIVDKyIGEsariIREMFGYAKEH----EPCVIFMDEI 234
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAL--SAVTSG-VKD----LREVIEEARQRrsagRRTILFIDEI 101
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
131-301 3.81e-08

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: 55.24  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   131 FAGVGGLNEQIRELREVIELPLKNPELFLRVGIKPpKGVLLYGPPGTGKTLLARAVA---ASLGV----NFLKVVSSAIV 203
Cdd:TIGR03922 278 QIGLERVKRQVAALKSSTAMALARAERGLPVAQTS-NHMLFAGPPGTGKTTIARVVAkiyCGLGVlrkpLVREVSRADLI 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   204 DKYIGESARIIREMFGYAKEHepcVIFMDEIDAIGGRRFSEGTSADREIQRTLMELLnQMDGFDYLgqtkIIMATNRPDt 283
Cdd:TIGR03922 357 GQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEAIDTLLARM-ENDRDRLV----VIGAGYRKD- 427
                         170       180
                  ....*....|....*....|...
gi 63054416   284 LDPAL-----LRpGRLDRKIEIP 301
Cdd:TIGR03922 428 LDKFLevnegLR-SRFTRVIEFP 449
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
166-260 7.55e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 52.00  E-value: 7.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 166 PKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVD-KYIG-ESARIIREMFgyakehePCVIFMDEIDAIGGRRFS 243
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLV-------EGIVFIDEIDKIAKRGGS 118
                        90
                ....*....|....*...
gi 63054416 244 EGTSADRE-IQRTLMELL 260
Cdd:cd19498 119 SGPDVSREgVQRDLLPIV 136
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
169-243 7.81e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.91  E-value: 7.81e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVNFLKVvsSAIVDKyIGEsariIREMFGYAKEH----EPCVIFMDEIDaiggrRFS 243
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVAL--SAVTSG-VKD----IREVIEEARERraygRRTILFVDEIH-----RFN 118
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
169-234 1.45e-07

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: 50.58  E-value: 1.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416   169 VLLYGPPGTGKTLLARAVAASLGVNFlKVVSSAIVDKyIGESARIIREMfgyaKEHEpcVIFMDEI 234
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL----EPGD--VLFIDEI 93
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
168-290 2.15e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.60  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   168 GVLLYGPPGTGKTLLARAVAASL-GVNFLKVVSSaivdKYIGESARI-IREMFGYAKEH----------EPCVIFMDEID 235
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLT----RDTTEEDLFgRRNIDPGGASWvdgplvraarEGEIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054416   236 aiggrrfsegtSADREIQRTLMELLN-----QMDGFDYLG----QTKIIMATNRPDT----LDPALLR 290
Cdd:pfam07728  77 -----------RANPDVLNSLLSLLDerrllLPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS 133
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
169-260 9.74e-07

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 49.52  E-value: 9.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVNFlkvvssAIVDK-------YIGES-----ARIIREMFGYAKEHEPCVIFMDEIDA 236
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPF------AIADAttlteagYVGEDvenilLKLLQAADYDVERAQRGIVYIDEIDK 126
                        90       100
                ....*....|....*....|....*....
gi 63054416 237 IGgrRFSEGTSADRE-----IQRTLMELL 260
Cdd:cd19497 127 IA--RKSENPSITRDvsgegVQQALLKIL 153
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
170-314 9.86e-07

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: 48.71  E-value: 9.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 170 LLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDK---------YIGE-SARIIREMfGYAKEHEPcVIFMDEIDAIGG 239
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmPGRIIQAL-KKAGTNNP-VFLLDEIDKIGS 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 240 RRFSEGTSAdreiqrtLMELLN--QMDGF-DY-------LGQTKIIMATNRPDTLDPALLrpgrldrkieiplpnevGRM 309
Cdd:cd19500 119 SFRGDPASA-------LLEVLDpeQNSTFsDHyldvpfdLSKVLFIATANSLDTIPGPLL-----------------DRM 174

                ....*
gi 63054416 310 EILKI 314
Cdd:cd19500 175 EIIEL 179
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
169-234 1.03e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.13  E-value: 1.03e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416  169 VLLYGPPGTGKTLLARAVAASLGVNfLKVVSSAIVDKyIGESARIIREMfgyaKEHEpcVIFMDEI 234
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGDLAAILTNL----EEGD--VLFIDEI 111
ycf2 CHL00206
Ycf2; Provisional
159-388 3.28e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 49.52  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   159 LRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDK----------------YIGESARIIREM----- 217
Cdd:CHL00206 1623 LRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDNkpkgfliddididdsdDIDDSDDIDRDLdtell 1702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   218 ----------------------FGYAKEHEPCVIFMDEIDAIggrrfsegtSADREIQRTLMELLNQMdGFD----YLGQ 271
Cdd:CHL00206 1703 tmmnaltmdmmpkidrfyitlqFELAKAMSPCIIWIPNIHDL---------NVNESNYLSLGLLVNSL-SRDcercSTRN 1772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   272 TKIIMATNRPDTLDPALLRPGRLDRKIEIP---LPNEVGRMEILK----IHLEKvskqGEIDYEALVKLTDGTNGADLRN 344
Cdd:CHL00206 1773 ILVIASTHIPQKVDPALIAPNKLNTCIKIRrllIPQQRKHFFTLSytrgFHLEK----KMFHTNGFGSITMGSNARDLVA 1848
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 63054416   345 VVTEAGFIAIKEdRDYVIQSDLMSAA--RKVADLK-KLEGTIDYQKL 388
Cdd:CHL00206 1849 LTNEALSISITQ-KKSIIDTNTIRSAlhRQTWDLRsQVRSVQDHGIL 1894
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
169-194 3.70e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 48.24  E-value: 3.70e-06
                        10        20
                ....*....|....*....|....*.
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVNF 194
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPF 59
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
159-238 5.31e-06

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: 47.68  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   159 LRVGIKPPKG-------VLLYGPPGTGKTLLARAVAASLGVNfLKVVSSAIVDKyIGESARIIREMfgyaKEHEpcVIFM 231
Cdd:TIGR00635  16 LQLFIEAAKMrqealdhLLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK-PGDLAAILTNL----EEGD--VLFI 87

                  ....*..
gi 63054416   232 DEIDAIG 238
Cdd:TIGR00635  88 DEIHRLS 94
44 PHA02544
clamp loader, small subunit; Provisional
170-385 8.84e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 47.29  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  170 LLYGP-PGTGKTLLARAVAASLGVNFLKVvssaivdkyIGESARI--IR-EMFGYAK----EHEPCVIFMDEIDaiggrr 241
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFV---------NGSDCRIdfVRnRLTRFAStvslTGGGKVIIIDEFD------ 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  242 fSEGTSADREIQRTLMEllnqmdgfDYLGQTKIIMATNRPDTLDPALLrpGRLdRKIEIPLPNEVGRMEILK--IH-LEK 318
Cdd:PHA02544 111 -RLGLADAQRHLRSFME--------AYSKNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMMKqmIVrCKG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  319 VSKQGEIDYE-----ALVKltdgTNGADLRNVVTEAGFIAIKEDRDYVIQSDLMSA----------ARKVADLKKLEGTI 383
Cdd:PHA02544 179 ILEAEGVEVDmkvlaALVK----KNFPDFRRTINELQRYASTGKIDAGILSEVTNSdiddvvealkAKDFKAVRALAPNY 254

                 ..
gi 63054416  384 DY 385
Cdd:PHA02544 255 AN 256
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
138-383 1.02e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 138 NEQIRELREVIElPLKNPElflrvgikPPKGVLLYGPPGTGKTLLARAVAASLG---------VNFLKV----------V 198
Cdd:COG1474  32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEELEeeaeergvdVRVVYVncrqastryrV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 199 SSAIVDKyIGESARI------IREMFGYAKEH-----EPCVIFMDEIDAIGgrrfsegtsaDREIQRTLMELLNQMDGFD 267
Cdd:COG1474 103 LSRILEE-LGSGEDIpstglsTDELFDRLYEAlderdGVLVVVLDEIDYLV----------DDEGDDLLYQLLRANEELE 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 268 --YLGqtkIIMATNRP---DTLDPALLRpgRLdRKIEIPLP----NEVGrmEILKIHLEKVSKQGEIDYEAL---VKLTD 335
Cdd:COG1474 172 gaRVG---VIGISNDLeflENLDPRVKS--SL-GEEEIVFPpydaDELR--DILEDRAELAFYDGVLSDEVIpliAALAA 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 63054416 336 GTNGaDLR---NVVTEAGFIAIKEDRDYVIQSDLmSAARKVADLKKLEGTI 383
Cdd:COG1474 244 QEHG-DARkaiDLLRVAGEIAEREGSDRVTEEHV-REAREKIERDRLLEVL 292
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
167-233 1.77e-05

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: 44.44  E-value: 1.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054416 167 KGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKYIGESARI--IREMFGYAKEHEPCVIFMDE 233
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGD 95
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
169-234 2.18e-05

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 45.84  E-value: 2.18e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVNfLKVVSSAIVDKyIGESARIIREMfgyaKEHEpcVIFMDEI 234
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVN-IRITSGPAIEK-PGDLAAILTNL----EEGD--VLFIDEI 114
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
160-298 3.17e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.09  E-value: 3.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 160 RVGIKPPK---GVLLY-GPPGTGKTLLARAVAASL---GVNFLKV----------VSSAIVD--KYIG--ESARIIREMf 218
Cdd:cd19499  31 RAGLSDPNrpiGSFLFlGPTGVGKTELAKALAELLfgdEDNLIRIdmseymekhsVSRLIGAppGYVGytEGGQLTEAV- 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 219 gyaKEHEPCVIFMDEIDaiggrrfsegtSADREIQRTLMELLNQ---MDGFDY---LGQTKIIMATNrpdTLDPALLrpG 292
Cdd:cd19499 110 ---RRKPYSVVLLDEIE-----------KAHPDVQNLLLQVLDDgrlTDSHGRtvdFKNTIIIMTSN---HFRPEFL--N 170

                ....*.
gi 63054416 293 RLDRKI 298
Cdd:cd19499 171 RIDEIV 176
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
166-279 6.62e-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: 42.95  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   166 PKGV-LLYGPPGTGKTLLARAVAASLGVNFLKVVSSA--------IVDKYIGESARIIR-EMFGYAKE----HEPCVIFM 231
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGDERALIRIDmseymeehSVSRLIGAPPGYVGyEEGGQLTEavrrKPYSIVLI 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054416   232 DEIDaiggrrfsegtSADREIQRTLMELL----------NQMDgFDYlgqTKIIMATN 279
Cdd:pfam07724  82 DEIE-----------KAHPGVQNDLLQILeggtltdkqgRTVD-FKN---TLFIMTGN 124
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
163-191 1.09e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 43.99  E-value: 1.09e-04
                        10        20
                ....*....|....*....|....*....
gi 63054416 163 IKPPKGVLLYGPPGTGKTLLARAVAASLG 191
Cdd:COG1401 218 LKTKKNVILAGPPGTGKTYLARRLAEALG 246
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
169-237 3.67e-04

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: 39.51  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054416   169 VLLYGPPGTGKTL----LARAVAASLGVNFLKVVSSAIVDKYigesariireMFGYAkeHEPCVIfMDEIDAI 237
Cdd:pfam00910   1 IWLYGPPGCGKSTlakyLARALLKKLGLPKDSVYSRNPDDDF----------WDGYT--GQPVVI-IDDFGQN 60
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
169-252 3.76e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.45  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  169 VLLYGPPGTGKTLLARAVAASLGVNFlkvvssAIVD-------KYIGESAR-IIREMFGYA----KEHEPCVIFMDEIDA 236
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF------AIADattlteaGYVGEDVEnILLKLLQAAdydvEKAQRGIVYIDEIDK 184
                         90
                 ....*....|....*.
gi 63054416  237 IGgrRFSEGTSADREI 252
Cdd:PRK05342 185 IA--RKSENPSITRDV 198
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
166-191 4.02e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.88  E-value: 4.02e-04
                        10        20
                ....*....|....*....|....*.
gi 63054416 166 PKGVLLYGPPGTGKTLLARAVAASLG 191
Cdd:COG0470  18 PHALLLHGPPGIGKTTLALALARDLL 43
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
123-232 4.47e-04

Protein of unknown function (DUF815); This family consists of several bacterial proteins of unknown function.


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 41.37  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416   123 IEDPGDISFAGVGGLNEQIRELrevielpLKNPELFLRvGiKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSsai 202
Cdd:pfam05673  19 VPHPDPVRLDDLVGIERQKEAL-------IRNTRRFLA-G-LPANNVLLWGARGTGKSSLVKALLNEYADQGLRLIE--- 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 63054416   203 VDKY-IGESARIIREMfgyAKEHEPCVIFMD 232
Cdd:pfam05673  87 VDKEdLGDLPDLVDLL---RDRPYRFILFCD 114
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
169-285 4.68e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 39.79  E-value: 4.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVDKyigesarIIREMFGYAKEHEPCVIFMDEIDAIGGRrfsEGTSA 248
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDT-------ILEAIEDLIEEKKLDIIIIDSLSSLARA---SQGDR 70
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 63054416 249 DREIQRTLMELLNqmdGFDYLGQTkiIMATNRPDTLD 285
Cdd:cd01120  71 SSELLEDLAKLLR---AARNTGIT--VIATIHSDKFD 102
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
167-191 4.76e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 4.76e-04
                        10        20
                ....*....|....*....|....*
gi 63054416 167 KGVLLYGPPGTGKTLLARAVAASLG 191
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELG 89
Sigma54_activat pfam00158
Sigma-54 interaction domain;
169-222 7.70e-04

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.69  E-value: 7.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 63054416   169 VLLYGPPGTGKTLLARAV-AASL--GVNFLKVVSSAIVDKYIgESariirEMFGYAK 222
Cdd:pfam00158  25 VLITGESGTGKELFARAIhQLSPraDGPFVAVNCAAIPEELL-ES-----ELFGHEK 75
PLN00020 PLN00020
ribulose bisphosphate carboxylase/oxygenase activase -RuBisCO activase (RCA); Provisional
162-296 8.48e-04

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


Pssm-ID: 215031 [Multi-domain]  Cd Length: 413  Bit Score: 41.24  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416  162 GIKPPKGVLLYGPPGTGKTLLARAVAASLGVNflKVVSSA--IVDKYIGESARIIREMFGYAKEH-----EPCVIFMDEI 234
Cdd:PLN00020 144 NIKVPLILGIWGGKGQGKSFQCELVFKKMGIE--PIVMSAgeLESENAGEPGKLIRQRYREAADIikkkgKMSCLFINDL 221
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054416  235 DAIGGR-RFSEGTSADREIQRTLMEL--------LNQM-DGFDYLGQTKIIMATNRPDTLDPALLRPGRLDR 296
Cdd:PLN00020 222 DAGAGRfGTTQYTVNNQMVNGTLMNIadnptnvsLGGDwREKEEIPRVPIIVTGNDFSTLYAPLIRDGRMEK 293
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
167-202 1.08e-03

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 40.76  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 63054416   167 KGVLLYGPPGTGKTLLARAVAASLG--VNFLKVVSSAI 202
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
139-204 1.46e-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: 39.02  E-value: 1.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054416   139 EQIRELREVIElplknpelflRVGIKPPKGVLLYGPPGTGKTLLARAVAASLGVNFLKVVSSAIVD 204
Cdd:pfam13191   7 EELEQLLDALD----------RVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDE 62
TsaE pfam02367
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ...
169-213 1.54e-03

Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).


Pssm-ID: 460540  Cd Length: 127  Bit Score: 38.18  E-value: 1.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 63054416   169 VLLYGPPGTGKTLLARAVAASLGVNflKVVSS---AIVDKYIGESARI 213
Cdd:pfam02367  24 ILLSGDLGAGKTTFTRGLARGLGVT--GPVTSptfTLVNEYEGGGLPL 69
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
137-194 1.84e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.77  E-value: 1.84e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054416 137 LNEQIRELREVIELPLKNPELFlrvgikppkgVLLYGPPGTGKTLLARAVAASLGVNF 194
Cdd:COG3267  24 LSPSHREALARLEYALAQGGGF----------VVLTGEVGTGKTTLLRRLLERLPDDV 71
PRK08116 PRK08116
hypothetical protein; Validated
168-198 2.07e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 39.62  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 63054416  168 GVLLYGPPGTGKTLLARAVAASLGVNFLKVV 198
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
170-238 2.71e-03

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 40.00  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054416 170 LLYGPPGTGKTLLARAVAASLGVNFLKV----VSsaivDK---------YIGesA---RIIREMfGYAKEHEPcVIFMDE 233
Cdd:COG0466 356 CLVGPPGVGKTSLGKSIARALGRKFVRIslggVR----DEaeirghrrtYIG--AmpgRIIQGL-KKAGTKNP-VFLLDE 427

                ....*
gi 63054416 234 IDAIG 238
Cdd:COG0466 428 IDKMG 432
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
169-209 2.97e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 39.26  E-value: 2.97e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 63054416 169 VLLYGPPGTGKTLLARAVAASLGVNFlkvvssAIVDK-------YIGE 209
Cdd:COG1219 112 ILLIGPTGSGKTLLAQTLARILDVPF------AIADAttlteagYVGE 153
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
169-190 4.02e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.29  E-value: 4.02e-03
                          10        20
                  ....*....|....*....|..
gi 63054416   169 VLLYGPPGTGKTLLARAVAASL 190
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPGIL 46
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
169-184 4.36e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 38.87  E-value: 4.36e-03
                        10
                ....*....|....*.
gi 63054416 169 VLLYGPPGTGKTLLAR 184
Cdd:COG0606 214 LLMIGPPGSGKTMLAR 229
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
163-187 4.66e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.22  E-value: 4.66e-03
                        10        20
                ....*....|....*....|....*
gi 63054416 163 IKPPKGVLLYGPPGTGKTLLARAVA 187
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALG 120
PRK13341 PRK13341
AAA family ATPase;
170-187 7.12e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 38.50  E-value: 7.12e-03
                         10
                 ....*....|....*...
gi 63054416  170 LLYGPPGTGKTLLARAVA 187
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIA 73
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
166-195 8.70e-03

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 37.96  E-value: 8.70e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 63054416 166 PKG--VLLYGPPGTGKTLLAR--AVAASLGVNFL 195
Cdd:COG3598  11 PEGgvTLLAGPPGTGKSFLALqlAAAVAAGGPWL 44
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
170-190 1.00e-02

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 37.48  E-value: 1.00e-02
                        10        20
                ....*....|....*....|.
gi 63054416 170 LLYGPPGTGKTLLARAVAASL 190
Cdd:COG2812  36 LFTGPRGVGKTTLARILAKAL 56
 
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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