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Conserved domains on  [gi|17137738|ref|NP_477473|]
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regulatory particle triple-A ATPase 1 [Drosophila melanogaster]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
 88-430 4.07e-158

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 451.59  E-value: 4.07e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   88 QNEQ----PLQVARCTKIInadsDDPKYIinVKQFA--KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTV 161
Cdd:PRK03992  44 ELEKlkspPLIVATVLEVL----DDGRVV--VKSSGgpQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  162 TMMQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVI 241
Cdd:PRK03992 118 QAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  242 GSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMAT 321
Cdd:PRK03992 198 GSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAAT 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  322 NRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARR 401
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDR 357

                        330       340       350
                 ....*....|....*....|....*....|
gi 17137738  402 KVATEKDFLEAVKKVI-KSYAKFSATPRYM 430
Cdd:PRK03992 358 TEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 88-430 4.07e-158

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 451.59  E-value: 4.07e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   88 QNEQ----PLQVARCTKIInadsDDPKYIinVKQFA--KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTV 161
Cdd:PRK03992  44 ELEKlkspPLIVATVLEVL----DDGRVV--VKSSGgpQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  162 TMMQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVI 241
Cdd:PRK03992 118 QAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  242 GSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMAT 321
Cdd:PRK03992 198 GSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAAT 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  322 NRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARR 401
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDR 357

                        330       340       350
                 ....*....|....*....|....*....|
gi 17137738  402 KVATEKDFLEAVKKVI-KSYAKFSATPRYM 430
Cdd:PRK03992 358 TEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 92-417 4.38e-134

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: 389.93  E-value: 4.38e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738    92 PLQVARCTKIInadsDDPKYIINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEDKPD 171
Cdd:TIGR01242  43 PLIVGTVLEVL----DDNRVVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   172 VTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVG 251
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   252 EGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPAL 331
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   332 MRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLE 411
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358


                  ....*.
gi 17137738   412 AVKKVI 417
Cdd:TIGR01242 359 AVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 164-419 4.63e-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: 4.63e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 164 MQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGS 243
Cdd:COG1222  67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 244 ELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGdnEVQRTMLELINQLDGFDPRGNIKVLMATNR 323
Cdd:COG1222 147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 324 PDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 403
Cdd:COG1222 225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                       250
                ....*....|....*.
gi 17137738 404 ATEKDFLEAVKKVIKS 419
Cdd:COG1222 305 VTMEDLEKAIEKVKKK 320
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 173-343 6.63e-124

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: 356.26  E-value: 6.63e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 173 TYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGE 252
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 253 GARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALM 332
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 17137738 333 RPGRLDRKVEF 343
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 212-345 1.67e-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: 167.00  E-value: 1.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   212 VLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDdgaGG 291
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17137738   292 DNEVQRTMLELINQLDGFDPR-GNIKVLMATNRPDTLDPALMrpGRLDRKVEFGL 345
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 208-347 1.18e-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: 85.12  E-value: 1.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738    208 PPKGVLLFGPPGTGKTLCARAVAN---RTDACFIRVIGSEL--------------VQKYVGEGARMVRELFEMARSKKAC 270
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137738    271 LIFFDEIDAIGGARFddgaggdnEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPgRLDRKVEFGLPD 347
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 ...
 212-362 7.74e-04

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: 40.92  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  212 VLLFGPPGTGKT-----LCARAVANRTDACFIRVigSELVQKYV---GEGaRMVRELFEMARSKkaCLIffdeIDAIGGA 283
Cdd:NF038214  93 VLLLGPPGTGKThlaiaLGYAACRQGYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLARYD--LLI----IDELGYL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  284 RFDDGAGGDnevqrtMLELINQLDGfdpRGNIkvLMATNRP----------DTLDPALmrpgrLDRKVEfglpdqdgRSH 353
Cdd:NF038214 164 PFSREGANL------LFELIADRYE---RGST--IITSNLPfsewgevfgdPTLAAAI-----LDRLVH--------HAH 219


                 ....*....
gi 17137738  354 IFKIHARSM 362
Cdd:NF038214 220 ILELKGESY 228
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 88-430 4.07e-158

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 451.59  E-value: 4.07e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   88 QNEQ----PLQVARCTKIInadsDDPKYIinVKQFA--KFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTV 161
Cdd:PRK03992  44 ELEKlkspPLIVATVLEVL----DDGRVV--VKSSGgpQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  162 TMMQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVI 241
Cdd:PRK03992 118 QAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVV 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  242 GSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMAT 321
Cdd:PRK03992 198 GSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAAT 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  322 NRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARR 401
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDR 357

                        330       340       350
                 ....*....|....*....|....*....|
gi 17137738  402 KVATEKDFLEAVKKVI-KSYAKFSATPRYM 430
Cdd:PRK03992 358 TEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 92-417 4.38e-134

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: 389.93  E-value: 4.38e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738    92 PLQVARCTKIInadsDDPKYIINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEDKPD 171
Cdd:TIGR01242  43 PLIVGTVLEVL----DDNRVVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   172 VTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVG 251
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   252 EGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPAL 331
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   332 MRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLE 411
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358


                  ....*.
gi 17137738   412 AVKKVI 417
Cdd:TIGR01242 359 AVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 164-419 4.63e-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: 4.63e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 164 MQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGS 243
Cdd:COG1222  67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 244 ELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGdnEVQRTMLELINQLDGFDPRGNIKVLMATNR 323
Cdd:COG1222 147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 324 PDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 403
Cdd:COG1222 225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                       250
                ....*....|....*.
gi 17137738 404 ATEKDFLEAVKKVIKS 419
Cdd:COG1222 305 VTMEDLEKAIEKVKKK 320
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 173-343 6.63e-124

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: 356.26  E-value: 6.63e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 173 TYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGE 252
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 253 GARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALM 332
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 17137738 333 RPGRLDRKVEF 343
Cdd:cd19502 161 RPGRFDRKIEF 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 92-418 1.18e-113

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 339.05  E-value: 1.18e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   92 PLQVARCTKIINADSDdpkyIINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEDKPD 171
Cdd:PTZ00454  66 PLVIGQFLEMIDSNYG----IVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  172 VTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVG 251
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  252 EGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPAL 331
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  332 MRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRF-DLLARlcPNS-TGAEIRSVCTEAGMFAIRARRKVATEKDF 409
Cdd:PTZ00454 302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLeDFVSR--PEKiSAADIAAICQEAGMQAVRKNRYVILPKDF 379


                 ....*....
gi 17137738  410 LEAVKKVIK 418
Cdd:PTZ00454 380 EKGYKTVVR 388
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 92-427 7.47e-112

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 335.59  E-value: 7.47e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   92 PLQVARCTKIInadsDDPKYIINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEDKPD 171
Cdd:PTZ00361 104 PLSVGTLEEII----DENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  172 VTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVG 251
Cdd:PTZ00361 180 ESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  252 EGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPAL 331
Cdd:PTZ00361 260 DGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  332 MRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLE 411
Cdd:PTZ00361 340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRK 419

                        330
                 ....*....|....*.
gi 17137738  412 AVKKVIksYAKFSATP 427
Cdd:PTZ00361 420 AKEKVL--YRKKGNIP 433
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 164-417 1.35e-87

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 275.32  E-value: 1.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   164 MQVEDKPDVTYSDVGGCKEQIEKLREVVETpLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGS 243
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   244 ELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNR 323
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   324 PDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 403
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....
gi 17137738   404 ATEKDFLEAVKKVI 417
Cdd:TIGR01241 283 ITMNDIEEAIDRVI 296
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
164-417 4.06e-86

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 273.84  E-value: 4.06e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 164 MQVEDKPDVTYSDVGGCKEQIEKLREVVETpLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGS 243
Cdd:COG0465 131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 244 ELVQKYVGEGARMVRELFEMARsKKA-CLIFFDEIDAIGGARfddGA---GGDNEVQRTmlelINQL----DGFDPRGNI 315
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAK-KNApCIIFIDEIDAVGRQR---GAglgGGHDEREQT----LNQLlvemDGFEGNEGV 281

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 316 KVLMATNRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMF 395
Cdd:COG0465 282 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALL 361

                       250       260
                ....*....|....*....|..
gi 17137738 396 AIRARRKVATEKDFLEAVKKVI 417
Cdd:COG0465 362 AARRNKKAVTMEDFEEAIDRVI 383
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 174-416 3.58e-76

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: 242.51  E-value: 3.58e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 174 YSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEG 253
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 254 ARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLElinQLDGFdpRGNIKVLMATNRPDTLDPALMR 333
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLT---EMEEL--RSDVVVIAATNRPDLLDPALLR 310

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 334 pgRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEAV 413
Cdd:COG0464 311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388


                ...
gi 17137738 414 KKV 416
Cdd:COG0464 389 ERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 157-423 7.74e-76

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: 250.59  E-value: 7.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   157 IDPTVTMMQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDAC 236
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGAN 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   237 FIRVIGSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARfddGAGGDNEV-QRTMLELINQLDGFDPRGNI 315
Cdd:TIGR01243 515 FIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR---GARFDTSVtDRIVNQLLTEMDGIQELSNV 591

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   316 KVLMATNRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMF 395
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMA 671

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 17137738   396 AIRARRK------------------VATEKDFLEAVKKVIKSYAKF 423
Cdd:TIGR01243 672 ALRESIGspakeklevgeeeflkdlKVEMRHFLEALKKVKPSVSKE 717
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 170-416 1.41e-72

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 242.12  E-value: 1.41e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   170 PDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKY 249
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   250 VGEGARMVRELFEMARSKKACLIFFDEIDAIGGARfdDGAGGDNEvQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDP 329
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   330 ALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIR----------- 398
Cdd:TIGR01243 330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRrfiregkinfe 409

                         250       260
                  ....*....|....*....|....*.
gi 17137738   399 ---ARRKV-----ATEKDFLEAVKKV 416
Cdd:TIGR01243 410 aeeIPAEVlkelkVTMKDFMEALKMV 435
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 172-341 2.82e-71

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: 222.11  E-value: 2.82e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 172 VTYSDVGGCKEQIEKLREVVETpLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVG 251
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 252 EGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPAL 331
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159

                       170
                ....*....|
gi 17137738 332 MRPGRLDRKV 341
Cdd:cd19501 160 LRPGRFDRQV 169
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
164-417 5.46e-70

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 233.39  E-value: 5.46e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  164 MQVEDKPDVTYSDVGGCKEQIEKLREVVETpLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGS 243
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  244 ELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNR 323
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  324 PDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 403
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379

                        250
                 ....*....|....
gi 17137738  404 ATEKDFLEAVKKVI 417
Cdd:PRK10733 380 VSMVEFEKAKDKIM 393
ftsH CHL00176
cell division protein; Validated
 165-417 1.94e-69

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 231.48  E-value: 1.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  165 QVEDKPDVTYSDVGGCKEQIEKLREVVeTPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSE 244
Cdd:CHL00176 173 QMEADTGITFRDIAGIEEAKEEFEEVV-SFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  245 LVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARfDDGAGGDN-EVQRTMLELINQLDGFDPRGNIKVLMATNR 323
Cdd:CHL00176 252 FVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQR-GAGIGGGNdEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  324 PDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKV 403
Cdd:CHL00176 331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKAT 410

                        250
                 ....*....|....
gi 17137738  404 ATEKDFLEAVKKVI 417
Cdd:CHL00176 411 ITMKEIDTAIDRVI 424
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 176-343 5.45e-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: 213.31  E-value: 5.45e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 255
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 256 MVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELinqLDGFDPRGNIKVLMATNRPDTLDPALMRPG 335
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTL---MDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                ....*...
gi 17137738 336 RLDRKVEF 343
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 ...
 185-339 1.64e-65

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 206.75  E-value: 1.64e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 185 EKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 264
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137738 265 RSKKACLIFFDEIDAIGGARFDDGAGGDNEvqRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDR 339
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 ...
 176-344 1.47e-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: 194.19  E-value: 1.47e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 255
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 256 MVRELFEMARSKKACLIFFDEIDAIGGARFDdgagGDNEVQRTML-ELINQLDGFDPRGNIKVLMATNRPDTLDPALMRP 334
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIVsQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                       170
                ....*....|
gi 17137738 335 GRLDRKVEFG 344
Cdd:cd19519 157 GRFDREIDIG 166
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 185-341 1.37e-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: 191.55  E-value: 1.37e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 185 EKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 264
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17137738 265 RSKKACLIFFDEIDAIGGARfddGAGGDNEV-QRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKV 341
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 ...
 183-343 3.34e-58

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 187.88  E-value: 3.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 183 QIEKLREVVETPLLHPEKFvNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFE 262
Cdd:cd19481   1 LKASLREAVEAPRRGSRLR-RYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 263 MARSKKACLIFFDEIDAIGGARfdDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVE 342
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                .
gi 17137738 343 F 343
Cdd:cd19481 158 F 158
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 79-358 2.00e-57

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: 196.85  E-value: 2.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738    79 DLAADKQILQNEQPLQVARCT-------KIINADSDDPKYIINVKQFAKFVVDLADSVAPTDIEEGMRVGVDRnKYQIHI 151
Cdd:TIGR03689  82 ELVPGQTVRLNEALQVVEACDfertgeiVTLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDP-RAGYAF 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   152 PLPPKIDptVTMMQVEDKPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVAN 231
Cdd:TIGR03689 161 EAIPRTE--VEDLVLEEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAN 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   232 ----------RTDACFIRVIGSELVQKYVGEGARMVRELFEMARSKKA----CLIFFDEIDAIGGARfddGAGGDNEVQR 297
Cdd:TIGR03689 239 slaarigaegGGKSYFLNIKGPELLNKYVGETERQIRLIFQRAREKASegrpVIVFFDEMDSLFRTR---GSGVSSDVET 315

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17137738   298 TML-ELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEFGLPDQDGRSHIFKIH 358
Cdd:TIGR03689 316 TVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY 377
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 185-341 1.88e-54

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 178.47  E-value: 1.88e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 185 EKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 264
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137738 265 RSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKV 341
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
175-423 8.65e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.00  E-value: 8.65e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 175 SDVGGCKEQIEKLREVVE--TPLLHPEKFvnlGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGE 252
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIKelRRRENLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 253 GARMVRELFEMARSKKaCLIFFDEIDAIGGARFDDGAGGdnEVQRTMLELINQLDGFdpRGNIKVLMATNRPDTLDPALM 332
Cdd:COG1223  79 TARNLRKLFDFARRAP-CVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALW 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 333 RpgRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLEA 412
Cdd:COG1223 154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231

                       250
                ....*....|.
gi 17137738 413 VKKVIKSYAKF 423
Cdd:COG1223 232 LKQRKERKKEP 242
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 212-345 1.67e-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: 167.00  E-value: 1.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   212 VLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDdgaGG 291
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17137738   292 DNEVQRTMLELINQLDGFDPR-GNIKVLMATNRPDTLDPALMrpGRLDRKVEFGL 345
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 185-339 1.14e-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: 1.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 185 EKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMA 264
Cdd:cd19530   6 EELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRA 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137738 265 RSKKACLIFFDEIDAIGGARFDDGAGGdneVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDR 339
Cdd:cd19530  86 RASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 176-343 4.35e-48

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 162.29  E-value: 4.35e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVAN------RTDACFIRViGSELVQKY 249
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAecskggQKVSFFMRK-GADCLSKW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 250 VGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELinqLDGFDPRGNIKVLMATNRPDTLDP 329
Cdd:cd19517  80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDP 156

                       170
                ....*....|....
gi 17137738 330 ALMRPGRLDRKVEF 343
Cdd:cd19517 157 ALRRPGRFDREFYF 170
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 176-341 1.13e-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: 155.64  E-value: 1.13e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 255
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 256 MVRELFEMARSKKACLIFFDEIDAIGGARfdDGAGGDNEvQRTMLELINQLDGF----DPRGNIKVLMATNRPDTLDPAL 331
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157

                       170
                ....*....|
gi 17137738 332 MRPGRLDRKV 341
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 177-341 1.84e-45

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 154.82  E-value: 1.84e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 177 VGGCKEQIEKLREVVETPLLHPEKFVNLgIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARM 256
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 257 VRELFEMARSKKACLIFFDEIDAIGGARfddgAGGDNEVQRTM-LELINQLDGF--DPRGNIKVLMATNRPDTLDPALMR 333
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSER----GSGEHEASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155


                ....*...
gi 17137738 334 pgRLDRKV 341
Cdd:cd19509 156 --RFEKRI 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 187-342 2.66e-43

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: 149.12  E-value: 2.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 187 LREVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARS 266
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137738 267 KKACLIFFDEIDAIGGARFDDGAGgdnEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVE 342
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 ...
 189-339 4.17e-42

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 146.12  E-value: 4.17e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 189 EVVETPLLHPEKFvNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFEMARSKK 268
Cdd:cd19527   7 DTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAK 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17137738 269 ACLIFFDEIDAIGGARfddGAGGDNE--VQRTMLELINQLDGF-DPRGNIKVLMATNRPDTLDPALMRPGRLDR 339
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; ...
 170-333 2.17e-39

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 139.74  E-value: 2.17e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 170 PDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNLGiEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKY 249
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 250 VGEGARMVRELFEMARSKKACLIFFDEIDAIGGARfddGAGGDNEVQRTMLELINQLDGFD--PRGNIKVLMATNRPDTL 327
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEI 172


                ....*.
gi 17137738 328 DPALMR 333
Cdd:cd19525 173 DEAARR 178
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 169-341 3.08e-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: 136.15  E-value: 3.08e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 169 KPDVTYSDVGGCKEQIEKLREVVETPLLHPEKFVNlGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQK 248
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 249 YVGEGARMVRELFEMARSKKACLIFFDEIDAIGGARFDdgagGDNE-VQRTMLELINQLDGF--DPRGnIKVLMATNRPD 325
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEaSRRIKTELLVQMNGVgnDSQG-VLVLGATNIPW 154

                       170
                ....*....|....*.
gi 17137738 326 TLDPALMRpgRLDRKV 341
Cdd:cd19521 155 QLDSAIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 176-333 6.20e-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: 132.55  E-value: 6.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLGI-EPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGA 254
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 255 RMVRELFEMARSKKACLIFFDEIDAIGGARfddgAGGDNEVQRTM-LELINQLDGFDPRGNIKVLM--ATNRPDTLDPAL 331
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156


                ..
gi 17137738 332 MR 333
Cdd:cd19520 157 LR 158
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 176-341 1.18e-36

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: 132.03  E-value: 1.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVnlGIEPP-KGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGA 254
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 255 RMVRELFEMARSKKACLIFFDEIDAIGGARfddGAGGDNEV-QRTMLELINQLDGF-------DPRGNIKVLMATNRPDT 326
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155

                       170
                ....*....|....*
gi 17137738 327 LDPALMRpgRLDRKV 341
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 176-341 2.49e-33

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: 123.04  E-value: 2.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLGiEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 255
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 256 MVRELFEMARSKKACLIFFDEIDAIGGARFDdgagGDNEVQRTM-LELINQLDGFDPRGNIKVLM--ATNRPDTLDPALM 332
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVL 155


                ....*....
gi 17137738 333 RpgRLDRKV 341
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; ...
 177-342 1.85e-30

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 115.66  E-value: 1.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 177 VGGCKEQIEKL-REVVETPLLHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVI-GSELVQKYVGEGA 254
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 255 RMVRELFEMA-RSKKAC-------LIFFDEIDAI---GGARFDDGAGGDNEVQrtmlELINQLDGFDPRGNIKVLMATNR 323
Cdd:cd19504  82 ANIRKLFADAeEEQRRLgansglhIIIFDEIDAIckqRGSMAGSTGVHDTVVN----QLLSKIDGVEQLNNILVIGMTNR 157

                       170
                ....*....|....*....
gi 17137738 324 PDTLDPALMRPGRLDRKVE 342
Cdd:cd19504 158 KDLIDEALLRPGRLEVQME 176
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 176-333 1.82e-27

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: 107.28  E-value: 1.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGCKEQIEKLREVVETPLLHPEKFVNLgIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEGAR 255
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 256 MVRELFEMARSKKACLIFFDEIDAIGGARFDdgagGDNEVQRTMLELINQLDGF--DPRGNIKVLMATNRPDTLDPALMR 333
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 178-345 2.53e-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: 103.77  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 178 GGCKEQIEKLREVVETPllhpekfvnlgiePPKGVLLFGPPGTGKTLCARAVAN---RTDACFIRVIGSELVQKYVGEGA 254
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAEL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 255 R---MVRELFEMARSKKACLIFFDEIDAIGgarfddgaggdNEVQRTMLELINQL-DGFDPRGNIKVLMATNRPDTLDPA 330
Cdd:cd00009  68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                       170
                ....*....|....*
gi 17137738 331 LMRPGRLDRKVEFGL 345
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
 170-417 7.98e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 100.48  E-value: 7.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  170 PDVTYSDVGGCKEQIEKLREVVETpllHPEKFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKY 249
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLKKRSTS---FSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  250 VGEGARMVRELFEMARSKKACLIFFDEID-AIGGARFDDGAGGDNEVQRTMLELINQLDGFdprgnIKVLMATNRPDTLD 328
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEKKSP-----VFVVATANNIDLLP 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  329 PALMRPGRLDRKVEFGLPDQDGRSHIFKIHARSMSVERDIRFD--LLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATE 406
Cdd:CHL00195 375 LEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDikKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTD 454

                        250
                 ....*....|.
gi 17137738  407 kDFLEAVKKVI 417
Cdd:CHL00195 455 -DILLALKQFI 464
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 208-347 1.18e-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: 85.12  E-value: 1.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738    208 PPKGVLLFGPPGTGKTLCARAVAN---RTDACFIRVIGSEL--------------VQKYVGEGARMVRELFEMARSKKAC 270
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137738    271 LIFFDEIDAIGGARFddgaggdnEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPgRLDRKVEFGLPD 347
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 ...
 176-339 5.34e-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: 5.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 176 DVGGckeqIEKLREVVE--TPLLHPEKFvNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQKYVGEG 253
Cdd:cd19507   1 DVGG----LDNLKDWLKkrKAAFSKQAS-AYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 254 ARMVRELFEMARSKKACLIFFDEID-AIGGARFDDGAGGDNEVQRTMLELINQldgfdpRGNIKVLMAT-NRPDTLDPAL 331
Cdd:cd19507  76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE------KKKPVFVVATaNNVQSLPPEL 149


                ....*...
gi 17137738 332 MRPGRLDR 339
Cdd:cd19507 150 LRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 203-343 2.99e-13

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: 66.99  E-value: 2.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 203 NLGIEPPKGVLLFGPPGTGKTLCARAVAN--RTDACFIrvigsELVQkyVGEGARMVRELfeMARSKKACLIFFDEIDA- 279
Cdd:cd19510  17 DRGIPYRRGYLLYGPPGTGKSSFIAALAGelDYDICDL-----NLSE--VVLTDDRLNHL--LNTAPKQSIILLEDIDAa 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137738 280 --IGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKVEF 343
Cdd:cd19510  88 feSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 210-343 1.99e-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: 58.69  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 210 KGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSElVQKYVGEGARMVRELFEMA-RSKKACLIFFDEIDAIGGARFDDG 288
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17137738 289 AggdNEVQRTMLELINQLDGfDPRGNIKVLMATNRPDTLDPALMrpGRLDRKVEF 343
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 ...
 185-331 4.25e-10

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 59.00  E-value: 4.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 185 EKLREVVETPLLHPEKFVNLG-IEPPKGVLLFGPPGTGKTLCARAVANRTD---------ACFIRVIGSELVQKYVGEGA 254
Cdd:cd19508  27 SRLLDYVTTTLLFSDKNVNTNlITWNRLVLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESG 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 255 RMVRELF----EMARSKKaCLIF--FDEIDAIGGARFDDGAGGD-NEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTL 327
Cdd:cd19508 107 KLVTKMFqkiqELIDDKD-ALVFvlIDEVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKI 185


                ....
gi 17137738 328 DPAL 331
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 ...
 367-411 1.42e-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: 53.31  E-value: 1.42e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17137738   367 DIRFDLLARLCPNSTGAEIRSVCTEAGMFAIRARRKVATEKDFLE 411
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 209-303 1.08e-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: 54.69  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 209 PKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQ-KYVGEGAR-MVRELFEmarskkaCLIFFDEIDAIggARFD 286
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGRDVEsIIRDLVE-------GIVFIDEIDKI--AKRG 116

                        90       100
                ....*....|....*....|
gi 17137738 287 DGAGGD---NEVQRTMLELI 303
Cdd:cd19498 117 GSSGPDvsrEGVQRDLLPIV 136
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 204-339 2.83e-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: 52.76  E-value: 2.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 204 LGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQK--------------YVGEGARMVRELFEMARSKKA 269
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMSP 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17137738 270 CLIFFDEIDAIGGARFDDGAGGDNevqRTMLELINQLDGFDPRG----NIKVLMATNRPDTLDPALMRPGRLDR 339
Cdd:cd19505  87 CIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKsstrNILVIASTHIPQKVDPALIAPNRLDT 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
 173-284 1.43e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 53.39  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  173 TYSDVGGCKEQIEKLREVVETpLLHPEkfvnlgiePPKGVLLFGPPGTGKTLCARAVANRtdacfirvIGSELV------ 246
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIES-WLKGK--------PKKALLLYGPPGVGKTSLAHALAND--------YGWEVIelnasd 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17137738  247 -------QKYVGEGARMvRELFEMARSkkacLIFFDEIDAI------GGAR 284
Cdd:PRK04195  75 qrtadviERVAGEAATS-GSLFGARRK----LILLDEVDGIhgnedrGGAR 120
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 212-277 4.26e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 51.62  E-value: 4.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137738  212 VLLFGPPGTGKTLCARAVANRTDACFIR---VIGSelvqkyVGEgarmVRELFEMARSKKA----CLIFFDEI 277
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAlsaVTSG------VKD----LREVIEEARQRRSagrrTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 212-277 7.15e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.21  E-value: 7.15e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 212 VLLFGPPGTGKTLCARAVANRTDACFIRVIGselvqkyVGEGARMVRELFEMARSKKA----CLIFFDEI 277
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRAygrrTILFVDEI 114
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 181-375 2.60e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 49.46  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   181 KEQIEKLREVVETPLLHPEKfvnlGIEPP---KGVLLFGPPGTGKTLCARAVANR-------TDACFIRVIGSELVQKYV 250
Cdd:TIGR03922 285 KRQVAALKSSTAMALARAER----GLPVAqtsNHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYI 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   251 GEGARMVRELFEMARSKkacLIFFDEIDAIGGARfdDGAGGDnevqrTMLELINQLDGF--DPRGNIKVLMATNRPD--- 325
Cdd:TIGR03922 361 GESEAKTNEIIDSALGG---VLFLDEAYTLVETG--YGQKDP-----FGLEAIDTLLARmeNDRDRLVVIGAGYRKDldk 430

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17137738   326 --TLDPALMRpgRLDRKVEFglpDQDGRSHIFKIhARSMSVERDIRFDLLAR 375
Cdd:TIGR03922 431 flEVNEGLRS--RFTRVIEF---PSYSPDELVEI-ARRMATERDSVLDDAAA 476
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 209-303 5.24e-06

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: 46.42  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   209 PKGVLLF-GPPGTGKTLCARAVANR---TDACFIRVIGSELVQK------------YVG--EGArmvrELFEMARSKKAC 270
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEhsvsrligappgYVGyeEGG----QLTEAVRRKPYS 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17137738   271 LIFFDEIDAIggarfddgaggDNEVQRTMLELI 303
Cdd:pfam07724  78 IVLIDEIEKA-----------HPGVQNDLLQIL 99
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 202-336 1.25e-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: 44.93  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 202 VNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVI--GSELVQKYVGEGARMV----------RELFEMARS--K 267
Cdd:cd00267  18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILidGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllL 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17137738 268 KACLIFFDEIDaiggarfddgAGGDNEVQRTMLELINQLdgfdPRGNIKVLMATNRPDTLDPA-----LMRPGR 336
Cdd:cd00267  98 NPDLLLLDEPT----------SGLDPASRERLLELLREL----AEEGRTVIIVTHDPELAELAadrviVLKDGK 157
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
182-287 2.08e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 46.38  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 182 EQIEKLREVVEtPLLHPEkfvnlgiePPKGVLLFGPPGTGKTLCARAVANR---------TDACFIRV----------IG 242
Cdd:COG1474  33 EEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrVL 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17137738 243 SELVQKyVGEGARMVR------ELFEM-----ARSKKACLIFFDEIDAIGGARFDD 287
Cdd:COG1474 104 SRILEE-LGSGEDIPStglstdELFDRlyealDERDGVLVVVLDEIDYLVDDEGDD 158
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 211-333 3.28e-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: 43.44  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   211 GVLLFGPPGTGKTLCARAVANRTDAC--FIRVIG-----SELVQKYV--GEGARMV-RELFEMARskKACLIFFDEIDAI 280
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRpvFYVQLTrdtteEDLFGRRNidPGGASWVdGPLVRAAR--EGEIAVLDEINRA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137738   281 GGarfddgaggdnEVQRTMLELIN-----QLDGF----DPRGNIKVLMATNRPDT----LDPALMR 333
Cdd:pfam07728  79 NP-----------DVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 209-343 3.40e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.09  E-value: 3.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 209 PKGVLLF-GPPGTGKTLCARAVA---NRTDACFIRVIGSELVQK------------YVGEGARMVreLFEMARSKKACLI 272
Cdd:cd19499  40 PIGSFLFlGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGGQ--LTEAVRRKPYSVV 117

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137738 273 FFDEIDAiggarfddgagGDNEVQRTMLELINqlDGF--DPRG------NIKVLMATNrpdTLDPALMrpGRLDRKVEF 343
Cdd:cd19499 118 LLDEIEK-----------AHPDVQNLLLQVLD--DGRltDSHGrtvdfkNTIIIMTSN---HFRPEFL--NRIDEIVVF 178
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 195-281 1.02e-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: 43.74  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 195 LLHPEKFVNLGIEPPKG-VLLFGPPGTGKTLCARAVANRTDACFIRVIGSELVQK-YVGEGAR--MVREL----FEMARS 266
Cdd:cd19497  35 IRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGEDVEniLLKLLqaadYDVERA 114

                        90
                ....*....|....*
gi 17137738 267 KKAcLIFFDEIDAIG 281
Cdd:cd19497 115 QRG-IVYIDEIDKIA 128
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
206-306 2.33e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.46  E-value: 2.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 206 IEPPKGVLLFGPPGTGKTLCARAVANRtdAC-------FIRVigSELVQKYvgEGARMVRELFEMARS-KKA-CLIffde 276
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALGHE--ACragyrvrFTTA--PDLVNEL--KEARADGRLERLLKRlAKVdLLI---- 165

                        90       100       110
                ....*....|....*....|....*....|
gi 17137738 277 IDAIGGARFDDGAGGDnevqrtMLELINQL 306
Cdd:COG1484 166 LDELGYLPLDAEGAEL------LFELISDR 189
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 212-278 4.83e-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: 41.69  E-value: 4.83e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137738 212 VLLFGPPGTGKTLCARAVANRTDACFIRVIGSE--LVQKYVGEgarmvrELFEMARSKK--------ACLIFFDEID 278
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFTPdlLPSDILGT------YIYDQQTGEFefrpgplfANVLLADEIN 104
44 PHA02544
clamp loader, small subunit; Provisional
 200-356 7.10e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 41.51  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  200 KFVNLGiEPPKGVLLFGPPGTGKTLCARAVANRTDACFIRVIGS----ELVQKYVGEGARmvrelfEMARSKKACLIFFD 275
Cdd:PHA02544  35 SIVKKG-RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFAS------TVSLTGGGKVIIID 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  276 EIDAIGGArfddgaggdnEVQRTMLELINQLDgfdprGNIKVLMATNRPDTLDPALMrpGRLdRKVEFGLPDQDGRSHIF 355
Cdd:PHA02544 108 EFDRLGLA----------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMM 169


                 .
gi 17137738  356 K 356
Cdd:PHA02544 170 K 170
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 212-362 7.74e-04

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: 40.92  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  212 VLLFGPPGTGKT-----LCARAVANRTDACFIRVigSELVQKYV---GEGaRMVRELFEMARSKkaCLIffdeIDAIGGA 283
Cdd:NF038214  93 VLLLGPPGTGKThlaiaLGYAACRQGYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLARYD--LLI----IDELGYL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  284 RFDDGAGGDnevqrtMLELINQLDGfdpRGNIkvLMATNRP----------DTLDPALmrpgrLDRKVEfglpdqdgRSH 353
Cdd:NF038214 164 PFSREGANL------LFELIADRYE---RGST--IITSNLPfsewgevfgdPTLAAAI-----LDRLVH--------HAH 219


                 ....*....
gi 17137738  354 IFKIHARSM 362
Cdd:NF038214 220 ILELKGESY 228
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
212-265 1.60e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.13  E-value: 1.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137738 212 VLLFGPPGTGKTLCARAVANRTDACFIR--VIGSELVQKYVGEGARMV-------RELFEMAR 265
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLFGAGLAPLERSPeatartyARLLALAR 64
PRK13341 PRK13341
AAA family ATPase;
213-277 2.00e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.42  E-value: 2.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  213 LLFGPPGTGKTLCARAVANRTDACFIrVIGSELvqkyvgEGARMVRELFEMARSK-----KACLIFFDEI 277
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKERlerhgKRTILFIDEV 118
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 182-282 2.33e-03

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 39.92  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   182 EQIEKLREVVEtPLLHpekfvnlGIEPPKgVLLFGPPGTGKTLCARAVANR----TDACFIRV---------------IG 242
Cdd:TIGR02928  22 EQIEELAKALR-PILR-------GSRPSN-VFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17137738   243 SELVQKYVGEG----------ARMVRELF-EMARSKKACLIFFDEIDAIGG 282
Cdd:TIGR02928  93 VELANQLRGSGeevpttglstSEVFRRLYkELNERGDSLIIVLDEIDYLVG 143
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
210-245 4.72e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.18  E-value: 4.72e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17137738 210 KGVLLFGPPGTGKTLCARAVANR--TDACFIRVIGSEL 245
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 212-278 5.48e-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: 5.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 212 VLLFGPPGTGKTLCARAVANRT-DACFIRVIGS----ELVQKYVGE-GARM----VRELFEMARSK-KAC--LIFFDEID 278
Cdd:COG2842  53 GVVYGESGVGKTTAAREYANRNpNVIYVTASPSwtskELLEELAEElGIPAppgtIADLRDRILERlAGTgrLLIIDEAD 132
AAA_22 pfam13401
AAA domain;
212-285 5.72e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   212 VLLFGPPGTGKTLCARAVANRTDAC-----------------FIRVIGSELVQKYVGEG-ARMVRELFE--MARSKKACL 271
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPEVrdsvvfvdlpsgtspkdLLRALLRALGLPLSGRLsKEELLAALQqlLLALAVAVV 87

                          90
                  ....*....|....
gi 17137738   272 IFFDEIDAIGGARF 285
Cdd:pfam13401  88 LIIDEAQHLSLEAL 101
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
212-278 6.49e-03

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 38.73  E-value: 6.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 212 VLLFGPPGTGKTLCARAVAN---RTDACFIRV---------IGSELvQKYVgEGArmvrelFEMARSK-KACLI------ 272
Cdd:COG3284 347 VLILGETGTGKELFARAIHAaspRADGPFVAVncaaipeelIESEL-FGYE-PGA------FTGARRKgRPGKIeqadgg 418


                ....*...
gi 17137738 273 --FFDEID 278
Cdd:COG3284 419 tlFLDEIG 426
rfc PRK00440
replication factor C small subunit; Reviewed
 173-230 7.74e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 38.32  E-value: 7.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738  173 TYSDVGGCKEQIEKLREVVETP-LLHpekfvnlgieppkgvLLF-GPPGTGKTLCARAVA 230
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVKEKnMPH---------------LLFaGPPGTGKTTAALALA 59
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 208-240 7.81e-03

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 38.16  E-value: 7.81e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 17137738 208 PPKGVL-LFGPPGTGKTLCARAVA--NRTDACFIRV 240
Cdd:COG4148  23 PGRGVTaLFGPSGSGKTTLLRAIAglERPDSGRIRL 58
Sigma54_activat pfam00158
Sigma-54 interaction domain;
212-277 8.50e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.00  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738   212 VLLFGPPGTGKTLCARAV---ANRTDACFIRV---------IGSEL--VQKyvgeGArmvrelFEMARSKKACL------ 271
Cdd:pfam00158  25 VLITGESGTGKELFARAIhqlSPRADGPFVAVncaaipeelLESELfgHEK----GA------FTGADSDRKGLfeladg 94


                  ....*...
gi 17137738   272 --IFFDEI 277
Cdd:pfam00158  95 gtLFLDEI 102
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 212-277 9.12e-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: 38.02  E-value: 9.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137738 212 VLLFGPPGTGKTLCARAV---ANRTDACFIRV---------IGSEL--VQKYVGEGARMVRE-LFEMArskKACLIFFDE 276
Cdd:COG2204 157 VLITGESGTGKELVARAIhrlSPRADGPFVAVncaaipeelLESELfgHEKGAFTGAVARRIgKFELA---DGGTLFLDE 233


                .
gi 17137738 277 I 277
Cdd:COG2204 234 I 234
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 207-231 9.86e-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: 36.71  E-value: 9.86e-03
                          10        20
                  ....*....|....*....|....*
gi 17137738   207 EPPKGVLLFGPPGTGKTLCARAVAN 231
Cdd:pfam05496  31 EALDHVLLYGPPGLGKTTLANIIAN 55
 
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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