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Conserved domains on  [gi|685326922|ref|XP_009101818|]
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26S proteasome regulatory subunit 10B homolog A [Brassica rapa]

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
24-397 2.25e-168

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 476.25  E-value: 2.25e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  24 QHKELESRVRTARENLRGSKKEFNKTEDDLKSLQSVGQ-------IIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKE 96
Cdd:PRK03992   9 RNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEklkspplIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  97 KLTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGV 176
Cdd:PRK03992  89 KLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 177 LLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSAD 256
Cdd:PRK03992 169 LLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 257 REIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEA 336
Cdd:PRK03992 249 REVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEE 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685326922 337 IVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKLSEAKKLESSSHYNADFG 397
Cdd:PRK03992 329 LAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSMEEPGVMFA 389
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
24-397 2.25e-168

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 476.25  E-value: 2.25e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  24 QHKELESRVRTARENLRGSKKEFNKTEDDLKSLQSVGQ-------IIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKE 96
Cdd:PRK03992   9 RNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEklkspplIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  97 KLTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGV 176
Cdd:PRK03992  89 KLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 177 LLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSAD 256
Cdd:PRK03992 169 LLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 257 REIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEA 336
Cdd:PRK03992 249 REVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEE 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685326922 337 IVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKLSEAKKLESSSHYNADFG 397
Cdd:PRK03992 329 LAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSMEEPGVMFA 389
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
18-380 1.09e-146

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: 420.36  E-value: 1.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   18 YRKKLLQHKELEsrvrtaRENLRgSKKEFNKTEDDLKSLQSVGQIIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEK 97
Cdd:TIGR01242   8 IRKLEDEKRSLE------KEKIR-LERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   98 LTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVL 177
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  178 LYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADR 257
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  258 EIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAI 337
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 685326922  338 VKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKL 380
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
135-385 4.60e-134

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 387.05  E-value: 4.60e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 135 NISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYI 214
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 215 GESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSAdrEIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPA 294
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 295 LLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFM 374
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLE 311
                        250
                 ....*....|.
gi 685326922 375 KAVRKLSEAKK 385
Cdd:COG1222  312 KAIEKVKKKTE 322
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
137-307 7.13e-108

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: 314.28  E-value: 7.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 137 SYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGE 216
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 217 SARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALL 296
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 685326922 297 RPGRLDRKIEI 307
Cdd:cd19502  161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
176-309 2.82e-53

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: 173.16  E-value: 2.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  176 VLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGtsa 255
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG--- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 685326922  256 DREIQRTLMELLNQLDGFDNL-GKVKMIMATNRPDVLDPALLrpGRLDRKIEIPL 309
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
172-311 6.22e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 6.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   172 PPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVS-----------------SAIIDKYIGESARLIREMFNYAREHQPC 234
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922   235 IIFMDEIDAIggrrfsegTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPgRLDRKIEIPLPN 311
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
24-397 2.25e-168

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 476.25  E-value: 2.25e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  24 QHKELESRVRTARENLRGSKKEFNKTEDDLKSLQSVGQ-------IIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKE 96
Cdd:PRK03992   9 RNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEklkspplIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  97 KLTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGV 176
Cdd:PRK03992  89 KLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 177 LLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSAD 256
Cdd:PRK03992 169 LLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 257 REIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEA 336
Cdd:PRK03992 249 REVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEE 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685326922 337 IVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKLSEAKKLESSSHYNADFG 397
Cdd:PRK03992 329 LAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSMEEPGVMFA 389
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
18-380 1.09e-146

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: 420.36  E-value: 1.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   18 YRKKLLQHKELEsrvrtaRENLRgSKKEFNKTEDDLKSLQSVGQIIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEK 97
Cdd:TIGR01242   8 IRKLEDEKRSLE------KEKIR-LERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   98 LTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVL 177
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  178 LYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADR 257
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  258 EIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAI 337
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 685326922  338 VKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKL 380
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
135-385 4.60e-134

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 387.05  E-value: 4.60e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 135 NISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYI 214
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 215 GESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSAdrEIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPA 294
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 295 LLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFM 374
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLE 311
                        250
                 ....*....|.
gi 685326922 375 KAVRKLSEAKK 385
Cdd:COG1222  312 KAIEKVKKKTE 322
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
28-385 1.69e-116

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 346.37  E-value: 1.69e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  28 LESRVRTARENLRGSKkefNKTEDDLK---SLQSVGQIIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEKLTSGTRV 104
Cdd:PTZ00361  72 LEEEFITNQEAQKPAQ---EKNEAELKkvdDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSV 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 105 VLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGT 184
Cdd:PTZ00361 149 LLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGT 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 185 GKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLM 264
Cdd:PTZ00361 229 GKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTML 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 265 ELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGF 344
Cdd:PTZ00361 309 ELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDEL 388
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 685326922 345 NGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKLSEAKK 385
Cdd:PTZ00361 389 SGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKK 429
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
23-379 8.95e-116

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 342.90  E-value: 8.95e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  23 LQHKELESR----------VRTARENLrgsKKEFNKTEDDLKSLQSVGQIIGEVLRPLDNERLIVKASSGPRYVVGCRSK 92
Cdd:PTZ00454  22 EKLKELEKElefldiqeeyIKEEQKNL---KRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILST 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  93 VDKEKLTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKP 172
Cdd:PTZ00454  99 LNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 173 PKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEG 252
Cdd:PTZ00454 179 PRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 253 TSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEI 332
Cdd:PTZ00454 259 TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEV 338
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 685326922 333 EYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRK 379
Cdd:PTZ00454 339 DLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKT 385
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
137-307 7.13e-108

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: 314.28  E-value: 7.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 137 SYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGE 216
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 217 SARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALL 296
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 685326922 297 RPGRLDRKIEI 307
Cdd:cd19502  161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
138-379 2.18e-81

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: 254.84  E-value: 2.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 138 YSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGES 217
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 218 ARLIREMFNYAREHQPCIIFMDEIDAIGGRRfseGTSADREIQRTLMELLNQLDGFDnlGKVKMIMATNRPDVLDPALLR 297
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEELR--SDVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 298 pgRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAV 377
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ..
gi 685326922 378 RK 379
Cdd:COG0464  389 ER 390
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
128-379 3.23e-74

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: 239.49  E-value: 3.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  128 MLHEDPGNISYSAVGGLGDQIRELRESIELpLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSS 207
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  208 AIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNR 287
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  288 PDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDY 367
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282
                         250
                  ....*....|..
gi 685326922  368 VIQEDFMKAVRK 379
Cdd:TIGR01241 283 ITMNDIEEAIDR 294
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
106-380 1.48e-72

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 240.58  E-value: 1.48e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  106 LDMTTLTIMRALpREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTG 185
Cdd:TIGR01243 421 LKVTMKDFMEAL-KMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTG 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  186 KTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIG---GRRFSEGTSadreiQRT 262
Cdd:TIGR01243 500 KTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAparGARFDTSVT-----DRI 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  263 LMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAE 342
Cdd:TIGR01243 575 VNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTE 654
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922  343 GFNGADLRNICTEAGMFAIRAERDYVIQE------------------DFMKAVRKL 380
Cdd:TIGR01243 655 GYTGADIEAVCREAAMAALRESIGSPAKEklevgeeeflkdlkvemrHFLEALKKV 710
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
128-377 1.35e-70

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 232.23  E-value: 1.35e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 128 MLHEDPGNISYSAVGGLGDQIRELRESIELpLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSS 207
Cdd:COG0465  131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 208 AIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFS--EGTSADREiqRTLMELLNQLDGFDNLGKVKMIMAT 285
Cdd:COG0465  210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglGGGHDERE--QTLNQLLVEMDGFEGNEGVIVIAAT 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 286 NRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAER 365
Cdd:COG0465  288 NRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNK 367
                        250
                 ....*....|..
gi 685326922 366 DYVIQEDFMKAV 377
Cdd:COG0465  368 KAVTMEDFEEAI 379
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
140-307 6.38e-70

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 217.54  E-value: 6.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 140 AVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESAR 219
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 220 LIREMFNYAREHQPCIIFMDEIDAIGGRRfsegTSADREI-QRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRP 298
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVeRRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 685326922 299 GRLDRKIEI 307
Cdd:cd19503  157 GRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
136-362 1.90e-66

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: 224.40  E-value: 1.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  136 ISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIG 215
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  216 ESARLIREMFNYAREHQPCIIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPAL 295
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922  296 LRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIR 362
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
149-305 2.60e-66

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: 207.91  E-value: 2.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 149 RELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYA 228
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922 229 REHQPCIIFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKI 305
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
149-307 3.55e-65

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: 205.04  E-value: 3.55e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 149 RELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYA 228
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685326922 229 REHQPCIIFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEI 307
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
136-307 8.86e-64

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: 201.69  E-value: 8.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 136 ISYSAVGGLGDQIRELRESIELpLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIG 215
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 216 ESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPAL 295
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 685326922 296 LRPGRLDRKIEI 307
Cdd:cd19501  160 LRPGRFDRQVYV 171
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
147-307 4.91e-62

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: 196.73  E-value: 4.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 147 QIRELRESIELPLMNPELfLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFN 226
Cdd:cd19481    1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 227 YAREHQPCIIFMDEIDAIGGRRFSEGTSADReiQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIE 306
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSGESGEL--RRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 685326922 307 I 307
Cdd:cd19481  158 F 158
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
128-394 1.22e-61

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 209.89  E-value: 1.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 128 MLHEDPGNISYSAVGGLGDQIRELRESIELpLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSS 207
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 208 AIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNR 287
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 288 PDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDY 367
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 685326922 368 VIQEDFMKAVRK-----------LSEAKKlESSSHYNA 394
Cdd:PRK10733 380 VSMVEFEKAKDKimmgaerrsmvMTEAQK-ESTAYHEA 416
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
59-368 1.40e-61

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: 206.87  E-value: 1.40e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   59 VGQIIgEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEKLTSGTRVVLDMTTLTIMRALPR-EVDPVVynmLHEDPgNIS 137
Cdd:TIGR03689 106 TGEIV-TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGYAFEAIPRtEVEDLV---LEEVP-DVT 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  138 YSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDAN----------FLKVVSS 207
Cdd:TIGR03689 181 YADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARigaegggksyFLNIKGP 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  208 AIIDKYIGESARLIREMFNYAREH----QPCIIFMDEIDAIGGRRFSeGTSADREiqRTLM-ELLNQLDGFDNLGKVKMI 282
Cdd:TIGR03689 261 ELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGS-GVSSDVE--TTVVpQLLAEIDGVESLDNVIVI 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  283 MATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILkihaagiAKH--GEIEYEAIVKLAEGFNGAD---LRNICTEAg 357
Cdd:TIGR03689 338 GASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF-------AKYltDDLPLPEDLAAHDGDREATaaaLIQRVVDA- 409
                         330
                  ....*....|.
gi 685326922  358 MFAIRAERDYV 368
Cdd:TIGR03689 410 LYARSEANRYV 420
ftsH CHL00176
cell division protein; Validated
136-380 3.38e-61

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 208.37  E-value: 3.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 136 ISYSAVGGLGDQIRELRESIELpLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIG 215
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 216 ESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPAL 295
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 296 LRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMK 375
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418

                 ....*
gi 685326922 376 AVRKL 380
Cdd:CHL00176 419 AIDRV 423
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
141-308 5.04e-59

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: 189.57  E-value: 5.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARL 220
Cdd:cd19519    2 IGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 221 IREMFNYAREHQPCIIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGR 300
Cdd:cd19519   82 LRKAFEEAEKNAPAIIFIDEIDAIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGR 158

                 ....*...
gi 685326922 301 LDRKIEIP 308
Cdd:cd19519  159 FDREIDIG 166
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
144-391 1.23e-56

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 185.86  E-value: 1.23e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 144 LGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIRE 223
Cdd:COG1223    6 GQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 224 MFNYAREHqPCIIFMDEIDAIGGRRFSegTSADREIQRTLMELLNQLDGFDNlgKVKMIMATNRPDVLDPALLRpgRLDR 303
Cdd:COG1223   86 LFDFARRA-PCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 304 KIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMKAVRKLSEA 383
Cdd:COG1223  159 VIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKER 238

                 ....*...
gi 685326922 384 KKLESSSH 391
Cdd:COG1223  239 KKEPKKEG 246
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
149-307 1.19e-54

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: 178.09  E-value: 1.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 149 RELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYA 228
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685326922 229 REHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEI 307
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
176-309 2.82e-53

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: 173.16  E-value: 2.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  176 VLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGtsa 255
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG--- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 685326922  256 DREIQRTLMELLNQLDGFDNL-GKVKMIMATNRPDVLDPALLrpGRLDRKIEIPL 309
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
141-305 1.31e-51

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: 170.28  E-value: 1.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARL 220
Cdd:cd19518    2 IGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 221 IREMFNYAREHQPCIIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQLDGFDNL----GKVKMIMATNRPDVLDPALL 296
Cdd:cd19518   82 IRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELNNEktagGPVLVIGATNRPDSLDPALR 158

                 ....*....
gi 685326922 297 RPGRLDRKI 305
Cdd:cd19518  159 RAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
146-303 4.00e-51

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: 168.82  E-value: 4.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 146 DQIR-ELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREM 224
Cdd:cd19530    2 DHVReELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685326922 225 FNYAREHQPCIIFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDR 303
Cdd:cd19530   82 FQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
141-307 3.18e-49

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: 164.06  E-value: 3.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFlRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARL 220
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 221 IREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIqRTlmELLNQLDGFDN--LGKVKMIMATNRPDVLDPALLRp 298
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVLNkpEDRVLVLGATNRPWELDEAFLR- 155

                 ....*....
gi 685326922 299 gRLDRKIEI 307
Cdd:cd19509  156 -RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
141-304 9.78e-49

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 163.06  E-value: 9.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVV-----SSAIIDKYIG 215
Cdd:cd19517    2 IGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 216 ESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqLDGFDNLGKVKMIMATNRPDVLDPAL 295
Cdd:cd19517   82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPAL 158

                 ....*....
gi 685326922 296 LRPGRLDRK 304
Cdd:cd19517  159 RRPGRFDRE 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
151-306 8.83e-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: 159.90  E-value: 8.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 151 LRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYARE 230
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922 231 HQPCIIFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIE 306
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTGV---TDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
150-303 1.46e-46

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: 156.90  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 150 ELRESIELPLMNPELFlRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAR 229
Cdd:cd19527    4 EILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685326922 230 EHQPCIIFMDEIDAIGGRRFSEGTSADrEIQRTLMELLNQLDGFDNLGK-VKMIMATNRPDVLDPALLRPGRLDR 303
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
141-307 2.26e-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: 146.03  E-value: 2.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFLRVGI-KPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESAR 219
Cdd:cd19520    2 IGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 220 LIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqLDGFDNLGKVKMIM--ATNRPDVLDPALLR 297
Cdd:cd19520   82 LVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSL---WDGLSTDGNCRVIVmgATNRPQDLDEAILR 158
                        170
                 ....*....|
gi 685326922 298 pgRLDRKIEI 307
Cdd:cd19520  159 --RMPKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
141-307 2.49e-40

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: 140.89  E-value: 2.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFlrVGIKPP-KGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESAR 219
Cdd:cd19522    2 IADLEEAKKLLEEAVVLPMWMPEFF--KGIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 220 LIREMFNYAREHQPCIIFMDEIDAIGGRRfseGTSADREIQRTL-MELLNQLDGF----DNLGKVKMIM---ATNRPDVL 291
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEASRRVkSELLVQMDGVggasENDDPSKMVMvlaATNFPWDI 156
                        170
                 ....*....|....*.
gi 685326922 292 DPALLRpgRLDRKIEI 307
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
135-307 1.19e-39

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 139.23  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 135 NISYSAVGGLGDQIRELRESIELPLMNPELFLRvGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYI 214
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 215 GESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQrtlMELLNQLDGF-DNLGKVKMIMATNRPDVLDP 293
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIK---TELLVQMNGVgNDSQGVLVLGATNIPWQLDS 158
                        170
                 ....*....|....
gi 685326922 294 ALLRpgRLDRKIEI 307
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; ...
128-307 6.56e-36

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: 130.11  E-value: 6.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 128 MLHEDPgnISYSAVGGLGDQIRELRESIELPLMNPELFlrVGIK-PPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVS 206
Cdd:cd19525   13 MDHGPP--INWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 207 SAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRfseGTSADREIQRTLMELLNQLDGFDNLGKVKMIM--A 284
Cdd:cd19525   89 SSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATTSSEDRILVvgA 165
                        170       180
                 ....*....|....*....|...
gi 685326922 285 TNRPDVLDPALLRpgRLDRKIEI 307
Cdd:cd19525  166 TNRPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
141-305 3.29e-35

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: 127.27  E-value: 3.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELF--LRvgiKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESA 218
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFtgLR---APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 219 RLIREMFNYAREHQPCIIFMDEIDAIggrrFSEGTSADREIQRTL-MELLNQLDGFDNLG--KVKMIMATNRPDVLDPAL 295
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSL----LSERSEGEHEASRRLkTEFLIEFDGVQSNGddRVLVMGATNRPQELDDAV 154
                        170
                 ....*....|
gi 685326922 296 LRpgRLDRKI 305
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; ...
141-307 1.70e-34

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: 125.68  E-value: 1.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIREL-RESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSS-AIIDKYIGESA 218
Cdd:cd19504    2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGpEILNKYVGESE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 219 RLIREMFNYAREHQPC--------IIFMDEIDAIGGRRFSEGTSADREiQRTLMELLNQLDGFDNLGKVKMIMATNRPDV 290
Cdd:cd19504   82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGSTGVH-DTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                        170
                 ....*....|....*..
gi 685326922 291 LDPALLRPGRLDRKIEI 307
Cdd:cd19504  161 IDEALLRPGRLEVQMEI 177
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
141-297 1.32e-26

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: 104.20  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 141 VGGLGDQIRELRESIELPLMNPELFLRVgIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARL 220
Cdd:cd19523    2 IAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685326922 221 IREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADReIQrtlMELLNQLDGFDNLGK--VKMIMATNRPDVLDPALLR 297
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGR-LQ---VELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
142-309 5.30e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 99.53  E-value: 5.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 142 GGLGDQIRELRESIELPlmnpelflrvgikPPKGVLLYGPPGTGKTLLARAIA---SNIDANFLKVVSSAIIDKYIGESA 218
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAEL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 219 R---LIREMFNYAREHQPCIIFMDEIDAIGgrrfsegtsadREIQRTLMELLNQL-DGFDNLGKVKMIMATNRPDVLDPA 294
Cdd:cd00009   68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136
                        170
                 ....*....|....*
gi 685326922 295 LLRPGRLDRKIEIPL 309
Cdd:cd00009  137 RALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
167-303 1.71e-20

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: 87.42  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 167 RVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEID-AIG 245
Cdd:cd19507   25 AYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFS 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685326922 246 GRRFS--EGTSAdreiqRTLMELLNQLDgfDNLGKVkMIMAT-NRPDVLDPALLRPGRLDR 303
Cdd:cd19507  105 NADSKgdSGTSS-----RVLGTFLTWLQ--EKKKPV-FVVATaNNVQSLPPELLRKGRFDE 157
ycf46 CHL00195
Ycf46; Provisional
169-390 4.15e-20

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 92.00  E-value: 4.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 169 GIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEID-AIGGR 247
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 248 RFS--EGTSAdreiqRTLMELLNQLDgfDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAG 325
Cdd:CHL00195 335 ESKgdSGTTN-----RVLATFITWLS--EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQK 407
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922 326 IAKHG--EIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQeDFMKAVRKLSEAKKLESSS 390
Cdd:CHL00195 408 FRPKSwkKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTD-DILLALKQFIPLAQTEKEQ 473
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
151-307 1.25e-19

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: 84.71  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 151 LRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANF--LKVVSSAIIDKyigesarLIREMFNYA 228
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVLTDD-------RLNHLLNTA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 229 RehQPCIIFMDEIDA---IGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKI 305
Cdd:cd19510   74 P--KQSIILLEDIDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151

                 ..
gi 685326922 306 EI 307
Cdd:cd19510  152 YM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
172-311 6.22e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 6.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922   172 PPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVS-----------------SAIIDKYIGESARLIREMFNYAREHQPC 234
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922   235 IIFMDEIDAIggrrfsegTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPgRLDRKIEIPLPN 311
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; ...
166-307 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: 67.79  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 166 LRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDK--------------YIGESARLIREMFNYAREH 231
Cdd:cd19505    5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAM 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685326922 232 QPCIIFMDEIDAIGGRRFSEGTSADREIqrTLMELLNQL-DGFDNLGKVKM--IMATNRPDVLDPALLRPGRLDRKIEI 307
Cdd:cd19505   85 SPCIIWIPNIHELNVNRSTQNLEEDPKL--LLGLLLNYLsRDFEKSSTRNIlvIASTHIPQKVDPALIAPNRLDTCINI 161
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
63-118 1.02e-12

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: 62.52  E-value: 1.02e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922   63 IGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEKLTSGTRVVLDMTTLTIMRALP 118
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 ...
331-375 6.53e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 56.78  E-value: 6.53e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 685326922  331 EIEYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIQEDFMK 375
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
174-306 6.56e-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: 60.23  E-value: 6.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 174 KGVLLYGPPGTGKTLLARAIA--SNIDANFLKVVSSAIIDKyigESARLIREMFNYA-REHQPCIIFMDEIDAIGGRRFS 250
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLAlhSGMDYAIMTGGDVAPMGR---EGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRST 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922 251 EGTSADreIQRTLMELLNQLDGFDNlgKVKMIMATNRPDVLDPALlrPGRLDRKIE 306
Cdd:cd19512  100 EKISED--LRAALNAFLYRTGEQSN--KFMLVLASNQPEQFDWAI--NDRIDEMVE 149
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
176-241 8.31e-11

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.18  E-value: 8.31e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANFLKVvsSAIIDKyIGEsarlIREMFNYAREH----QPCIIFMDEI 241
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAL--SAVTSG-VKD----LREVIEEARQRrsagRRTILFIDEI 101
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
176-295 1.87e-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: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIA---------SNIDANFLKVVSSAIIDKYIGESARLIREMFNYARE---HQPCIIF--MDEI 241
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQElidDKDALVFvlIDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922 242 DAIGGRR--FSEGTSADREIqRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPAL 295
Cdd:cd19508  135 ESLAAARsaSSSGTEPSDAI-RVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
176-241 5.00e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.84  E-value: 5.00e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANFLKVvsSAIIDKyIGEsarlIREMFNYAREH----QPCIIFMDEI 241
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVAL--SAVTSG-VKD----IREVIEEARERraygRRTILFVDEI 114
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
173-267 7.60e-10

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: 57.77  E-value: 7.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 173 PKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIID-KYIGesarliREMFNYAREHQPCIIFMDEIDAIGGRRFSE 251
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119
                         90
                 ....*....|....*..
gi 685326922 252 GTSADRE-IQRTLMELL 267
Cdd:cd19498  120 GPDVSREgVQRDLLPIV 136
PRK04195 PRK04195
replication factor C large subunit; Provisional
171-350 2.85e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 58.78  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 171 KPPKGVLLYGPPGTGKTLLARAIASNIDanfLKVV--------SSAIIDKYIGESARLiREMFNYAREhqpcIIFMDEID 242
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYG---WEVIelnasdqrTADVIERVAGEAATS-GSLFGARRK----LILLDEVD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 243 AIGGRrfsegtsADREIQRTLMELLNQldgfdnlGKVKMIMATNrpDVLDPAlLRPGRlDRKIEIPLPNEQSRmDIL--- 319
Cdd:PRK04195 109 GIHGN-------EDRGGARAILELIKK-------AKQPIILTAN--DPYDPS-LRELR-NACLMIEFKRLSTR-SIVpvl 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 685326922 320 -KIHAA-GIakhgEIEYEAIVKLAEGfNGADLR 350
Cdd:PRK04195 170 kRICRKeGI----ECDDEALKEIAER-SGGDLR 197
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
176-267 4.19e-08

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 53.76  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANFlkvvssAIIDK-------YIGES-----ARLIRE-MFNYAREhQPCIIFMDEID 242
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPF------AIADAttlteagYVGEDvenilLKLLQAaDYDVERA-QRGIVYIDEID 125
                         90       100       110
                 ....*....|....*....|....*....|
gi 685326922 243 AIGgrRFSEGTSADRE-----IQRTLMELL 267
Cdd:cd19497  126 KIA--RKSENPSITRDvsgegVQQALLKIL 153
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
146-386 6.16e-08

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 54.08  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 146 DQIRELRESIElPLMNPElflrvgikPPKGVLLYGPPGTGKTLLARAIAS---------NIDANFLKV----------VS 206
Cdd:COG1474   33 EEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEeleeeaeerGVDVRVVYVncrqastryrVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 207 SAIIDKyIGESARL------IREMFNYAREH-----QPCIIFMDEIDAIGgrrfsegtsaDREIQRTLMELLNQLDGFDN 275
Cdd:COG1474  104 SRILEE-LGSGEDIpstglsTDELFDRLYEAlderdGVLVVVLDEIDYLV----------DDEGDDLLYQLLRANEELEG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 276 lGKVKMIMATNRPDVLDpallrpgRLDRKI-------EIPLPN---EQSRmDILKIHAA-----GIAKHGEIEYeaIVKL 340
Cdd:COG1474  173 -ARVGVIGISNDLEFLE-------NLDPRVksslgeeEIVFPPydaDELR-DILEDRAElafydGVLSDEVIPL--IAAL 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685326922 341 AEGFNGaDLR---NICTEAGMFAIRAERDYVIQED------------FMKAVRKLSEAKKL 386
Cdd:COG1474  242 AAQEHG-DARkaiDLLRVAGEIAEREGSDRVTEEHvrearekierdrLLEVLRGLPTHEKL 301
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
174-288 1.49e-07

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: 50.60  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 174 KGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESA--RLIREMFNYAREHQPCIIFMDEIDAIGGRRF-- 249
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGlqMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVpk 106
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685326922 250 SEGTSADREIQRTLMELLNQLDGFDnlgKVKMIMATNRP 288
Cdd:cd19506  107 TEKQLDPKRLKKDLPKILKSLKPED---RVLIVGTTSRP 142
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
175-297 1.72e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 46.90  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  175 GVLLYGPPGTGKTLLARAIASNID-ANFLKVV------SSAIIDKYI---GESARLIREMFNYAREhqPCIIFMDEIDai 244
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQltrdttEEDLFGRRNidpGGASWVDGPLVRAARE--GEIAVLDEIN-- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922  245 ggrrfsegtSADREIQRTLMELLN-----QLDGFdNLGKVKM-----IMATNRPD----VLDPALLR 297
Cdd:pfam07728  77 ---------RANPDVLNSLLSLLDerrllLPDGG-ELVKAAPdgfrlIATMNPLDrglnELSPALRS 133
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
147-308 3.47e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 49.07  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  147 QIRELRESIELPLMNPELFLRVGIKPpKGVLLYGPPGTGKTLLARAIAsNIDA--------NFLKVVSSAIIDKYIGESA 218
Cdd:TIGR03922 287 QVAALKSSTAMALARAERGLPVAQTS-NHMLFAGPPGTGKTTIARVVA-KIYCglgvlrkpLVREVSRADLIGQYIGESE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  219 RLIREMFNYAREHqpcIIFMDEIDAIGGRRFSEGTSADREIQRTL---MEllNQLDGFdnlgkvKMIMATNRPDvLDPAL 295
Cdd:TIGR03922 365 AKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEAIDTLlarME--NDRDRL------VVIGAGYRKD-LDKFL 432
                         170
                  ....*....|....*...
gi 685326922  296 -----LRpGRLDRKIEIP 308
Cdd:TIGR03922 433 evnegLR-SRFTRVIEFP 449
ycf2 CHL00206
Ycf2; Provisional
135-307 3.95e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 49.14  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  135 NISYSavgglgdQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDK-- 212
Cdd:CHL00206 1599 TITYS-------QTSCGANSFHFPSHGKPFSLRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDNkp 1671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  213 --------------YIGESARLIREM---------------------------FNYAREHQPCIIFMDEIDAIggrrfse 251
Cdd:CHL00206 1672 kgfliddididdsdDIDDSDDIDRDLdtelltmmnaltmdmmpkidrfyitlqFELAKAMSPCIIWIPNIHDL------- 1744
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  252 gtSADREIQRTLMELLNQLdGFD----NLGKVKMIMATNRPDVLDPALLRPGRLDRKIEI 307
Cdd:CHL00206 1745 --NVNESNYLSLGLLVNSL-SRDcercSTRNILVIASTHIPQKVDPALIAPNKLNTCIKI 1801
44 PHA02544
clamp loader, small subunit; Provisional
177-366 8.25e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 47.29  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 177 LLYGP-PGTGKTLLARAIASNIDANFLKVvssaiidkyIGESARL--IR-EMFNYA----REHQPCIIFMDEIDaiggrr 248
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFV---------NGSDCRIdfVRnRLTRFAstvsLTGGGKVIIIDEFD------ 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 249 fSEGTSADREIQRTLMELLNqldgfdnlGKVKMIMATNRPDVLDPALLrpGRLdRKIEIPLPNEQSRMDILK--IH-AAG 325
Cdd:PHA02544 111 -RLGLADAQRHLRSFMEAYS--------KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMMKqmIVrCKG 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 685326922 326 IAKHGEIEYE-----AIVKLaegfNGADLRNICTEAGMFAIRAERD 366
Cdd:PHA02544 179 ILEAEGVEVDmkvlaALVKK----NFPDFRRTINELQRYASTGKID 220
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
176-241 1.61e-05

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: 44.80  E-value: 1.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922  176 VLLYGPPGTGKTLLARAIASNIDANFlKVVSSAIIDKyIGESARLIREMfnyaREHQpcIIFMDEI 241
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL----EPGD--VLFIDEI 93
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
176-289 3.23e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 42.88  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIgesaRLIREmfnYAREHQPCIIFMDEIDAIGGRRFSEGTSA 255
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARASQGDRSSE 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 685326922 256 DREIQRTLMELLNQLDgfdnlgkvKMIMATNRPD 289
Cdd:cd01120   74 LLEDLAKLLRAARNTG--------ITVIATIHSD 99
PRK13341 PRK13341
AAA family ATPase;
177-241 3.24e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.20  E-value: 3.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685326922 177 LLYGPPGTGKTLLARAIASNIDANF--LKVVSSAIIDkyigesarlIREMFNYAREH-----QPCIIFMDEI 241
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFssLNAVLAGVKD---------LRAEVDRAKERlerhgKRTILFIDEV 118
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
176-201 6.58e-05

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: 44.39  E-value: 6.58e-05
                         10        20
                 ....*....|....*....|....*.
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANF 201
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPF 59
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
176-241 6.67e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.35  E-value: 6.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANfLKVVSSAIIDKyigesARLIREMFNYAREHQpcIIFMDEI 241
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-----PGDLAAILTNLEEGD--VLFIDEI 111
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
166-245 1.36e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 43.44  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  166 LRVGIKPPKG-------VLLYGPPGTGKTLLARAIASNIDANfLKVVSSAIIDKyigesARLIREMFNYAREHQpcIIFM 238
Cdd:TIGR00635  16 LQLFIEAAKMrqealdhLLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK-----PGDLAAILTNLEEGD--VLFI 87

                  ....*..
gi 685326922  239 DEIDAIG 245
Cdd:TIGR00635  88 DEIHRLS 94
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
177-308 1.81e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 42.16  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 177 LLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDK---------YIGE-SARLIREMFNyAREHQPcIIFMDEIDAIGG 246
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmPGRIIQALKK-AGTNNP-VFLLDEIDKIGS 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685326922 247 RRFSEGTSAdreiqrtLMELLN--QLDGF-DN-------LGKVKMIMATNRPDVLDPALlrpgrLDRK--IEIP 308
Cdd:cd19500  119 SFRGDPASA-------LLEVLDpeQNSTFsDHyldvpfdLSKVLFIATANSLDTIPGPL-----LDRMeiIELS 180
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
176-259 2.09e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 43.22  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANFlkvvssAIID-------KYIGES-----ARLIREM-FNYAREhQPCIIFMDEID 242
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF------AIADattlteaGYVGEDvenilLKLLQAAdYDVEKA-QRGIVYIDEID 183
                         90
                 ....*....|....*..
gi 685326922 243 AIGgrRFSEGTSADREI 259
Cdd:PRK05342 184 KIA--RKSENPSITRDV 198
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
166-270 2.10e-04

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 41.37  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 166 LRVGIKPPKGVLLYGPPGTGKTLLARAIA-------SNI----DANFL----------------------KVVSSaiidk 212
Cdd:cd03223   20 LSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsGRIgmpeGEDLLflpqrpylplgtlreqliypwdDVLSG----- 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685326922 213 yiGESARLiremfNYARE--HQPCIIFMDeidaiggrrfsEGTSA-DREIQRTLMELLNQL 270
Cdd:cd03223   95 --GEQQRL-----AFARLllHKPKFVFLD-----------EATSAlDEESEDRLYQLLKEL 137
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
173-380 2.54e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 42.65  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 173 PKGVLLYGPPGTGKTLLARAIA-----------------------SNIDANFLkVVSSAIIDKYIGESA--RLIREMFNY 227
Cdd:COG0470   18 PHALLLHGPPGIGKTTLALALArdllcenpeggkacgqchsrlmaAGNHPDLL-ELNPEEKSDQIGIDQirELGEFLSLT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 228 AREHQPCIIFMDEIDAIggrrfseGTSADREIQRTLMELlnqldgfdnLGKVKMIMATNRPDVLDPALlrpgrLDR--KI 305
Cdd:COG0470   97 PLEGGRKVVIIDEADAM-------NEAAANALLKTLEEP---------PKNTPFILIANDPSRLLPTI-----RSRcqVI 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685326922 306 EIPLPNEQSRMDILKihAAGIAkhgEIEYEAIVKLAEGfngaDLRnicteagmFAIRAERDYVIQEDFMKAVRKL 380
Cdd:COG0470  156 RFRPPSEEEALAWLR--EEGVD---EDALEAILRLAGG----DPR--------AAINLLQALAGRKELLEDLAAL 213
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
176-244 2.59e-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: 39.90  E-value: 2.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685326922  176 VLLYGPPGTGKTLLARAIASNIdANFLKVVSSAII-----DKYigesarlireMFNYAreHQPCIIfMDEIDAI 244
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSVYsrnpdDDF----------WDGYT--GQPVVI-IDDFGQN 60
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
173-267 3.20e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 41.03  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  173 PKGV-LLYGPPGTGKTLLARAIAS--NIDANFLKVVSSA------IIDKYIGESARLIR-----EMFNYAREHQPCIIFM 238
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAEllFGDERALIRIDMSeymeehSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81
                          90       100
                  ....*....|....*....|....*....
gi 685326922  239 DEIDaiggrrfsegtSADREIQRTLMELL 267
Cdd:pfam07724  82 DEIE-----------KAHPGVQNDLLQIL 99
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
176-212 3.31e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.38  E-value: 3.31e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANfLKVVSSAIIDK 212
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVN-IRITSGPAIEK 92
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
176-254 3.45e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 42.34  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANFlkvvssAIIDK-------YIGES-----ARLIremfnyarehQPC--------- 234
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVPF------AIADAttlteagYVGEDvenilLKLL----------QAAdydvekaer 175
                         90       100
                 ....*....|....*....|.
gi 685326922 235 -IIFMDEIDAIGgrRFSEGTS 254
Cdd:COG1219  176 gIIYIDEIDKIA--RKSENPS 194
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
170-194 3.99e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.45  E-value: 3.99e-04
                         10        20
                 ....*....|....*....|....*
gi 685326922 170 IKPPKGVLLYGPPGTGKTLLARAIA 194
Cdd:COG1401  218 LKTKKNVILAGPPGTGKTYLARRLA 242
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
167-305 5.16e-04

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: 40.62  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 167 RVGIKPPK---GVLLY-GPPGTGKTLLARAIASNI---DANFLKV----------VSSAIID--KYIG--ESARLIREMf 225
Cdd:cd19499   31 RAGLSDPNrpiGSFLFlGPTGVGKTELAKALAELLfgdEDNLIRIdmseymekhsVSRLIGAppGYVGytEGGQLTEAV- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 226 nyaREHQPCIIFMDEIDaiggrrfsegtSADREIQRTLMELLNqlDGF--DNLGK------VKMIMATNrpdVLDPALLr 297
Cdd:cd19499  110 ---RRKPYSVVLLDEIE-----------KAHPDVQNLLLQVLD--DGRltDSHGRtvdfknTIIIMTSN---HFRPEFL- 169

                 ....*...
gi 685326922 298 pGRLDRKI 305
Cdd:cd19499  170 -NRIDEIV 176
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
144-201 6.22e-04

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: 41.31  E-value: 6.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 685326922 144 LGDQIRELRESIELPLMNPELFlrvgikppkgVLLYGPPGTGKTLLARAIASNIDANF 201
Cdd:COG3267   24 LSPSHREALARLEYALAQGGGF----------VVLTGEVGTGKTTLLRRLLERLPDDV 71
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
143-206 8.27e-04

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: 39.79  E-value: 8.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685326922  143 GLGDQIRELREsielplmnpeLFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVS 206
Cdd:pfam13191   4 GREEELEQLLD----------ALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLR 57
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
174-194 1.06e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.11  E-value: 1.06e-03
                         10        20
                 ....*....|....*....|.
gi 685326922 174 KGVLLYGPPGTGKTLLARAIA 194
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIA 85
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
170-194 1.07e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 1.07e-03
                         10        20
                 ....*....|....*....|....*
gi 685326922 170 IKPPKGVLLYGPPGTGKTLLARAIA 194
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALG 120
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
176-195 1.33e-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: 40.79  E-value: 1.33e-03
                         10        20
                 ....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIAS 195
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
176-324 1.34e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 40.17  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNIDANF--LKVVssaiidkYIgESARLIREMFNYAREHQP----------CIIFMDEIDA 243
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEALENNpgARVV-------YL-TAEEFTNDFINAIRNNTIeefkekyrsvDVLLIDDIQF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 244 IGGRrfsEGTsadreiQRTLMELLNQLdgFDNlGKvKMIMATNRPdvldPALLrPGRLDR---------KIEIPLPNEQS 314
Cdd:COG0593  109 LAGK---EAT------QEEFFHTFNAL--REA-GK-QIVLTSDRP----PKEL-PGLEERlrsrlewglVVDIQPPDLET 170
                        170
                 ....*....|
gi 685326922 315 RMDILKIHAA 324
Cdd:COG0593  171 RIAILRKKAA 180
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
176-198 1.95e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 39.60  E-value: 1.95e-03
                          10        20
                  ....*....|....*....|...
gi 685326922  176 VLLYGPPGTGKTLLARAIASNID 198
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIAHAVP 138
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
176-195 2.56e-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: 38.67  E-value: 2.56e-03
                          10        20
                  ....*....|....*....|
gi 685326922  176 VLLYGPPGTGKTLLARAIAS 195
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
PRK08116 PRK08116
hypothetical protein; Validated
175-194 3.50e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.85  E-value: 3.50e-03
                         10        20
                 ....*....|....*....|
gi 685326922 175 GVLLYGPPGTGKTLLARAIA 194
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIA 135
Sigma54_activat pfam00158
Sigma-54 interaction domain;
176-241 3.69e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.77  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  176 VLLYGPPGTGKTLLARAI--ASN-IDANFLKVVSSAIIDKYIgESarlirEMFNY-------AREHQP--------CIIF 237
Cdd:pfam00158  25 VLITGESGTGKELFARAIhqLSPrADGPFVAVNCAAIPEELL-ES-----ELFGHekgaftgADSDRKglfeladgGTLF 98

                  ....
gi 685326922  238 MDEI 241
Cdd:pfam00158  99 LDEI 102
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
146-380 4.04e-03

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 39.15  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  146 DQIRELRESIElPLMNPElflrvgikPPKGVLLYGPPGTGKTLLAR-------AIASNIDANFLKV-VSSAIIDKY---- 213
Cdd:TIGR02928  22 EQIEELAKALR-PILRGS--------RPSNVFIYGKTGTGKTAVTKyvmkeleEAAEDRDVRVVTVyVNCQILDTLyqvl 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  214 ---------IGES--------ARLIREMFNYAREHQPCIIF-MDEIDAIGGrrfsegtsadrEIQRTLMELL-----NQL 270
Cdd:TIGR02928  93 velanqlrgSGEEvpttglstSEVFRRLYKELNERGDSLIIvLDEIDYLVG-----------DDDDLLYQLSrarsnGDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922  271 DGfdnlGKVKMIMATNRP---DVLDPAL---LRPgrldRKIEIPLPNEQSRMDILKIHAAGIAKHGEIEYEAIVKLAE-- 342
Cdd:TIGR02928 162 DN----AKVGVIGISNDLkfrENLDPRVkssLCE----EEIIFPPYDAEELRDILENRAEKAFYDGVLDDGVIPLCAAla 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 685326922  343 GFNGADLR---NICTEAGMFAIRAERDYVIQEDFMKAVRKL 380
Cdd:TIGR02928 234 AQEHGDARkaiDLLRVAGEIAEREGAERVTEDHVEKAQEKI 274
PRK06835 PRK06835
DNA replication protein DnaC; Validated
145-202 7.95e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 37.96  E-value: 7.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 685326922 145 GDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASN-IDANFL 202
Cdd:PRK06835 155 DDEPLSPRKNMEKILEKCKNFIENFDKNNENLLFYGNTGTGKTFLSNCIAKElLDRGKS 213
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
176-297 8.46e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 38.63  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685326922 176 VLLYGPPGTGKTLLARAIASNI----------------------DANFLKVVSSAIIDKYiGESARLIREMFnyaREHQP 233
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELaeryldaedpipilielrdlaeEASLEDLLAEALEKRG-GEPEDALERLL---RNGRL 258
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685326922 234 CIIF--MDEIDAIGGRRfsegtsadreiqrtlmELLNQLDGF-DNLGKVKMIMATnRPDVLDPALLR 297
Cdd:COG5635  259 LLLLdgLDEVPDEADRD----------------EVLNQLRRFlERYPKARVIITS-RPEGYDSSELE 308
 
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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