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Conserved domains on  [gi|17563248|ref|NP_506005|]
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26S proteasome regulatory subunit 7 [Caenorhabditis elegans]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
117-420 1.21e-157

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 450.44  E-value: 1.21e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  117 VKQFA--KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVE 194
Cdd:PRK03992  69 VKSSGgpQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  195 TPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLI 274
Cdd:PRK03992 149 LPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSII 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  275 FFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRA 354
Cdd:PRK03992 229 FIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRL 308
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17563248  355 HILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKVVK 420
Cdd:PRK03992 309 EILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMG 374
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
117-420 1.21e-157

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 450.44  E-value: 1.21e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  117 VKQFA--KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVE 194
Cdd:PRK03992  69 VKSSGgpQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  195 TPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLI 274
Cdd:PRK03992 149 LPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSII 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  275 FFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRA 354
Cdd:PRK03992 229 FIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRL 308
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17563248  355 HILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKVVK 420
Cdd:PRK03992 309 EILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMG 374
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
122-418 3.87e-132

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: 384.92  E-value: 3.87e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   122 KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPE 201
Cdd:TIGR01242  67 NFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   202 RYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDA 281
Cdd:TIGR01242 147 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDA 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   282 VGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHA 361
Cdd:TIGR01242 227 IAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHT 306
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17563248   362 KQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKV 418
Cdd:TIGR01242 307 RKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
166-420 5.13e-132

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 383.20  E-value: 5.13e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 166 MQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGS 245
Cdd:COG1222  67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 246 ELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGdnEVQRTMLELINQLDGFDPRGNIKVLMATNR 325
Cdd:COG1222 147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 326 PDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 405
Cdd:COG1222 225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304
                       250
                ....*....|....*
gi 17563248 406 ATEKDFLEAINKVVK 420
Cdd:COG1222 305 VTMEDLEKAIEKVKK 319
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
175-345 3.38e-123

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: 354.72  E-value: 3.38e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 175 TYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGE 254
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 255 GARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALM 334
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 17563248 335 RPGRLDRKVEF 345
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
214-345 6.89e-50

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 165.46  E-value: 6.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   214 VLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDdgqGG 293
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17563248   294 DNEVQRTMLELINQLDGFDPR-GNIKVLMATNRPDTLDPALMrpGRLDRKVEF 345
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEF 128
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
210-349 6.57e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.19  E-value: 6.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248    210 PPKGVLLYGPPGTGKTLCARAVAN---RTDACFIRVIGSEL--------------VQKYVGEGARMVRELFEMARTKKAC 272
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17563248    273 LIFFDEIDAVGGARFddgqggdnEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPgRLDRKVEFALPD 349
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
214-308 6.52e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 37.84  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  214 VLLYGPPGTGKT-----LCARAVANRTDACFIRVigSELVQKYvgEGARMVRELFEMART-KKACLIFFDEIdavGGARF 287
Cdd:NF038214  93 VLLLGPPGTGKThlaiaLGYAACRQGYRVRFTTA--ADLVEQL--AQARADGRLGRLLRRlARYDLLIIDEL---GYLPF 165
                         90       100
                 ....*....|....*....|.
gi 17563248  288 DDGQGGDnevqrtMLELINQL 308
Cdd:NF038214 166 SREGANL------LFELIADR 180
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
117-420 1.21e-157

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 450.44  E-value: 1.21e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  117 VKQFA--KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVE 194
Cdd:PRK03992  69 VKSSGgpQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  195 TPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLI 274
Cdd:PRK03992 149 LPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSII 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  275 FFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRA 354
Cdd:PRK03992 229 FIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRL 308
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17563248  355 HILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKVVK 420
Cdd:PRK03992 309 EILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMG 374
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
122-418 3.87e-132

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: 384.92  E-value: 3.87e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   122 KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPE 201
Cdd:TIGR01242  67 NFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   202 RYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDA 281
Cdd:TIGR01242 147 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDA 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   282 VGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHA 361
Cdd:TIGR01242 227 IAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHT 306
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17563248   362 KQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKV 418
Cdd:TIGR01242 307 RKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
166-420 5.13e-132

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 383.20  E-value: 5.13e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 166 MQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGS 245
Cdd:COG1222  67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 246 ELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGdnEVQRTMLELINQLDGFDPRGNIKVLMATNR 325
Cdd:COG1222 147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 326 PDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 405
Cdd:COG1222 225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304
                       250
                ....*....|....*
gi 17563248 406 ATEKDFLEAINKVVK 420
Cdd:COG1222 305 VTMEDLEKAIEKVKK 319
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
175-345 3.38e-123

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: 354.72  E-value: 3.38e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 175 TYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGE 254
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 255 GARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALM 334
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 17563248 335 RPGRLDRKVEF 345
Cdd:cd19502 161 RPGRFDRKIEF 171
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
94-429 5.35e-112

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 336.36  E-value: 5.35e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   94 PLQVARCTKI------ITSDKHDPRYLINVKQFakfvvdladsVAPTDIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQ 167
Cdd:PTZ00361 104 PLSVGTLEEIidenhaIVSSSVGPEYYVNILSF----------VDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMK 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  168 VEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSEL 247
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEL 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  248 VQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPD 327
Cdd:PTZ00361 254 IQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIE 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  328 TLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVAT 407
Cdd:PTZ00361 334 SLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVT 413
                        330       340
                 ....*....|....*....|..
gi 17563248  408 EKDFLEAINKVVkgYAKFSATP 429
Cdd:PTZ00361 414 QADFRKAKEKVL--YRKKGNIP 433
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
135-420 5.30e-111

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 332.11  E-value: 5.30e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  135 DIEEGMRVGVDRNKYQIHLPLPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGV 214
Cdd:PTZ00454 103 LLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  215 LLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGD 294
Cdd:PTZ00454 183 LLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGAD 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  295 NEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRY-D 373
Cdd:PTZ00454 263 REVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLeD 342
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 17563248  374 LLARlcPNS-TGAEIRSVCTEAGMFAIRARRKVATEKDFLEAINKVVK 420
Cdd:PTZ00454 343 FVSR--PEKiSAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVR 388
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
166-426 1.74e-89

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: 280.33  E-value: 1.74e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   166 MQVEEKPDVTYSDVGGCKDQIEKLREVVETpLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGS 245
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   246 ELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNR 325
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   326 PDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 405
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282
                         250       260
                  ....*....|....*....|.
gi 17563248   406 ATEKDFLEAINKVVKGYAKFS 426
Cdd:TIGR01241 283 ITMNDIEEAIDRVIAGPEKKS 303
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
166-424 9.63e-87

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 275.38  E-value: 9.63e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 166 MQVEEKPDVTYSDVGGCKDQIEKLREVVETpLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGS 245
Cdd:COG0465 131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 246 ELVQKYVGEGARMVRELFEMARtKKA-CLIFFDEIDAVGGARfDDGQGGDN-EVQRTmlelINQL----DGFDPRGNIKV 319
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAK-KNApCIIFIDEIDAVGRQR-GAGLGGGHdEREQT----LNQLlvemDGFEGNEGVIV 283
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 320 LMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAI 399
Cdd:COG0465 284 IAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAA 363
                       250       260
                ....*....|....*....|....*
gi 17563248 400 RARRKVATEKDFLEAINKVVKGYAK 424
Cdd:COG0465 364 RRNKKAVTMEDFEEAIDRVIAGPER 388
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
75-418 1.56e-74

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: 238.66  E-value: 1.56e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  75 APPALWDIAADKQAMQQEQPLQVARCTKIITSDKHDPRYLINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLP 154
Cdd:COG0464  55 ELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAP 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 155 LPAKIDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANR 234
Cdd:COG0464 135 LVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGE 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 235 TDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLElinQLDGFdpR 314
Cdd:COG0464 215 LGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLT---EMEEL--R 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 315 GNIKVLMATNRPDTLDPALMRpgRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEA 394
Cdd:COG0464 290 SDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRA 367
                       330       340
                ....*....|....*....|....
gi 17563248 395 GMFAIRARRKVATEKDFLEAINKV 418
Cdd:COG0464 368 ALQALRLGREPVTTEDLLEALERE 391
ftsH CHL00176
cell division protein; Validated
167-423 4.34e-72

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 238.80  E-value: 4.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  167 QVEEKPDVTYSDVGGCKDQIEKLREVVeTPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSE 246
Cdd:CHL00176 173 QMEADTGITFRDIAGIEEAKEEFEEVV-SFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSE 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  247 LVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRP 326
Cdd:CHL00176 252 FVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRV 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  327 DTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVA 406
Cdd:CHL00176 332 DILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATI 411
                        250
                 ....*....|....*..
gi 17563248  407 TEKDFLEAINKVVKGYA 423
Cdd:CHL00176 412 TMKEIDTAIDRVIAGLE 428
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
159-418 2.04e-70

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 236.34  E-value: 2.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   159 IDPTVTMMQVEEKPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDAC 238
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGAN 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   239 FIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARfddGQGGDNEV-QRTMLELINQLDGFDPRGNI 317
Cdd:TIGR01243 515 FIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR---GARFDTSVtDRIVNQLLTEMDGIQELSNV 591
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   318 KVLMATNRPDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMF 397
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMA 671
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 17563248   398 AIRARRK------------------VATEKDFLEAINKV 418
Cdd:TIGR01243 672 ALRESIGspakeklevgeeeflkdlKVEMRHFLEALKKV 710
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
174-343 2.19e-70

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 219.80  E-value: 2.19e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 174 VTYSDVGGCKDQIEKLREVVETpLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVG 253
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 254 EGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPAL 333
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|
gi 17563248 334 MRPGRLDRKV 343
Cdd:cd19501 160 LRPGRFDRQV 169
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
166-426 1.63e-69

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 231.85  E-value: 1.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  166 MQVEEKPDVTYSDVGGCKDQIEKLREVVETpLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGS 245
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  246 ELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNR 325
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  326 PDTLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 405
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                        250       260
                 ....*....|....*....|.
gi 17563248  406 ATEKDFLEAINKVVKGYAKFS 426
Cdd:PRK10733 380 VSMVEFEKAKDKIMMGAERRS 400
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
172-400 8.17e-69

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: 232.10  E-value: 8.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   172 PDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKY 251
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   252 VGEGARMVRELFEMARTKKACLIFFDEIDAVGGARfdDGQGGDNEvQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDP 331
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17563248   332 ALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIR 400
Cdd:TIGR01243 330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
178-345 9.45e-68

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: 212.92  E-value: 9.45e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 257
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 258 MVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELinqLDGFDPRGNIKVLMATNRPDTLDPALMRPG 337
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTL---MDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                ....*...
gi 17563248 338 RLDRKVEF 345
Cdd:cd19503 158 RFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
187-341 1.73e-64

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 204.44  E-value: 1.73e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 187 EKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 266
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17563248 267 RTKKACLIFFDEIDAVGGARFDDGQGGDNEvqRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDR 341
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
178-344 7.92e-60

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 192.65  E-value: 7.92e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 257
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 258 MVRELFEMARTKKACLIFFDEIDAVGGARfDDGQGgdnEVQRTML-ELINQLDGFDPRGNIKVLMATNRPDTLDPALMRP 336
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHG---EVERRIVsQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                ....*...
gi 17563248 337 GRLDRKVE 344
Cdd:cd19519 157 GRFDREID 164
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
187-343 6.83e-59

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: 190.01  E-value: 6.83e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 187 EKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 266
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17563248 267 RTKKACLIFFDEIDAVGGARfddGQGGDNEV-QRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKV 343
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRR---GTTGDSGVtERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
185-345 8.00e-59

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 189.80  E-value: 8.00e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 185 QIEKLREVVETPLLHPERYvNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFE 264
Cdd:cd19481   1 LKASLREAVEAPRRGSRLR-RYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 265 MARTKKACLIFFDEIDAVGGARfdDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVE 344
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 17563248 345 F 345
Cdd:cd19481 158 F 158
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
110-360 4.50e-58

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: 198.39  E-value: 4.50e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   110 DPRYLINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHLPLPAKidpTVTMMQVEEKPDVTYSDVGGCKDQIEKL 189
Cdd:TIGR03689 118 DGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGYAFEAIPRT---EVEDLVLEEVPDVTYADIGGLGSQIEQI 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   190 REVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVAN----------RTDACFIRVIGSELVQKYVGEGARMV 259
Cdd:TIGR03689 195 RDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNKYVGETERQI 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   260 RELFEMARTKKA----CLIFFDEIDAVGGARfddGQGGDNEVQRTML-ELINQLDGFDPRGNIKVLMATNRPDTLDPALM 334
Cdd:TIGR03689 275 RLIFQRAREKASegrpVIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAIL 351
                         250       260
                  ....*....|....*....|....*.
gi 17563248   335 RPGRLDRKVEFALPDLAGRAHILKIH 360
Cdd:TIGR03689 352 RPGRLDVKIRIERPDAEAAADIFAKY 377
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
187-343 1.87e-53

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: 175.78  E-value: 1.87e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 187 EKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 266
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17563248 267 RTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKV 343
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
177-417 9.26e-51

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 171.61  E-value: 9.26e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 177 SDVGGCKDQIEKLREVVETpLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGA 256
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 257 RMVRELFEMARTKKaCLIFFDEIDAVGGARFDDGQGGdnEVQRTMLELINQLDGFdpRGNIKVLMATNRPDTLDPALMRp 336
Cdd:COG1223  81 RNLRKLFDFARRAP-CVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 337 gRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAIN 416
Cdd:COG1223 155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                .
gi 17563248 417 K 417
Cdd:COG1223 234 Q 234
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
214-345 6.89e-50

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 165.46  E-value: 6.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   214 VLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDdgqGG 293
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17563248   294 DNEVQRTMLELINQLDGFDPR-GNIKVLMATNRPDTLDPALMrpGRLDRKVEF 345
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEF 128
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
187-341 1.06e-49

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 166.12  E-value: 1.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 187 EKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 266
Cdd:cd19530   6 EELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRA 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17563248 267 RTKKACLIFFDEIDAVGGARfddGQGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDR 341
Cdd:cd19530  86 RASAPCVIFFDEVDALVPKR---GDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
178-345 7.03e-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: 164.22  E-value: 7.03e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVAN------RTDACFIRViGSELVQKY 251
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAecskggQKVSFFMRK-GADCLSKW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 252 VGEGARMVRELFEMARTKKACLIFFDEIDAVGGARFDDGQGGDNEVQRTMLELinqLDGFDPRGNIKVLMATNRPDTLDP 331
Cdd:cd19517  80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDP 156
                       170
                ....*....|....
gi 17563248 332 ALMRPGRLDRKVEF 345
Cdd:cd19517 157 ALRRPGRFDREFYF 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
179-343 9.98e-46

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: 155.59  E-value: 9.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 179 VGGCKDQIEKLREVVETPLLHPERYVNLgIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARM 258
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 259 VRELFEMARTKKACLIFFDEIDAVGGARFDdgqgGDNEVQRTM-LELINQLDGF--DPRGNIKVLMATNRPDTLDPALMR 335
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155

                ....*...
gi 17563248 336 pgRLDRKV 343
Cdd:cd19509 156 --RFEKRI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
178-343 2.09e-45

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: 155.26  E-value: 2.09e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 257
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 258 MVRELFEMARTKKACLIFFDEIDAVGGARfdDGQGGDNEvQRTMLELINQLDGF----DPRGNIKVLMATNRPDTLDPAL 333
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 17563248 334 MRPGRLDRKV 343
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
189-344 2.01e-42

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: 146.80  E-value: 2.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 189 LREVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMART 268
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17563248 269 KKACLIFFDEIDAVGGARFDDGQGgdnEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVE 344
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
191-341 7.12e-42

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 145.73  E-value: 7.12e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 191 EVVETPLLHPERYvNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKK 270
Cdd:cd19527   7 DTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAK 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563248 271 ACLIFFDEIDAVGGARfddGQGGDNE--VQRTMLELINQLDGF-DPRGNIKVLMATNRPDTLDPALMRPGRLDR 341
Cdd:cd19527  86 PCVIFFDELDSLAPSR---GNSGDSGgvMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
172-335 6.48e-39

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 138.58  E-value: 6.48e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 172 PDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNLGiEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKY 251
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 252 VGEGARMVRELFEMARTKKACLIFFDEIDAVGGARfddGQGGDNEVQRTMLELINQLDGFD--PRGNIKVLMATNRPDTL 329
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEI 172

                ....*.
gi 17563248 330 DPALMR 335
Cdd:cd19525 173 DEAARR 178
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
171-343 1.34e-38

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: 137.30  E-value: 1.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 171 KPDVTYSDVGGCKDQIEKLREVVETPLLHPERYVNlGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQK 250
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 251 YVGEGARMVRELFEMARTKKACLIFFDEIDAVGGARfddGQGGDNEVQRTMLELINQLDGF--DPRGnIKVLMATNRPDT 328
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR---GEGESEASRRIKTELLVQMNGVgnDSQG-VLVLGATNIPWQ 155
                       170
                ....*....|....*
gi 17563248 329 LDPALMRpgRLDRKV 343
Cdd:cd19521 156 LDSAIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
178-335 1.76e-37

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: 134.09  E-value: 1.76e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLGI-EPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGA 256
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 257 RMVRELFEMARTKKACLIFFDEIDAVGGARfddgQGGDNEVQRTM-LELINQLDGFDPRGNIKVLM--ATNRPDTLDPAL 333
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156

                ..
gi 17563248 334 MR 335
Cdd:cd19520 157 LR 158
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
178-343 9.50e-35

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: 127.02  E-value: 9.50e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVnlGIEPP-KGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGA 256
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 257 RMVRELFEMARTKKACLIFFDEIDAVGGARfddGQGGDNEV-QRTMLELINQLDGF-------DPRGNIKVLMATNRPDT 328
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155
                       170
                ....*....|....*
gi 17563248 329 LDPALMRpgRLDRKV 343
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
178-343 2.17e-31

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: 117.64  E-value: 2.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLGiEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 257
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 258 MVRELFEMARTKKACLIFFDEIDAVGGARFDdgqgGDNEVQRTM-LELINQLDGFDPRGNIKVLM--ATNRPDTLDPALM 334
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVL 155

                ....*....
gi 17563248 335 RpgRLDRKV 343
Cdd:cd19524 156 R--RFTKRV 162
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
179-344 3.51e-30

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 114.89  E-value: 3.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 179 VGGCKDQIEKL-REVVETPLLHPERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVI-GSELVQKYVGEGA 256
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 257 RMVRELFEMA-RTKKAC-------LIFFDEIDAV---GGARFDDGQGGDNEVQrtmlELINQLDGFDPRGNIKVLMATNR 325
Cdd:cd19504  82 ANIRKLFADAeEEQRRLgansglhIIIFDEIDAIckqRGSMAGSTGVHDTVVN----QLLSKIDGVEQLNNILVIGMTNR 157
                       170
                ....*....|....*....
gi 17563248 326 PDTLDPALMRPGRLDRKVE 344
Cdd:cd19504 158 KDLIDEALLRPGRLEVQME 176
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
178-335 3.68e-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: 103.43  E-value: 3.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 178 DVGGCKDQIEKLREVVETPLLHPERYVNLgIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 257
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 258 MVRELFEMARTKKACLIFFDEIDAVGGARFDdgqgGDNEVQRTMLELINQLDGF--DPRGNIKVLMATNRPDTLDPALMR 335
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
180-347 5.09e-26

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 102.99  E-value: 5.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 180 GGCKDQIEKLREVVETPllhperyvnlgiePPKGVLLYGPPGTGKTLCARAVAN---RTDACFIRVIGSELVQKYVGEGA 256
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 257 R---MVRELFEMARTKKACLIFFDEIDAVGgarfddgqggdNEVQRTMLELINQL-DGFDPRGNIKVLMATNRPDTLDPA 332
Cdd:cd00009  68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136
                       170
                ....*....|....*
gi 17563248 333 LMRPGRLDRKVEFAL 347
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
172-419 1.07e-21

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 97.01  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  172 PDVTYSDVGGC---KDQIEKLREVVEtpllhpERYVNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELV 248
Cdd:CHL00195 223 VNEKISDIGGLdnlKDWLKKRSTSFS------KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  249 QKYVGEGARMVRELFEMARTKKACLIFFDEID-AVGGARFDDGQGGDNEVQRTMLELINQLDGFdprgnIKVLMATNRPD 327
Cdd:CHL00195 297 GGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEKKSP-----VFVVATANNID 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  328 TLDPALMRPGRLDRKVEFALPDLAGRAHILKIHAKQMSVERDIRYD--LLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 405
Cdd:CHL00195 372 LLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDikKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREF 451
                        250
                 ....*....|....
gi 17563248  406 ATEkDFLEAINKVV 419
Cdd:CHL00195 452 TTD-DILLALKQFI 464
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
210-349 6.57e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.19  E-value: 6.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248    210 PPKGVLLYGPPGTGKTLCARAVAN---RTDACFIRVIGSEL--------------VQKYVGEGARMVRELFEMARTKKAC 272
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17563248    273 LIFFDEIDAVGGARFddgqggdnEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPgRLDRKVEFALPD 349
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
205-341 5.55e-18

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: 80.88  E-value: 5.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 205 NLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEID-AVG 283
Cdd:cd19507  25 AYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFS 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17563248 284 GARFDDGQGGDNEVQRTMLELINQldgfdpRGNIKVLMAT-NRPDTLDPALMRPGRLDR 341
Cdd:cd19507 105 NADSKGDSGTSSRVLGTFLTWLQE------KKKPVFVVATaNNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
203-345 3.73e-15

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: 72.38  E-value: 3.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 203 YVNLGIEPPKGVLLYGPPGTGKTLCARAVAN--RTDACFIrvigsELVQkyVGEGARMVRELfeMARTKKACLIFFDEID 280
Cdd:cd19510  15 YNDRGIPYRRGYLLYGPPGTGKSSFIAALAGelDYDICDL-----NLSE--VVLTDDRLNHL--LNTAPKQSIILLEDID 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 281 AVGGARFDDGQ-----GGDNEVqrTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEF 345
Cdd:cd19510  86 AAFESREHNKKnpsayGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
212-345 1.03e-10

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 59.85  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 212 KGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSElVQKYVGEGARMVRELFEMART-KKACLIFFDEIDAVGGARFDDG 290
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEK 101
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17563248 291 QggdNEVQRTMLELINQLDGfDPRGNIKVLMATNRPDTLDPALMrpGRLDRKVEF 345
Cdd:cd19512 102 I---SEDLRAALNAFLYRTG-EQSNKFMLVLASNQPEQFDWAIN--DRIDEMVEF 150
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
187-333 2.06e-09

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 57.07  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 187 EKLREVVETPLLHPERYVNLG-IEPPKGVLLYGPPGTGKTLCARAVANRTD---------ACFIRVIGSELVQKYVGEGA 256
Cdd:cd19508  27 SRLLDYVTTTLLFSDKNVNTNlITWNRLVLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESG 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 257 RMVRELF----EMARTKKaCLIF--FDEIDAVGGARFDDGQGGD-NEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTL 329
Cdd:cd19508 107 KLVTKMFqkiqELIDDKD-ALVFvlIDEVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKI 185

                ....
gi 17563248 330 DPAL 333
Cdd:cd19508 186 DVAF 189
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
369-413 2.24e-09

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 52.54  E-value: 2.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17563248   369 DIRYDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLE 413
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
211-305 2.01e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 53.92  E-value: 2.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 211 PKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQ-KYVGEGAR-MVRELFEmartkkaCLIFFDEIDAVGGARFD 288
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGRDVEsIIRDLVE-------GIVFIDEIDKIAKRGGS 118
                        90
                ....*....|....*...
gi 17563248 289 DGQGGDNE-VQRTMLELI 305
Cdd:cd19498 119 SGPDVSREgVQRDLLPIV 136
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
206-341 4.13e-08

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: 52.38  E-value: 4.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 206 LGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQK--------------YVGEGARMVRELFEMARTKKA 271
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMSP 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563248 272 CLIFFDEIDAVGGARFDDGQGGDNevqRTMLELINQLDGFDPRG----NIKVLMATNRPDTLDPALMRPGRLDR 341
Cdd:cd19505  87 CIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKsstrNILVIASTHIPQKVDPALIAPNRLDT 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
165-286 7.27e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 54.54  E-value: 7.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  165 MMQVEEK--PdVTYSDVGGCKDQIEKLREVVETpLLHPEryvnlgiePPKGVLLYGPPGTGKTLCARAVANRtdacfirv 242
Cdd:PRK04195   1 MMPWVEKyrP-KTLSDVVGNEKAKEQLREWIES-WLKGK--------PKKALLLYGPPGVGKTSLAHALAND-------- 62
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17563248  243 IGSELV-------------QKYVGEGARMvRELFEMARTkkacLIFFDEIDAV------GGAR 286
Cdd:PRK04195  63 YGWEVIelnasdqrtadviERVAGEAATS-GSLFGARRK----LILLDEVDGIhgnedrGGAR 120
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
214-279 2.21e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.78  E-value: 2.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17563248  214 VLLYGPPGTGKTLCARAVANRTDACFIR---VIGSelvqkyVGEgarmVRELFEMARTKKA----CLIFFDEI 279
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAlsaVTSG------VKD----LREVIEEARQRRSagrrTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
214-279 2.44e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 52.75  E-value: 2.44e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 214 VLLYGPPGTGKTLCARAVANRTDACFIRVIGselvqkyVGEGARMVRELFEMARTKKA----CLIFFDEI 279
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRAygrrTILFVDEI 114
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
184-234 1.43e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 50.23  E-value: 1.43e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 17563248 184 DQIEKLREVVEtPLLHPERYVNlgieppkgVLLYGPPGTGKTLCARAVANR 234
Cdd:COG1474  33 EEIEELASALR-PALRGERPSN--------VLIYGPTGTGKTAVAKYVLEE 74
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
183-377 1.31e-05

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: 47.53  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   183 KDQIEKLREVVETPLLHPERyvnlGIEPP---KGVLLYGPPGTGKTLCARAVANR-------TDACFIRVIGSELVQKYV 252
Cdd:TIGR03922 285 KRQVAALKSSTAMALARAER----GLPVAqtsNHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYI 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   253 GEGARMVRELFEMARTKkacLIFFDEIDAVGGARfdDGQGGDnevqrTMLELINQLDGF--DPRGNIKVLMATNRPD--- 327
Cdd:TIGR03922 361 GESEAKTNEIIDSALGG---VLFLDEAYTLVETG--YGQKDP-----FGLEAIDTLLARmeNDRDRLVVIGAGYRKDldk 430
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17563248   328 --TLDPALMRpgRLDRKVEFalpDLAGRAHILKIhAKQMSVERDIRYDLLAR 377
Cdd:TIGR03922 431 flEVNEGLRS--RFTRVIEF---PSYSPDELVEI-ARRMATERDSVLDDAAA 476
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
213-335 2.52e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 43.82  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   213 GVLLYGPPGTGKTLCARAVANRTDAC--FIRVIG-----SELVQKYV--GEGARMV-RELFEMARtkKACLIFFDEIDAV 282
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRpvFYVQLTrdtteEDLFGRRNidPGGASWVdGPLVRAAR--EGEIAVLDEINRA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17563248   283 GGarfddgqggdnEVQRTMLELIN-----QLDGF----DPRGNIKVLMATNRPDT----LDPALMR 335
Cdd:pfam07728  79 NP-----------DVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
215-345 8.20e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.93  E-value: 8.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 215 LLYGPPGTGKTLCARAVA---NRTDACFIRVIGSELVQK------------YVGEGARMVreLFEMARTKKACLIFFDEI 279
Cdd:cd19499  45 LFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGGQ--LTEAVRRKPYSVVLLDEI 122
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563248 280 DAVggarfddgqggDNEVQRTMLELINqlDGF--DPRG------NIKVLMATNrpdTLDPALMrpGRLDRKVEF 345
Cdd:cd19499 123 EKA-----------HPDVQNLLLQVLD--DGRltDSHGrtvdfkNTIIIMTSN---HFRPEFL--NRIDEIVVF 178
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
204-338 8.50e-05

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 42.62  E-value: 8.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 204 VNLGIEPPKGVLLYGPPGTGKTLCARAVANRTDACFIRVI--GSELVQKYVGEGARMV----------RELFEMART--K 269
Cdd:cd00267  18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILidGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllL 97
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563248 270 KACLIFFDEIDAvggarfddgqGGDNEVQRTMLELINQLdgfdPRGNIKVLMATNRPDTLDPA-----LMRPGR 338
Cdd:cd00267  98 NPDLLLLDEPTS----------GLDPASRERLLELLREL----AEEGRTVIIVTHDPELAELAadrviVLKDGK 157
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
211-305 1.04e-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: 42.57  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   211 PKGV-LLYGPPGTGKTLCARAVANR---TDACFIRVIGSELVQK------------YVG--EGArmvrELFEMARTKKAC 272
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEhsvsrligappgYVGyeEGG----QLTEAVRRKPYS 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 17563248   273 LIFFDEID-AVGGarfddgqggdneVQRTMLELI 305
Cdd:pfam07724  78 IVLIDEIEkAHPG------------VQNDLLQIL 99
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
208-308 1.80e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.85  E-value: 1.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 208 IEPPKGVLLYGPPGTGKTLCARAVANRtdAC-------FIRVigSELVQKYvgEGARMVRELFE-MARTKKACLIFFDEI 279
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALGHE--ACragyrvrFTTA--PDLVNEL--KEARADGRLERlLKRLAKVDLLILDEL 169
                        90       100
                ....*....|....*....|....*....
gi 17563248 280 davGGARFDDGQGGDnevqrtMLELINQL 308
Cdd:COG1484 170 ---GYLPLDAEGAEL------LFELISDR 189
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
184-280 2.92e-04

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: 42.62  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   184 DQIEKLREVVEtPLLHPERyvnlgiepPKGVLLYGPPGTGKTLCARAVANR----TDACFIRV---------------IG 244
Cdd:TIGR02928  22 EQIEELAKALR-PILRGSR--------PSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVL 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 17563248   245 SELVQKYVGEG----------ARMVRELF-EMARTKKACLIFFDEID 280
Cdd:TIGR02928  93 VELANQLRGSGeevpttglstSEVFRRLYkELNERGDSLIIVLDEID 139
PRK13341 PRK13341
AAA family ATPase;
215-240 5.23e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 42.35  E-value: 5.23e-04
                         10        20
                 ....*....|....*....|....*.
gi 17563248  215 LLYGPPGTGKTLCARAVANRTDACFI 240
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFS 81
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
214-280 6.65e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 41.31  E-value: 6.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 214 VLLYGPPGTGKTLCARAVANRTDACFIRV-----------IGSELVQKYVGEgarmvrelFEMartKK----ACLIFFDE 278
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGE--------FEF---RPgplfANVLLADE 102

                ..
gi 17563248 279 ID 280
Cdd:COG0714 103 IN 104
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
197-305 9.96e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 40.66  E-value: 9.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 197 LLHPERYVNLGIEPPKG-VLLYGPPGTGKTLCARAVANRTDACFIRVIGSELVQK-YVGEGAR--MVREL----FEMART 268
Cdd:cd19497  35 IRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGEDVEniLLKLLqaadYDVERA 114
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17563248 269 KKAcLIFFDEIDAVG-------GARFDDGQGgdneVQRTMLELI 305
Cdd:cd19497 115 QRG-IVYIDEIDKIArksenpsITRDVSGEG----VQQALLKIL 153
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
214-419 1.32e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 40.56  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 214 VLLYGPPGTGKTLCARAVANRtdacfIRVIGSELVQKYVgEGARMVRELFEMARTKK--ACLIFFDEIDAVggaRFDDGQ 291
Cdd:COG0593  37 LFLYGGVGLGKTHLLHAIGNE-----ALENNPGARVVYL-TAEEFTNDFINAIRNNTieEFKEKYRSVDVL---LIDDIQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 292 --GGDNEVQRTMLELINQLDgfdpRGNIKVLMATNRPdtldPALMrPGRLDR---------KVEFALPDLAGRAHIL--K 358
Cdd:COG0593 108 flAGKEATQEEFFHTFNALR----EAGKQIVLTSDRP----PKEL-PGLEERlrsrlewglVVDIQPPDLETRIAILrkK 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17563248 359 IHAKQMSVERDIrYDLLARLCPNStGAEIRSVCTEAGMFAIRARRKV----ATE--KDFLEAINKVV 419
Cdd:COG0593 179 AADRGLELPDEV-LEYLARRIERN-VRELEGALNRLDAYALLTGRPItlelAREvlKDLLRAQKKEI 243
Sigma54_activat pfam00158
Sigma-54 interaction domain;
214-279 1.93e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 38.92  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   214 VLLYGPPGTGKTLCARAV---ANRTDACFIRV---------IGSEL--VQKyvG--EGARMVRE-LFEMAR--TkkaclI 274
Cdd:pfam00158  25 VLITGESGTGKELFARAIhqlSPRADGPFVAVncaaipeelLESELfgHEK--GafTGADSDRKgLFELADggT-----L 97

                  ....*
gi 17563248   275 FFDEI 279
Cdd:pfam00158  98 FLDEI 102
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
214-379 2.33e-03

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 39.95  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 214 VLLYGPPGTGKTLCARAV---ANRTDACFIRV---------IGSEL--VQKYVGEGARMVRE-LFEMARTkkaCLIFFDE 278
Cdd:COG2204 157 VLITGESGTGKELVARAIhrlSPRADGPFVAVncaaipeelLESELfgHEKGAFTGAVARRIgKFELADG---GTLFLDE 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 279 IDAVggarfddgqggDNEVQRTMLELInQLDGFDPRG-------NIKVLMATNRPdtLDpALMRPGRLDRK-------VE 344
Cdd:COG2204 234 IGEM-----------PLALQAKLLRVL-QEREFERVGgnkpipvDVRVIAATNRD--LE-ELVEEGRFREDlyyrlnvFP 298
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 17563248 345 FALPDLAGR--------AHILKIHAKQMSVERDIRYDLLARLC 379
Cdd:COG2204 299 IELPPLRERredipllaRHFLARFAAELGKPVKLSPEALEALL 341
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
209-233 3.45e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 3.45e-03
                          10        20
                  ....*....|....*....|....*
gi 17563248   209 EPPKGVLLYGPPGTGKTLCARAVAN 233
Cdd:pfam05496  31 EALDHVLLYGPPGLGKTTLANIIAN 55
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
187-232 3.86e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 39.37  E-value: 3.86e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17563248 187 EKLREVVETPLlhpERYVNLgIEPPKGVLLYGPPGTGKTLCARAVA 232
Cdd:COG1401 201 DLLREKFEETL---EAFLAA-LKTKKNVILAGPPGTGKTYLARRLA 242
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
212-247 4.03e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.18  E-value: 4.03e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17563248 212 KGVLLYGPPGTGKTLCARAVANR--TDACFIRVIGSEL 247
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
214-280 5.04e-03

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 38.39  E-value: 5.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 214 VLLYGPPGTGKTLCARAVANRT-DACFIRVIGS----ELVQKYVGE-GARM----VRELFEMARTK-KAC--LIFFDEID 280
Cdd:COG2842  53 GVVYGESGVGKTTAAREYANRNpNVIYVTASPSwtskELLEELAEElGIPAppgtIADLRDRILERlAGTgrLLIIDEAD 132
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
207-278 5.08e-03

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 38.62  E-value: 5.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248 207 GIEPPKG-VLLYGPPGTGKTLCARAVANR----TDACFI-----------RVIGSELVQKYVGEG-----ARMVRELFEM 265
Cdd:COG3267  38 ALAQGGGfVVLTGEVGTGKTTLLRRLLERlpddVKVAYIpnpqlspaellRAIADELGLEPKGASkadllRQLQEFLLEL 117
                        90
                ....*....|...
gi 17563248 266 ARTKKACLIFFDE 278
Cdd:COG3267 118 AAAGRRVVLIIDE 130
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
214-268 5.56e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.59  E-value: 5.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17563248 214 VLLYGPPGTGKTLCARAVANRTDACFIR--VIGSELVQKYVGEGARMV-------RELFEMART 268
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLFGAGLAPLERSPeatartyARLLALARE 65
PRK08116 PRK08116
hypothetical protein; Validated
213-233 6.07e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.46  E-value: 6.07e-03
                         10        20
                 ....*....|....*....|.
gi 17563248  213 GVLLYGPPGTGKTLCARAVAN 233
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIAN 136
AAA_22 pfam13401
AAA domain;
214-287 6.39e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.55  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248   214 VLLYGPPGTGKTLCARAVANRTDAC-----------------FIRVIGSELVQKYVGEG-ARMVRELFE--MARTKKACL 273
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPEVrdsvvfvdlpsgtspkdLLRALLRALGLPLSGRLsKEELLAALQqlLLALAVAVV 87
                          90
                  ....*....|....
gi 17563248   274 IFFDEIDAVGGARF 287
Cdd:pfam13401  88 LIIDEAQHLSLEAL 101
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
214-308 6.52e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 37.84  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  214 VLLYGPPGTGKT-----LCARAVANRTDACFIRVigSELVQKYvgEGARMVRELFEMART-KKACLIFFDEIdavGGARF 287
Cdd:NF038214  93 VLLLGPPGTGKThlaiaLGYAACRQGYRVRFTTA--ADLVEQL--AQARADGRLGRLLRRlARYDLLIIDEL---GYLPF 165
                         90       100
                 ....*....|....*....|.
gi 17563248  288 DDGQGGDnevqrtMLELINQL 308
Cdd:NF038214 166 SREGANL------LFELIADR 180
44 PHA02544
clamp loader, small subunit; Provisional
215-364 6.53e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.43  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  215 LLYGP-PGTGKTLCARAVANRTDACFIRVIGS----ELVQKYVGEGARmvrelfEMARTKKACLIFFDEIDAVGGArfdd 289
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFAS------TVSLTGGGKVIIIDEFDRLGLA---- 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17563248  290 gqggdnEVQRTMLELINQLDgfdprGNIKVLMATNRPDTLDPALMrpGRLdRKVEFALPDLAGRAHIlkihAKQM 364
Cdd:PHA02544 116 ------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEM----MKQM 172
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
211-234 7.88e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 38.03  E-value: 7.88e-03
                        10        20
                ....*....|....*....|....
gi 17563248 211 PKGVLLYGPPGTGKTLCARAVANR 234
Cdd:COG0470  18 PHALLLHGPPGIGKTTLALALARD 41
cdc6 PRK00411
ORC1-type DNA replication protein;
184-280 9.01e-03

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 38.29  E-value: 9.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17563248  184 DQIEKLREVVEtPLLHPERYVNlgieppkgVLLYGPPGTGKTLCARAVA----NRTDAC-FIRV----------IGSELV 248
Cdd:PRK00411  37 EQIEELAFALR-PALRGSRPLN--------VLIYGPPGTGKTTTVKKVFeeleEIAVKVvYVYIncqidrtryaIFSEIA 107
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 17563248  249 QKYVGEGARMV----RELFEM-----ARTKKACLIFFDEID 280
Cdd:PRK00411 108 RQLFGHPPPSSglsfDELFDKiaeylDERDRVLIVALDDIN 148
 
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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