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Conserved domains on  [gi|19113597|ref|NP_596805|]
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proteasome regulatory subunit Rpt1 [Schizosaccharomyces pombe]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
124-434 1.57e-154

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 442.73  E-value: 1.57e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  124 KFVVSLGERVSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPE 203
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  204 RFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDA 283
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  284 IGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHA 363
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113597  364 KSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQKVV-KGNQKFSSTADYM 434
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
124-434 1.57e-154

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 442.73  E-value: 1.57e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  124 KFVVSLGERVSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPE 203
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  204 RFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDA 283
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  284 IGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHA 363
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113597  364 KSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQKVV-KGNQKFSSTADYM 434
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
94-420 2.05e-132

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 385.69  E-value: 2.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597    94 PLQVARCTKIIENEQSAEKNAyvinlkQIAKFVVSLGERVSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEK 173
Cdd:TIGR01242  43 PLIVGTVLEVLDDNRVVVKSS------TGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEER 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   174 PDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKY 253
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   254 VGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDE 333
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDP 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   334 ALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDF 413
Cdd:TIGR01242 277 ALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDF 356

                  ....*..
gi 19113597   414 LDAVQKV 420
Cdd:TIGR01242 357 IKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
152-422 1.04e-130

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 379.74  E-value: 1.04e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 152 AIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCAR 231
Cdd:COG1222  51 NDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAK 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 232 AVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGdnEVQRTMLELITQLD 311
Cdd:COG1222 131 AVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELD 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 312 GFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRS 391
Cdd:COG1222 209 GFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKA 288
                       250       260       270
                ....*....|....*....|....*....|.
gi 19113597 392 VCTEAGMFAIRARRRVATEKDFLDAVQKVVK 422
Cdd:COG1222 289 IVTEAGMFAIREGRDTVTMEDLEKAIEKVKK 319
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
177-347 1.37e-119

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: 345.48  E-value: 1.37e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 177 TYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGE 256
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 257 GARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALM 336
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 19113597 337 RPGRIDRKVEF 347
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
216-349 7.09e-49

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: 162.76  E-value: 7.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   216 IMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDdgaGG 295
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19113597   296 DNEVQRTMLELITQLDGFDPR-GNIKVLFATNRPNTLDEALMrpGRIDRKVEFGL 349
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
212-351 3.53e-20

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: 86.66  E-value: 3.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597    212 PPKGIMLYGPPGTGKTLCARAVANRTDATFIRVI-----------------GSELVQKYVGEGARMVRELFEMARTKKAC 274
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113597    275 IIFFDEIDAIGGARFddgaggdnEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPgRIDRKVEFGLPD 351
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 ...
216-366 2.24e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  216 IMLYGPPGTGKT-----LCARAVANRTDATFIRVigSELVQKYV---GEGaRMVRELFEMARTKkaCIIffdeIDAIGGA 287
Cdd:NF038214  93 VLLLGPPGTGKThlaiaLGYAACRQGYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLARYD--LLI----IDELGYL 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  288 RFDDGAGGDnevqrtMLELITQLDGfdpRGNIkvLFATNRP----------NTLDEALmrpgrIDRKVEfglpdlegRAH 357
Cdd:NF038214 164 PFSREGANL------LFELIADRYE---RGST--IITSNLPfsewgevfgdPTLAAAI-----LDRLVH--------HAH 219

                 ....*....
gi 19113597  358 ILRIHAKSM 366
Cdd:NF038214 220 ILELKGESY 228
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
124-434 1.57e-154

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 442.73  E-value: 1.57e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  124 KFVVSLGERVSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPE 203
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  204 RFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDA 283
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  284 IGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHA 363
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113597  364 KSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQKVV-KGNQKFSSTADYM 434
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgKEEKDSMEEPGVM 387
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
94-420 2.05e-132

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 385.69  E-value: 2.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597    94 PLQVARCTKIIENEQSAEKNAyvinlkQIAKFVVSLGERVSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEK 173
Cdd:TIGR01242  43 PLIVGTVLEVLDDNRVVVKSS------TGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEER 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   174 PDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKY 253
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   254 VGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDE 333
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDP 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   334 ALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDF 413
Cdd:TIGR01242 277 ALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDF 356

                  ....*..
gi 19113597   414 LDAVQKV 420
Cdd:TIGR01242 357 IKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
152-422 1.04e-130

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 379.74  E-value: 1.04e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 152 AIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCAR 231
Cdd:COG1222  51 NDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAK 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 232 AVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGdnEVQRTMLELITQLD 311
Cdd:COG1222 131 AVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELD 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 312 GFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRS 391
Cdd:COG1222 209 GFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKA 288
                       250       260       270
                ....*....|....*....|....*....|.
gi 19113597 392 VCTEAGMFAIRARRRVATEKDFLDAVQKVVK 422
Cdd:COG1222 289 IVTEAGMFAIREGRDTVTMEDLEKAIEKVKK 319
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
177-347 1.37e-119

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: 345.48  E-value: 1.37e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 177 TYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGE 256
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 257 GARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALM 336
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 19113597 337 RPGRIDRKVEF 347
Cdd:cd19502 161 RPGRFDRKIEF 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
137-426 5.02e-108

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 324.79  E-value: 5.02e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  137 DIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGI 216
Cdd:PTZ00454 103 LLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  217 MLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGD 296
Cdd:PTZ00454 183 LLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGAD 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  297 NEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWEL 376
Cdd:PTZ00454 263 REVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLED 342
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 19113597  377 IARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQKVVKGNQK 426
Cdd:PTZ00454 343 FVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDR 392
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
133-424 1.81e-105

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 319.41  E-value: 1.81e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  133 VSPTDIEEGMRVGCDRNKYAIQLPLPPKIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDP 212
Cdd:PTZ00361 137 VDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKP 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  213 PKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDG 292
Cdd:PTZ00361 217 PKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDAT 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  293 AGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDI 372
Cdd:PTZ00361 297 SGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDV 376
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19113597  373 RWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQKVV---KGN 424
Cdd:PTZ00361 377 DLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLyrkKGN 431
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
168-428 1.91e-88

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: 277.63  E-value: 1.91e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   168 MQVEEKPDVTYGDVGGCKEQIERLREVVELpLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGS 247
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   248 ELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNR 327
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   328 PNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRV 407
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282
                         250       260
                  ....*....|....*....|.
gi 19113597   408 ATEKDFLDAVQKVVKGNQKFS 428
Cdd:TIGR01241 283 ITMNDIEEAIDRVIAGPEKKS 303
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
168-426 4.61e-84

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 268.83  E-value: 4.61e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 168 MQVEEKPDVTYGDVGGCKEQIERLREVVELpLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGS 247
Cdd:COG0465 131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 248 ELVQKYVGEGARMVRELFEMARtKKA-CIIFFDEIDAIGGARfddGA---GGDNEVQRTMLELITQLDGFDPRGNIKVLF 323
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAK-KNApCIIFIDEIDAVGRQR---GAglgGGHDEREQTLNQLLVEMDGFEGNEGVIVIA 285
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 324 ATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRA 403
Cdd:COG0465 286 ATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARR 365
                       250       260
                ....*....|....*....|...
gi 19113597 404 RRRVATEKDFLDAVQKVVKGNQK 426
Cdd:COG0465 366 NKKAVTMEDFEEAIDRVIAGPER 388
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
180-420 6.71e-75

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: 239.43  E-value: 6.71e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:COG0464 158 DLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEK 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLeliTQLDGFdpRGNIKVLFATNRPNTLDEALMRpg 339
Cdd:COG0464 238 NLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLL---TEMEEL--RSDVVVIAATNRPDLLDPALLR-- 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 340 RIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQK 419
Cdd:COG0464 311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALER 390

                .
gi 19113597 420 V 420
Cdd:COG0464 391 E 391
ftsH CHL00176
cell division protein; Validated
169-423 6.74e-73

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 240.72  E-value: 6.74e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  169 QVEEKPDVTYGDVGGCKEQIERLREVVELpLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSE 248
Cdd:CHL00176 173 QMEADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSE 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  249 LVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARfDDGAGGDN-EVQRTMLELITQLDGFDPRGNIKVLFATNR 327
Cdd:CHL00176 252 FVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQR-GAGIGGGNdEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  328 PNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRV 407
Cdd:CHL00176 331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKAT 410
                        250
                 ....*....|....*.
gi 19113597  408 ATEKDFLDAVQKVVKG 423
Cdd:CHL00176 411 ITMKEIDTAIDRVIAG 426
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
164-428 7.03e-71

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 235.70  E-value: 7.03e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  164 SVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELpLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIR 243
Cdd:PRK10733 137 SKARMLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFT 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  244 VIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLF 323
Cdd:PRK10733 216 ISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIA 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  324 ATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRA 403
Cdd:PRK10733 296 ATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARG 375
                        250       260
                 ....*....|....*....|....*
gi 19113597  404 RRRVATEKDFLDAVQKVVKGNQKFS 428
Cdd:PRK10733 376 NKRVVSMVEFEKAKDKIMMGAERRS 400
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
174-402 1.11e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 231.72  E-value: 1.11e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   174 PDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKY 253
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   254 VGEGARMVRELFEMARTKKACIIFFDEIDAIGGARfdDGAGGDNEvQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDE 333
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113597   334 ALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIR 402
Cdd:TIGR01243 330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
135-420 3.85e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 230.18  E-value: 3.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   135 PTDIEEGMRVGCDRNKYAIQLplppkIDPSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGIDPPK 214
Cdd:TIGR01243 414 PAEVLKELKVTMKDFMEALKM-----VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPK 488
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   215 GIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARfddGAG 294
Cdd:TIGR01243 489 GVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR---GAR 565
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   295 GDNEV-QRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIR 373
Cdd:TIGR01243 566 FDTSVtDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVD 645
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113597   374 WELIARLCPSQTGAELRSVCTEAGMFAIR------------------ARRRVATEKDFLDAVQKV 420
Cdd:TIGR01243 646 LEELAEMTEGYTGADIEAVCREAAMAALResigspakeklevgeeefLKDLKVEMRHFLEALKKV 710
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
176-345 4.58e-68

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 214.02  E-value: 4.58e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 176 VTYGDVGGCKEQIERLREVVELpLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVG 255
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 256 EGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEAL 335
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|
gi 19113597 336 MRPGRIDRKV 345
Cdd:cd19501 160 LRPGRFDRQV 169
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
180-347 4.71e-64

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: 203.29  E-value: 4.71e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKACIIFFDEIDAIGGARfddgAGGDNEVQRTML-ELITQLDGFDPRGNIKVLFATNRPNTLDEALMRP 338
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVERRVVaQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 19113597 339 GRIDRKVEF 347
Cdd:cd19503 157 GRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
189-343 6.61e-62

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: 197.89  E-value: 6.61e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 189 ERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMA 268
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113597 269 RTKKACIIFFDEIDAIGGARFDDGAGGDNEvqRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDR 343
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 ...
180-348 1.75e-59

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 191.88  E-value: 1.75e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKACIIFFDEIDAIGGARfdDGAGGDNEvQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPG 339
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 19113597 340 RIDRKVEFG 348
Cdd:cd19519 158 RFDREIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
187-347 1.55e-57

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: 186.33  E-value: 1.55e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 187 QIERLREVVELPLLSPERFvKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFE 266
Cdd:cd19481   1 LKASLREAVEAPRRGSRLR-RYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 267 MARTKKACIIFFDEIDAIGGARfdDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVE 346
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 19113597 347 F 347
Cdd:cd19481 158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
189-345 6.53e-57

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: 185.01  E-value: 6.53e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 189 ERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMA 268
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113597 269 RTKKACIIFFDEIDAIGGARfddGAGGDNEV-QRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKV 345
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRR---GTTGDSGVtERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
131-407 1.71e-55

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: 191.85  E-value: 1.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   131 ERV---SPTDIEEGMRVGcD------RNKYAIQlPLPPKidpSVTMMQVEEKPDVTYGDVGGCKEQIERLREVVELPLLS 201
Cdd:TIGR03689 130 ERVvklAGALADEGLRPG-DtllvdpRAGYAFE-AIPRT---EVEDLVLEEVPDVTYADIGGLGSQIEQIRDAVELPFLH 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   202 PERFVKLGIDPPKGIMLYGPPGTGKTLCARAVAN----------RTDATFIRVIGSELVQKYVGEGARMVRELFEMARTK 271
Cdd:TIGR03689 205 PELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNKYVGETERQIRLIFQRAREK 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   272 KA----CIIFFDEIDAIGGARfddGAGGDNEVQRTML-ELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVE 346
Cdd:TIGR03689 285 ASegrpVIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIR 361
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113597   347 FGLPDLEGRAHILrihAKSMAIDKDIRWELIARLCPSQ-TGAELRSVCTEAgMFAIRARRRV 407
Cdd:TIGR03689 362 IERPDAEAAADIF---AKYLTDDLPLPEDLAAHDGDREaTAAALIQRVVDA-LYARSEANRY 419
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
180-419 3.75e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 175.46  E-value: 3.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVElPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:COG1223   3 DVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKaCIIFFDEIDAIGGARFDDGAGGdnEVQRTMLELITQLDGFdpRGNIKVLFATNRPNTLDEALMRpg 339
Cdd:COG1223  82 NLRKLFDFARRAP-CVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 340 RIDRKVEFGLPDLEGRAHILRIHAKSMAIDKDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLDAVQK 419
Cdd:COG1223 155 RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQ 234
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
189-345 8.83e-52

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 171.54  E-value: 8.83e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 189 ERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMA 268
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113597 269 RTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKV 345
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
216-349 7.09e-49

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: 162.76  E-value: 7.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   216 IMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDdgaGG 295
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19113597   296 DNEVQRTMLELITQLDGFDPR-GNIKVLFATNRPNTLDEALMrpGRIDRKVEFGL 349
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
181-337 9.65e-48

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 160.98  E-value: 9.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 181 VGGCKEQIERLREVVELPLLSPERFvKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARM 260
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 261 VRELFEMARTKKACIIFFDEIDAIGGARfddgAGGDNEVQRTM-LELITQLDGF--DPRGNIKVLFATNRPNTLDEALMR 337
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSER----GSGEHEASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
198-343 1.48e-47

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: 160.73  E-value: 1.48e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 198 PLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIF 277
Cdd:cd19530  15 PIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIF 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113597 278 FDEIDAIGGARFDDGAGGdneVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDR 343
Cdd:cd19530  95 FDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
180-347 8.48e-47

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: 158.83  E-value: 8.48e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVAN--RTDA---TFIRVIGSELVQKYV 254
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAecSKGGqkvSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 255 GEGARMVRELFEMARTKKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLELitqLDGFDPRGNIKVLFATNRPNTLDEA 334
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157
                       170
                ....*....|...
gi 19113597 335 LMRPGRIDRKVEF 347
Cdd:cd19517 158 LRRPGRFDREFYF 170
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
180-345 5.49e-43

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: 148.71  E-value: 5.49e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKACIIFFDEIDAIGGARfdDGAGGDNEvQRTMLELITQLDGF----DPRGNIKVLFATNRPNTLDEAL 335
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 19113597 336 MRPGRIDRKV 345
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
191-346 6.49e-42

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 145.65  E-value: 6.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 191 LREVVELPLLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMART 270
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113597 271 KKACIIFFDEIDAIGGARFDDGAGGDNEVQRTMLeliTQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVE 346
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLL---TQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
193-343 1.88e-40

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: 141.88  E-value: 1.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 193 EVVELPLLSPERFVKlGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKK 272
Cdd:cd19527   7 DTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAK 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113597 273 ACIIFFDEIDAIGGARfddGAGGDNE--VQRTMLELITQLDGF-DPRGNIKVLFATNRPNTLDEALMRPGRIDR 343
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; ...
174-337 2.51e-40

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: 142.43  E-value: 2.51e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 174 PDVTYGDVGGCKEQIERLREVVELPLLSPERFVKLGiDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKY 253
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 254 VGEGARMVRELFEMARTKKACIIFFDEIDAIGGARfddGAGGDNEVQRTMLELITQLDGFD--PRGNIKVLFATNRPNTL 331
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEI 172

                ....*.
gi 19113597 332 DEALMR 337
Cdd:cd19525 173 DEAARR 178
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
180-337 1.81e-39

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: 139.48  E-value: 1.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGI-DPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGA 258
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 259 RMVRELFEMARTKKACIIFFDEIDAIGGARfddgAGGDNEVQRTM-LELITQLDGFDPRGNIKVLF--ATNRPNTLDEAL 335
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156

                ..
gi 19113597 336 MR 337
Cdd:cd19520 157 LR 158
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
173-345 1.84e-39

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 139.61  E-value: 1.84e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 173 KPDVTYGDVGGCKEQIERLREVVELPLLSPERFVKlGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQK 252
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 253 YVGEGARMVRELFEMARTKKACIIFFDEIDAIGGARfddGAGGDNEVQRTMLELITQLDGF--DPRGnIKVLFATNRPNT 330
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR---GEGESEASRRIKTELLVQMNGVgnDSQG-VLVLGATNIPWQ 155
                       170
                ....*....|....*
gi 19113597 331 LDEALMRpgRIDRKV 345
Cdd:cd19521 156 LDSAIRR--RFEKRI 168
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
180-345 1.25e-37

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: 134.73  E-value: 1.25e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVklGIDPP-KGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGA 258
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 259 RMVRELFEMARTKKACIIFFDEIDAIGGARfddGAGGDNEV-QRTMLELITQLDGF-------DPRGNIKVLFATNRPNT 330
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155
                       170
                ....*....|....*
gi 19113597 331 LDEALMRpgRIDRKV 345
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
180-337 3.03e-34

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 125.35  E-value: 3.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLGIdPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKACIIFFDEIDAIGGARFDdgagGDNEVQRTM-LELITQLDGFDPRGNIKVLF--ATNRPNTLDEALM 336
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVL 155

                .
gi 19113597 337 R 337
Cdd:cd19524 156 R 156
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
199-346 5.26e-32

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 119.90  E-value: 5.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 199 LLSPERFVKLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVI-GSELVQKYVGEGARMVRELFEMA-RTKKAC-- 274
Cdd:cd19504  21 VFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESEANIRKLFADAeEEQRRLga 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 275 -----IIFFDEIDAI---GGARFDDGAGGDNEVQrtmlELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVE 346
Cdd:cd19504 101 nsglhIIIFDEIDAIckqRGSMAGSTGVHDTVVN----QLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
182-349 5.27e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 108.39  E-value: 5.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 182 GGCKEQIERLREVVELPllsperfvklgidPPKGIMLYGPPGTGKTLCARAVAN---RTDATFIRVIGSELVQKYVGEGA 258
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 259 R---MVRELFEMARTKKACIIFFDEIDAIggarfddGAGGDNEVQRTMLELItqlDGFDPRGNIKVLFATNRPNTLDEAL 335
Cdd:cd00009  68 FghfLVRLLFELAEKAKPGVLFIDEIDSL-------SRGAQNALLRVLETLN---DLRIDRENVRVIGATNRPLLGDLDR 137
                       170
                ....*....|....
gi 19113597 336 MRPGRIDRKVEFGL 349
Cdd:cd00009 138 ALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
180-337 1.67e-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: 1.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 180 DVGGCKEQIERLREVVELPLLSPERFVKLgIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGAR 259
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 260 MVRELFEMARTKKACIIFFDEIDAIGGARFDdgagGDNEVQRTMLELITQLDGF--DPRGNIKVLFATNRPNTLDEALMR 337
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
212-351 3.53e-20

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: 86.66  E-value: 3.53e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597    212 PPKGIMLYGPPGTGKTLCARAVANRTDATFIRVI-----------------GSELVQKYVGEGARMVRELFEMARTKKAC 274
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113597    275 IIFFDEIDAIGGARFddgaggdnEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPgRIDRKVEFGLPD 351
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
ycf46 CHL00195
Ycf46; Provisional
209-421 1.19e-17

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 85.07  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  209 GIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEID-AIGGA 287
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  288 RFDDGAGGDNEVQRTMlelITQLDgfDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEFGLPDLEGRAHILRIHAKSMA 367
Cdd:CHL00195 335 ESKGDSGTTNRVLATF---ITWLS--EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR 409
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113597  368 ID--KDIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEkDFLDAVQKVV 421
Cdd:CHL00195 410 PKswKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTD-DILLALKQFI 464
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
209-343 2.89e-17

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: 78.56  E-value: 2.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 209 GIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEID-AIGGA 287
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113597 288 RFDDGAGGDNEVQRTMLELITQldgfdprgNIKVLF--AT-NRPNTLDEALMRPGRIDR 343
Cdd:cd19507 107 DSKGDSGTSSRVLGTFLTWLQE--------KKKPVFvvATaNNVQSLPPELLRKGRFDE 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
214-347 7.93e-12

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 62.93  E-value: 7.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 214 KGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSElVQKYVGEGARMVRELFEMART-KKACIIFFDEIDAIGGARFDDG 292
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEK 101
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19113597 293 AggdNEVQRTMLELITQLDGFDPRGNIKVLfATNRPNTLDEALMrpGRIDRKVEF 347
Cdd:cd19512 102 I---SEDLRAALNAFLYRTGEQSNKFMLVL-ASNQPEQFDWAIN--DRIDEMVEF 150
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
207-347 1.64e-10

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: 59.29  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 207 KLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSElvqkyVGEGARMVRELfeMARTKKACIIFFDEIDA--- 283
Cdd:cd19510  17 DRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDIDAafe 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113597 284 IGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALMRPGRIDRKVEF 347
Cdd:cd19510  90 SREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
216-343 1.30e-09

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 57.46  E-value: 1.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 216 IMLYGPPGTGKT-LC---ARAVANRTDAT-----FIRVIGSELVQKYVGEGARMVRELF----EMARTKKACI-IFFDEI 281
Cdd:cd19508  55 VLLHGPPGTGKTsLCkalAQKLSIRLSSRyrygqLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKDALVfVLIDEV 134
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113597 282 DAIGGARFDDGAGGD-NEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLDEALmrpgrIDR 343
Cdd:cd19508 135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF-----VDR 192
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
213-307 2.16e-09

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 56.62  E-value: 2.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 213 PKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQ-KYVGEGAR-MVRELFEmartkkaCIIFFDEIDAIggARFD 290
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGRDVEsIIRDLVE-------GIVFIDEIDKI--AKRG 116
                        90       100
                ....*....|....*....|
gi 19113597 291 DGAGGD---NEVQRTMLELI 307
Cdd:cd19498 117 GSSGPDvsrEGVQRDLLPIV 136
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
216-281 3.69e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 55.09  E-value: 3.69e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113597  216 IMLYGPPGTGKTLCARAVANRTDATFIR---VIGSelvqkyVGEgarmVRELFEMARTKKA----CIIFFDEI 281
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAlsaVTSG------VKD----LREVIEEARQRRSagrrTILFIDEI 101
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
371-415 4.01e-08

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: 49.07  E-value: 4.01e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 19113597   371 DIRWELIARLCPSQTGAELRSVCTEAGMFAIRARRRVATEKDFLD 415
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
218-281 6.20e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 54.68  E-value: 6.20e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113597 218 LYGPPGTGKTLCARAVANRTDATFIRVIGselvqkyVGEGARMVRELFEMARTKKA----CIIFFDEI 281
Cdd:COG2256  54 LWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRAygrrTILFVDEI 114
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
186-291 3.03e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 52.16  E-value: 3.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 186 EQIERLREVVElPLLSPERfvklgidpPKGIMLYGPPGTGKTLCARAVANR---------TDATFIRV----------IG 246
Cdd:COG1474  33 EEIEELASALR-PALRGER--------PSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrVL 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113597 247 SELVQKyVGEG----------ARMVRELFE-MARTKKACIIFFDEIDAIGGARFDD 291
Cdd:COG1474 104 SRILEE-LGSGedipstglstDELFDRLYEaLDERDGVLVVVLDEIDYLVDDEGDD 158
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
213-307 4.63e-07

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: 49.50  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   213 PKG-IMLYGPPGTGKTLCARAVANR---TDATFIRVIGSELVQK------------YVG--EGArmvrELFEMARTKKAC 274
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEhsvsrligappgYVGyeEGG----QLTEAVRRKPYS 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 19113597   275 IIFFDEIDAIggarfddgaggDNEVQRTMLELI 307
Cdd:pfam07724  78 IVLIDEIEKA-----------HPGVQNDLLQIL 99
PRK04195 PRK04195
replication factor C large subunit; Provisional
212-288 1.04e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.69  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  212 PPKGIMLYGPPGTGKTLCARAVANRtdatfirvIGSELV-------------QKYVGEGARMvRELFEMARTkkacIIFF 278
Cdd:PRK04195  38 PKKALLLYGPPGVGKTSLAHALAND--------YGWEVIelnasdqrtadviERVAGEAATS-GSLFGARRK----LILL 104
                         90
                 ....*....|....*.
gi 19113597  279 DEIDAI------GGAR 288
Cdd:PRK04195 105 DEVDGIhgnedrGGAR 120
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
185-280 1.53e-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: 50.23  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   185 KEQIERLREVVELPLLSPERFVKLGIDPpKGIMLYGPPGTGKTLCARAVANR-------TDATFIRVIGSELVQKYVGEG 257
Cdd:TIGR03922 285 KRQVAALKSSTAMALARAERGLPVAQTS-NHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGES 363
                          90       100
                  ....*....|....*....|...
gi 19113597   258 ARMVRELFEMARTKkacIIFFDE 280
Cdd:TIGR03922 364 EAKTNEIIDSALGG---VLFLDE 383
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
207-343 3.10e-06

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: 46.99  E-value: 3.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 207 KLGIDPPKGIMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQK--------------YVGEGARMVRELFEMARTKK 272
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113597 273 ACIIFFDEIDAIGGARFDDGAGGDNevqRTMLELITQLDGFDPRG----NIKVLFATNRPNTLDEALMRPGRIDR 343
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKsstrNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
211-282 1.82e-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: 44.86  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 211 DPPKGI---MLYGPPGTGKTLCARAVA---NRTDATFIRVIGSELVQK------------YVGEGARMVreLFEMARTKK 272
Cdd:cd19499  36 DPNRPIgsfLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGGQ--LTEAVRRKP 113
                        90
                ....*....|
gi 19113597 273 ACIIFFDEID 282
Cdd:cd19499 114 YSVVLLDEIE 123
44 PHA02544
clamp loader, small subunit; Provisional
205-351 1.64e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.44  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  205 FVKLGIDPpkGIMLYGP-PGTGKTLCARAVANRTDATFIRVIGS----ELVQKYVGEGARmvrelfEMARTKKACIIFFD 279
Cdd:PHA02544  36 IVKKGRIP--NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFAS------TVSLTGGGKVIIID 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113597  280 EIDAIGGArfddgaggdnEVQRTMLELITQLDgfdprGNIKVLFATNRPNTLDEALMrpGRIdRKVEFGLPD 351
Cdd:PHA02544 108 EFDRLGLA----------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPT 161
PRK13341 PRK13341
AAA family ATPase;
218-281 2.76e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.12  E-value: 2.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113597  218 LYGPPGTGKTLCARAVANRTDATFIrVIGSELvqkyvgEGARMVRELFEMARTK-----KACIIFFDEI 281
Cdd:PRK13341  57 LYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKERlerhgKRTILFIDEV 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
215-337 3.20e-04

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: 40.74  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   215 GIMLYGPPGTGKTLCARAVANRTD--ATFIRVIG-----SELVQKYV--GEGARMV-RELFEMARtkKACIIFFDEIDAI 284
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrPVFYVQLTrdtteEDLFGRRNidPGGASWVdGPLVRAAR--EGEIAVLDEINRA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113597   285 GGarfddgaggdnEVQRTMLELI-----TQLDGF----DPRGNIKVLFATNRP----NTLDEALMR 337
Cdd:pfam07728  79 NP-----------DVLNSLLSLLderrlLLPDGGelvkAAPDGFRLIATMNPLdrglNELSPALRS 133
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
186-286 3.58e-04

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 42.62  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   186 EQIERLREVVElPLLSPERfvklgidpPKGIMLYGPPGTGKTLCARAVANR----TDATFIRV---------------IG 246
Cdd:TIGR02928  22 EQIEELAKALR-PILRGSR--------PSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVL 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19113597   247 SELVQKYVGEG----------ARMVRELF-EMARTKKACIIFFDEIDAIGG 286
Cdd:TIGR02928  93 VELANQLRGSGeevpttglstSEVFRRLYkELNERGDSLIIVLDEIDYLVG 143
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
216-285 4.97e-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: 41.43  E-value: 4.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113597 216 IMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQK-YVGEGAR--MVREL----FEMARTKKAcIIFFDEIDAIG 285
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGEDVEniLLKLLqaadYDVERAQRG-IVYIDEIDKIA 128
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
216-332 6.11e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 39.41  E-value: 6.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 216 IMLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVgegaRMVRELFEmarTKKACIIFFDEIDAIGGARfddgagg 295
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIEDLIE---EKKLDIIIIDSLSSLARAS------- 66
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19113597 296 DNEVQRTMLELITQLDGFDPRGNIKVLFATNRPNTLD 332
Cdd:cd01120  67 QGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDI 103
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
220-282 7.60e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 41.31  E-value: 7.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113597 220 GPPGTGKTLCARAVANRTDATFIRV-----------IGSELVQKYVGEgarmvrelFEMartKK----ACIIFFDEID 282
Cdd:COG0714  38 GVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGE--------FEF---RPgplfANVLLADEIN 104
AAA_22 pfam13401
AAA domain;
216-289 9.00e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 9.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   216 IMLYGPPGTGKTLCARAVANRTD-----------------ATFIRVIGSELVQKYVGEG-ARMVRELFE--MARTKKACI 275
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPevrdsvvfvdlpsgtspKDLLRALLRALGLPLSGRLsKEELLAALQqlLLALAVAVV 87
                          90
                  ....*....|....
gi 19113597   276 IFFDEIDAIGGARF 289
Cdd:pfam13401  88 LIIDEAQHLSLEAL 101
rfc PRK00440
replication factor C small subunit; Reviewed
177-283 2.05e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 39.86  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  177 TYGDVGGCKEQIERLREVVE---LPLLsperfvklgidppkgiMLYGPPGTGKTLCARAVA---------------NRTD 238
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVKeknMPHL----------------LFAGPPGTGKTTAALALArelygedwrenflelNASD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19113597  239 ATFIRVIgselvqkyvgegarmvRE-LFEMARTKKAC-----IIFFDEIDA 283
Cdd:PRK00440  79 ERGIDVI----------------RNkIKEFARTAPVGgapfkIIFLDEADN 113
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
216-366 2.24e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  216 IMLYGPPGTGKT-----LCARAVANRTDATFIRVigSELVQKYV---GEGaRMVRELFEMARTKkaCIIffdeIDAIGGA 287
Cdd:NF038214  93 VLLLGPPGTGKThlaiaLGYAACRQGYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLARYD--LLI----IDELGYL 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597  288 RFDDGAGGDnevqrtMLELITQLDGfdpRGNIkvLFATNRP----------NTLDEALmrpgrIDRKVEfglpdlegRAH 357
Cdd:NF038214 164 PFSREGANL------LFELIADRYE---RGST--IITSNLPfsewgevfgdPTLAAAI-----LDRLVH--------HAH 219

                 ....*....
gi 19113597  358 ILRIHAKSM 366
Cdd:NF038214 220 ILELKGESY 228
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
220-340 3.58e-03

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: 37.99  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 220 GPPGTGKTLCARAVANRTDATFIRVI--GSELVQKYVGEGARMV----------RELFEMART--KKACIIFFDEIDaig 285
Cdd:cd00267  32 GPNGSGKSTLLRAIAGLLKPTSGEILidGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPDLLLLDEPT--- 108
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 286 garfddgAGGDNEVQRTMLELITQLdgfdPRGNIKVLFATNRPNTLDEA-----LMRPGR 340
Cdd:cd00267 109 -------SGLDPASRERLLELLREL----AEEGRTVIIVTHDPELAELAadrviVLKDGK 157
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
210-252 3.71e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 3.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 19113597 210 IDPPKGIMLYGPPGTGKT--LCA---RAVANRTDATFIRVigSELVQK 252
Cdd:COG1484  96 IERGENLILLGPPGTGKThlAIAlghEACRAGYRVRFTTA--PDLVNE 141
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
216-280 5.08e-03

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 38.62  E-value: 5.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 216 IMLYGPPGTGKTLCARAVANRTD---------------ATFIRVIGSELVQKYVGEG-----ARMVRELFEMARTKKACI 275
Cdd:COG3267  46 VVLTGEVGTGKTTLLRRLLERLPddvkvayipnpqlspAELLRAIADELGLEPKGASkadllRQLQEFLLELAAAGRRVV 125

                ....*
gi 19113597 276 IFFDE 280
Cdd:COG3267 126 LIIDE 130
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
216-285 5.39e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 37.92  E-value: 5.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597 216 IMLYGPPGTGKTLCARAVANRTDATFIRV-IG-----SELV---QKYVGE-GARMVRelfEMARTKKA-CIIFFDEIDAI 284
Cdd:cd19500  40 LCLVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAmPGRIIQ---ALKKAGTNnPVFLLDEIDKI 116

                .
gi 19113597 285 G 285
Cdd:cd19500 117 G 117
Sigma54_activat pfam00158
Sigma-54 interaction domain;
216-281 8.00e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.00  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113597   216 IMLYGPPGTGKTLCARAV---ANRTDATFIRV---------IGSEL--VQKyvG--EGARMVRE-LFEMArtkKACIIFF 278
Cdd:pfam00158  25 VLITGESGTGKELFARAIhqlSPRADGPFVAVncaaipeelLESELfgHEK--GafTGADSDRKgLFELA---DGGTLFL 99

                  ...
gi 19113597   279 DEI 281
Cdd:pfam00158 100 DEI 102
 
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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