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Conserved domains on  [gi|1013362348|ref|NP_001308897|]
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outer mitochondrial transmembrane helix translocase isoform 2 [Homo sapiens]

Protein Classification

ATP-binding protein( domain architecture ID 14291541)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain, similar to yeast Pch2 which is required for the meiotic checkpoint that prevents chromosome segregation when recombination and chromosome synapsis are defective, and to IQCA1 (dynein regulatory complex subunit 11) which is an ATPase subunit of the nexin-dynein regulatory complex

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 92-232 6.09e-98

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19520:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 166  Bit Score: 286.24  E-value: 6.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQAL 232
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVI 141
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 4-314 1.17e-49

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: 170.48  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348   4 AEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDP 83
Cdd:COG0464    70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  84 LNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:COG0464   150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTD-----------HSCQAL 232
Cdd:COG0464   229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSDvvviaatnrpdLLDPAL 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 233 K---------------QREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVnstseeshdede 297
Cdd:COG0464   309 LrrfdeiiffplpdaeERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGR------------ 376

                         330
                  ....*....|....*..
gi 1013362348 298 iRPVQQQDLHRAIEKMK 314
Cdd:COG0464   377 -EPVTTEDLLEALERED 392
 
Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 92-232 6.09e-98

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: 286.24  E-value: 6.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQAL 232
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVI 141
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 88-320 1.10e-68

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 217.57  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:COG1222    75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSS-DHEATAMMKAQFMSLWDGLDTDHSC-------------QAL- 232
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFESRGDVliiaatnrpdlldPALl 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 233 ----------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstseeshDED 296
Cdd:COG1222   234 rpgrfdrvievplpdeEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE----------GRD 303

                         250       260
                  ....*....|....*....|....
gi 1013362348 297 EIRpvqQQDLHRAIEKMKKSKDAA 320
Cdd:COG1222   304 TVT---MEDLEKAIEKVKKKTETA 324
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 88-318 1.69e-52

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 177.33  E-value: 1.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:PRK03992  128 VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEAT-AMMkaQFMSLWDGLDT-------------DHSC 229
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsgTSGDREVQrTLM--QLLAEMDGFDPrgnvkiiaatnriDILD 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 230 QAL-----------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstsees 292
Cdd:PRK03992  285 PAIlrpgrfdriievplpdeEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD--------- 355

                         250       260
                  ....*....|....*....|....*.
gi 1013362348 293 hDEDEIRpvqQQDLHRAIEKMKKSKD 318
Cdd:PRK03992  356 -DRTEVT---MEDFLKAIEKVMGKEE 377
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 4-314 1.17e-49

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: 170.48  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348   4 AEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDP 83
Cdd:COG0464    70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  84 LNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:COG0464   150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTD-----------HSCQAL 232
Cdd:COG0464   229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSDvvviaatnrpdLLDPAL 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 233 K---------------QREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVnstseeshdede 297
Cdd:COG0464   309 LrrfdeiiffplpdaeERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGR------------ 376

                         330
                  ....*....|....*..
gi 1013362348 298 iRPVQQQDLHRAIEKMK 314
Cdd:COG0464   377 -EPVTTEDLLEALERED 392
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 88-314 1.15e-43

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: 153.80  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQ------------- 230
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsgTSGDREVQRTL-MQLLAELDGFDPRGNVKviaatnrpdildp 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 231 -----------------ALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstseesh 293
Cdd:TIGR01242 277 allrpgrfdriievplpDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIRE---------- 346

                         250       260
                  ....*....|....*....|.
gi 1013362348 294 dedEIRPVQQQDLHRAIEKMK 314
Cdd:TIGR01242 347 ---ERDYVTMDDFIKAVEKVL 364
cell_div_CdvC NF041006
cell division protein CdvC;
88-316 9.84e-38

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.94  E-value: 9.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFEnsrlLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:NF041006  100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFP----LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKL-----QPSIIFIDEIDSFLrNRSSSDHEATAMMKAQFMSLWDGL-DTDHSCQA---------- 231
Cdd:NF041006  176 GEAEKNVAKIFKKAREKskeegKPAIIFIDEIDALL-GVYSSEVGGEVRVRNQFLKEMDGLqDKSENYHVyvigatnkpw 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 232 --------------------LKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNStsee 291
Cdd:NF041006  255 rldepflrrfqkriyiplpdREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK---- 330

                         250       260
                  ....*....|....*....|....*
gi 1013362348 292 shDEDEIRPVQQQDLHRAIEKMKKS 316
Cdd:NF041006  331 --GLGEPRPITMEDFKEVLKIRKPS 353
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 129-228 2.89e-34

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: 121.93  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEA 208
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100
                  ....*....|....*....|
gi 1013362348 209 TAMMKAQFMSLWDGLDTDHS 228
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNS 100
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 125-219 7.09e-12

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: 62.39  E-value: 7.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  125 PPKGVLLYGPPGCGKTLIAKATAKEAGC-----------------RFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPS 187
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPpgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1013362348  188 IIFIDEIDSFLRNRSSSDHEATAMMKAQFMSL 219
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK 112
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 252-291 4.75e-10

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: 54.08  E-value: 4.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1013362348 252 VDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEE 291
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
 
Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 92-232 6.09e-98

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: 286.24  E-value: 6.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQAL 232
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVI 141
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 88-320 1.10e-68

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 217.57  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:COG1222    75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSS-DHEATAMMKAQFMSLWDGLDTDHSC-------------QAL- 232
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFESRGDVliiaatnrpdlldPALl 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 233 ----------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstseeshDED 296
Cdd:COG1222   234 rpgrfdrvievplpdeEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE----------GRD 303

                         250       260
                  ....*....|....*....|....
gi 1013362348 297 EIRpvqQQDLHRAIEKMKKSKDAA 320
Cdd:COG1222   304 TVT---MEDLEKAIEKVKKKTETA 324
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 93-228 5.36e-59

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: 187.17  E-value: 5.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  93 IAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQK 172
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLR--GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1013362348 173 LAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHS 228
Cdd:cd19509    79 IVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPE 134
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 88-318 1.69e-52

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 177.33  E-value: 1.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:PRK03992  128 VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEAT-AMMkaQFMSLWDGLDT-------------DHSC 229
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsgTSGDREVQrTLM--QLLAEMDGFDPrgnvkiiaatnriDILD 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 230 QAL-----------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstsees 292
Cdd:PRK03992  285 PAIlrpgrfdriievplpdeEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD--------- 355

                         250       260
                  ....*....|....*....|....*.
gi 1013362348 293 hDEDEIRpvqQQDLHRAIEKMKKSKD 318
Cdd:PRK03992  356 -DRTEVT---MEDFLKAIEKVMGKEE 377
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 4-314 1.17e-49

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: 170.48  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348   4 AEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDP 83
Cdd:COG0464    70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  84 LNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:COG0464   150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTD-----------HSCQAL 232
Cdd:COG0464   229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSDvvviaatnrpdLLDPAL 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 233 K---------------QREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVnstseeshdede 297
Cdd:COG0464   309 LrrfdeiiffplpdaeERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGR------------ 376

                         330
                  ....*....|....*..
gi 1013362348 298 iRPVQQQDLHRAIEKMK 314
Cdd:COG0464   377 -EPVTTEDLLEALERED 392
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 85-225 1.01e-43

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: 148.60  E-value: 1.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  85 NMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTD 164
Cdd:cd19525    16 GPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR--GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 165 KWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDT 225
Cdd:cd19525    94 KWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATT 154
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 92-225 1.01e-43

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: 147.69  E-value: 1.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLR--APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDT 225
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS 132
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 88-314 1.15e-43

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: 153.80  E-value: 1.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQ------------- 230
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsgTSGDREVQRTL-MQLLAELDGFDPRGNVKviaatnrpdildp 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 231 -----------------ALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstseesh 293
Cdd:TIGR01242 277 allrpgrfdriievplpDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIRE---------- 346

                         250       260
                  ....*....|....*....|.
gi 1013362348 294 dedEIRPVQQQDLHRAIEKMK 314
Cdd:TIGR01242 347 ---ERDYVTMDDFIKAVEKVL 364
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 92-226 3.63e-43

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: 146.28  E-value: 3.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGL-KPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTD 226
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSR 134
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 54-316 2.23e-42

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: 155.84  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  54 QAEKLMKQIgVKNVKLSEYEMSIAAHLVDPLNM--------HVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQP 125
Cdd:TIGR01243 409 EAEEIPAEV-LKELKVTMKDFMEALKMVEPSAIrevlvevpNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGI-RP 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 126 PKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSD 205
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 206 HEA-TAMMKAQFMSLWDGLDTDHSCQAL------------------------------KQREAILKLILKNENVDRHVDL 254
Cdd:TIGR01243 567 DTSvTDRIVNQLLTEMDGIQELSNVVVIaatnrpdildpallrpgrfdrlilvpppdeEARKEIFKIHTRSMPLAEDVDL 646

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013362348 255 LEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRP-----VQQQDLHRAIEKMKKS 316
Cdd:TIGR01243 647 EELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFlkdlkVEMRHFLEALKKVKPS 713
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 87-226 6.26e-42

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: 143.46  E-value: 6.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  87 HVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKW 166
Cdd:cd19521     3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNR--KPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 167 YGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTD 226
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGND 140
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 88-328 3.10e-40

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: 150.06  E-value: 3.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFEnsRL-LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKW 166
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFE--HLgIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 167 YGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLD-------------TDHSCQALK 233
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKgrgrvivigatnrPDALDPALR 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 234 Q-----------------REAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTS-----EE 291
Cdd:TIGR01243 333 RpgrfdreivirvpdkraRKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKinfeaEE 412

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1013362348 292 SHDE--DEIRpVQQQDLHraiEKMKKSKDAAFQNVLTHV 328
Cdd:TIGR01243 413 IPAEvlKELK-VTMKDFM---EALKMVEPSAIREVLVEV 447
cell_div_CdvC NF041006
cell division protein CdvC;
88-316 9.84e-38

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.94  E-value: 9.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFEnsrlLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:NF041006  100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFP----LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKL-----QPSIIFIDEIDSFLrNRSSSDHEATAMMKAQFMSLWDGL-DTDHSCQA---------- 231
Cdd:NF041006  176 GEAEKNVAKIFKKAREKskeegKPAIIFIDEIDALL-GVYSSEVGGEVRVRNQFLKEMDGLqDKSENYHVyvigatnkpw 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 232 --------------------LKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNStsee 291
Cdd:NF041006  255 rldepflrrfqkriyiplpdREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK---- 330

                         250       260
                  ....*....|....*....|....*
gi 1013362348 292 shDEDEIRPVQQQDLHRAIEKMKKS 316
Cdd:NF041006  331 --GLGEPRPITMEDFKEVLKIRKPS 353
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 89-225 2.03e-37

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: 131.69  E-value: 2.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  89 TWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYG 168
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGI-EPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 169 ESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDT 225
Cdd:cd19502    80 EGARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsgTGGDREVQRTM-LELLNQLDGFDP 139
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 92-223 6.36e-36

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 127.79  E-value: 6.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR--RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNR-SSSDHEATAMMKAQFMSLWDGL 223
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGV 131
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 129-228 2.89e-34

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: 121.93  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEA 208
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100
                  ....*....|....*....|
gi 1013362348 209 TAMMKAQFMSLWDGLDTDHS 228
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNS 100
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 103-205 4.24e-34

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: 122.78  E-value: 4.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 103 LKDTVILPIKKKHLFenSRL-LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLA 181
Cdd:cd19511     5 LKEAVEWPLKHPDAF--KRLgIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                          90       100
                  ....*....|....*....|....
gi 1013362348 182 IKLQPSIIFIDEIDSFLRNRSSSD 205
Cdd:cd19511    83 RQAAPCIIFFDEIDSLAPRRGQSD 106
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 88-224 2.27e-33

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: 128.67  E-value: 2.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCR----------FINL 157
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELPFLHPELYREYGL-KPPKGVLLYGPPGCGKTLIAKAVANSLAARigaegggksyFLNI 257

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013362348 158 QPSTLTDKWYGESQKLAAAVFSLAIKL----QPSIIFIDEIDSFLRNRS---SSDHEATAMmkAQFMSLWDGLD 224
Cdd:TIGR03689 258 KGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGsgvSSDVETTVV--PQLLAEIDGVE 329
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 99-226 2.07e-32

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: 118.15  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  99 VITDLKDTVILPikKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVF 178
Cdd:cd19481     1 LKASLREAVEAP--RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1013362348 179 SLAIKLQPSIIFIDEIDSFLRNRSSS-DHEATAMMKAQFMSLWDGLDTD 226
Cdd:cd19481    79 ERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSR 127
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 92-223 3.19e-31

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: 115.23  E-value: 3.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFEnSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFK-AIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGL 223
Cdd:cd19519    80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGL 131
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 88-317 2.85e-30

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: 119.70  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVilpikkKHLFENSRLLQ----PPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:TIGR01241  52 VTFKDVAGIDEAKEELMEIV------DFLKNPSKFTKlgakIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRS---SSDHEATAMMKAQFMSLWDGLDT--------------- 225
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGTntgviviaatnrpdv 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 226 -----------DHSCQA----LKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVReyvnstse 290
Cdd:TIGR01241 206 ldpallrpgrfDRQVVVdlpdIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAAR-------- 277

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1013362348 291 esHDEDEIRpvqQQDLHRAIEKM-----KKSK 317
Cdd:TIGR01241 278 --KNKTEIT---MNDIEEAIDRViagpeKKSR 304
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 81-319 3.62e-30

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 118.72  E-value: 3.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  81 VDPLN--MHV------TWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGC 152
Cdd:PTZ00361  165 VDPLVsvMKVdkapleSYADIGGLEQQIQEIKEAVELPLTHPELYDDIGI-KPPKGVILYGPPGTGKTLLAKAVANETSA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 153 RFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQAL 232
Cdd:PTZ00361  244 TFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDV 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 233 KQREAILKL------ILKNENVDRH---------------------------VDLLEVAQETDGFSGSDLKEMCRDAALL 279
Cdd:PTZ00361  324 KVIMATNRIesldpaLIRPGRIDRKiefpnpdektkrrifeihtskmtlaedVDLEEFIMAKDELSGADIKAICTEAGLL 403

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1013362348 280 CVREyvnstseeshdedEIRPVQQQDLHRAIEKMKKSKDA 319
Cdd:PTZ00361  404 ALRE-------------RRMKVTQADFRKAKEKVLYRKKG 430
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 92-225 1.46e-29

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: 111.06  E-value: 1.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAG-----CRFINLQPSTLTDKW 166
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKI-TPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKW 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1013362348 167 YGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDT 225
Cdd:cd19517    80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN 138
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 102-224 2.72e-29

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: 109.89  E-value: 2.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 102 DLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLA 181
Cdd:cd19529     4 ELKEAVEWPLLKPEVFKRLGI-RPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1013362348 182 IKLQPSIIFIDEIDSFLRNR-SSSDHEATAMMKAQFMSLWDGLD 224
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLE 126
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 92-223 2.81e-29

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: 110.19  E-value: 2.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLqPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGL 223
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDEL 131
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 96-224 8.00e-29

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: 108.73  E-value: 8.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  96 LDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAA 175
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGI-DLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1013362348 176 AVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLD 224
Cdd:cd19530    80 QVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE 128
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 88-285 5.13e-28

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 112.16  E-value: 5.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:PTZ00454  142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGI-DPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQAL----------- 232
Cdd:PTZ00454  221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaqTGADREVQRIL-LELLNQMDGFDQTTNVKVImatnradtldp 299

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013362348 233 -------------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVRE--YV 285
Cdd:PTZ00454  300 allrpgrldrkiefplpdrRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKnrYV 373
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 99-225 3.39e-26

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: 101.82  E-value: 3.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  99 VITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVF 178
Cdd:cd19528     1 VKRELQELVQYPVEHPDKFLKFGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1013362348 179 SLAIKLQPSIIFIDEIDSFLRNRSSS---DHEATAMMKAQFMSLWDGLDT 225
Cdd:cd19528    80 DKARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGMNT 129
ftsH CHL00176
cell division protein; Validated
 88-283 9.00e-26

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 107.83  E-value: 9.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVILpIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGA-KIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 168 GesqkLAAA----VFSLAIKLQPSIIFIDEIDSFLRNRSS-----SDHEATAMMkaQFMSLWDG---------------- 222
Cdd:CHL00176  258 G----VGAArvrdLFKKAKENSPCIVFIDEIDAVGRQRGAgigggNDEREQTLN--QLLTEMDGfkgnkgviviaatnrv 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 223 --LDTdhscqAL-----------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVRE 283
Cdd:CHL00176  332 diLDA-----ALlrpgrfdrqitvslpdrEGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARR 406
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 92-222 4.14e-25

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 99.19  E-value: 4.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDVITDLKDTVILPIKKKHLFenSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAF--SGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRsSSDHEATAMMKAQFMSLWDG 222
Cdd:cd19523    79 KILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDG 128
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
78-317 9.94e-25

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 104.35  E-value: 9.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  78 AHLVDPLNMHVTWSDIAGLDDVITDLKDTVilpikkkhlfenSRLLQP----------PKGVLLYGPPGCGKTLIAKATA 147
Cdd:COG0465   129 AKLYDEDKPKVTFDDVAGVDEAKEELQEIV------------DFLKDPekftrlgakiPKGVLLVGPPGTGKTLLAKAVA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 148 KEAGCRFINLQPSTLTDKWYGesqkLAAA----VFSLAIKLQPSIIFIDEIDSFLRNRSSS------DHEAT-----AMM 212
Cdd:COG0465   197 GEAGVPFFSISGSDFVEMFVG----VGASrvrdLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdEREQTlnqllVEM 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 213 kaqfmslwDGLDT----------------DhscQAL-----------------KQREAILKLILKNENVDRHVDLLEVAQ 259
Cdd:COG0465   273 --------DGFEGnegviviaatnrpdvlD---PALlrpgrfdrqvvvdlpdvKGREAILKVHARKKPLAPDVDLEVIAR 341

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013362348 260 ETDGFSGSDLKEMCRDAALLCVREyvNSTSeeshdedeirpVQQQDLHRAIEKM-----KKSK 317
Cdd:COG0465   342 RTPGFSGADLANLVNEAALLAARR--NKKA-----------VTMEDFEEAIDRViagpeRKSR 391
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 103-224 1.52e-24

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: 97.50  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 103 LKDTVILPIKKKHLFENSRLLQPpKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAI 182
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLR-SGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQ 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1013362348 183 KLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLD 224
Cdd:cd19526    84 SAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVE 125
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 88-226 3.73e-24

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: 96.53  E-value: 3.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKDTVilpikkKHLFENSRLLQ----PPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVV------EFLKNPEKFTKlgakIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1013362348 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR---SSSDHEATAMMKAQFMSLWDGLDTD 226
Cdd:cd19501    75 EMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgagLGGGHDEREQTLNQLLVEMDGFESN 140
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
123-320 1.88e-23

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 96.88  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 123 LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAiKLQPSIIFIDEIDSFLRNRS 202
Cdd:COG1223    32 LWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 203 SSdhEATAMMKA------QFMslwDGLDtDHSC------------QAL---------------KQREAILKLILKNENVD 249
Cdd:COG1223   111 DQ--NDVGEVKRvvnallQEL---DGLP-SGSVviaatnhpelldSALwrrfdeviefplpdkEERKEILELNLKKFPLP 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1013362348 250 RHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstseeshDEDEIRPvqqQDLHRAIEKMKKSKDAA 320
Cdd:COG1223   185 FELDLKKLAKKLEGLSGADIEKVLKTALKKAILE----------DREKVTK---EDLEEALKQRKERKKEP 242
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
78-298 3.30e-22

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 97.41  E-value: 3.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  78 AHLVDPLNMHVTWSDIAGLDDVITDLKDTVilpikkKHLFENSRLLQ----PPKGVLLYGPPGCGKTLIAKATAKEAGCR 153
Cdd:PRK10733  139 ARMLTEDQIKTTFADVAGCDEAKEEVAELV------EYLREPSRFQKlggkIPKGVLMVGPPGTGKTLLAKAIAGEAKVP 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 154 FINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSS---SDHEATAMMKAQFMSLWDGLDTDHSCQ 230
Cdd:PRK10733  213 FFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFEGNEGII 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 231 AL------------------------------KQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLC 280
Cdd:PRK10733  293 VIaatnrpdvldpallrpgrfdrqvvvglpdvRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFA 372

                         250       260
                  ....*....|....*....|
gi 1013362348 281 VR--EYVNSTSEESHDEDEI 298
Cdd:PRK10733  373 ARgnKRVVSMVEFEKAKDKI 392
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 99-225 1.45e-20

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: 86.80  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  99 VITDLKDTVILPIKKKHLFenSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVF 178
Cdd:cd19527     1 VKKEILDTIQLPLEHPELF--SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1013362348 179 SLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMK--AQFMSLWDGLDT 225
Cdd:cd19527    79 QKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDRvvSQLLAELDGMSS 127
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 114-199 9.80e-17

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: 76.03  E-value: 9.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 114 KHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEA---GCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKL---QPS 187
Cdd:cd00009     7 IEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAekaKPG 86

                          90
                  ....*....|..
gi 1013362348 188 IIFIDEIDSFLR 199
Cdd:cd00009    87 VLFIDEIDSLSR 98
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 92-220 3.02e-15

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: 72.02  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  92 DIAGLDDvitdLKDtvILPIKKKHLFENSRL--LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGE 169
Cdd:cd19507     1 DVGGLDN----LKD--WLKKRKAAFSKQASAygLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1013362348 170 SQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR-SSSDHEATAMMKAQFMSlW 220
Cdd:cd19507    75 SESRLRQMIQTAEAIAPCVLWIDEIEKGFSNAdSKGDSGTSSRVLGTFLT-W 125
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 125-219 7.09e-12

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: 62.39  E-value: 7.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  125 PPKGVLLYGPPGCGKTLIAKATAKEAGC-----------------RFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPS 187
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPpgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1013362348  188 IIFIDEIDSFLRNRSSSDHEATAMMKAQFMSL 219
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK 112
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 252-291 4.75e-10

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: 54.08  E-value: 4.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1013362348 252 VDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEE 291
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 119-204 2.94e-09

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: 55.57  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 119 NSRLLQPP----------KGVLLYGPPGCGKTLIAKATAKEAGCR---FINlQPSTLtDKWYGESQKLAAAVFSLAIKLQ 185
Cdd:cd19504    18 ASRVFPPEiveqlgckhvKGILLYGPPGTGKTLMARQIGKMLNARepkIVN-GPEIL-NKYVGESEANIRKLFADAEEEQ 95

                          90       100
                  ....*....|....*....|....*..
gi 1013362348 186 PS--------IIFIDEIDSFLRNRSSS 204
Cdd:cd19504    96 RRlgansglhIIIFDEIDAICKQRGSM 122
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 108-193 3.51e-09

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 55.23  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 108 ILPIKKKHLFENSRLLqppKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGES--QKLAAAVFSLAIKLQ 185
Cdd:cd19506    11 ILPLGSQAVHEKAPLV---KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQ 87


                  ....*...
gi 1013362348 186 PSIIFIDE 193
Cdd:cd19506    88 PSVIWIGD 95
ycf46 CHL00195
Ycf46; Provisional
 88-220 1.41e-08

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 55.80  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  88 VTWSDIAGLDDVITDLKdtvilpiKKKHLFENSRL---LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTD 164
Cdd:CHL00195  225 EKISDIGGLDNLKDWLK-------KRSTSFSKQASnygLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFG 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1013362348 165 KWYGESQKLAAAVFSLAIKLQPSIIFIDEID-SFLRNRSSSDHEATAMMKAQFMSlW 220
Cdd:CHL00195  298 GIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFIT-W 353
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 129-198 4.12e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 54.32  E-value: 4.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKwygESQKLAAAVFSLAIKLQPSIIFIDEI--------DSFL 198
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTSGVK---DLREVIEEARQRRSAGRRTILFIDEIhrfnkaqqDALL 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 126-210 4.91e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 52.00  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 126 PKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYgesqkLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSD 205
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGY-----VGRDVESIIRDLVEGIVFIDEIDKIAKRGGSSG 120


                  ....*
gi 1013362348 206 HEATA 210
Cdd:cd19498   121 PDVSR 125
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 119-204 1.32e-07

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: 51.29  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 119 NSRLLQPPKGVLLYGPPGCGKTLIAKATAKE---------AGCRFINLQPSTLTDKWYGESQKLAAAVFSLA---IKLQP 186
Cdd:cd19508    45 NTNLITWNRLVLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIqelIDDKD 124

                          90       100
                  ....*....|....*....|
gi 1013362348 187 SIIF--IDEIDSFLRNRSSS 204
Cdd:cd19508   125 ALVFvlIDEVESLAAARSAS 144
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 129-198 7.31e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.44  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLqpstltdkwygesqklaAAVFS--------------LAIKLQPSIIFIDEI 194
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVAL-----------------SAVTSgvkdirevieeareRRAYGRRTILFVDEI 114

                          90
                  ....*....|..
gi 1013362348 195 --------DSFL 198
Cdd:COG2256   115 hrfnkaqqDALL 126
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 127-203 1.23e-06

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: 47.52  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 127 KGVLLYGPPGCGKTLIAKATAKEAGCRFinlqpSTLTDkwyGESQKLAA-------AVFSLAIKLQPS-IIFIDEIDSFL 198
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDY-----AIMTG---GDVAPMGRegvtaihKVFDWANTSRRGlLLFVDEADAFL 94


                  ....*
gi 1013362348 199 RNRSS 203
Cdd:cd19512    95 RKRST 99
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 129-195 3.07e-06

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: 47.59  E-value: 3.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY-GES-----QKL-AAAVFSLAiKLQPSIIFIDEID 195
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYvGEDvenilLKLlQAADYDVE-RAQRGIVYIDEID 125
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 127-218 4.42e-06

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: 45.81  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 127 KGVLLYGPPGCGKTLIAKATAKEAGCRF--INLQPSTLTDkwygESQKLAaavfsLAIKLQPSIIFIDEIDSFLrnrSSS 204
Cdd:cd19510    24 RGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVLTD----DRLNHL-----LNTAPKQSIILLEDIDAAF---ESR 91

                          90
                  ....*....|....
gi 1013362348 205 DHEATAMMKAQFMS 218
Cdd:cd19510    92 EHNKKNPSAYGGLS 105
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 129-195 9.32e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.70  E-value: 9.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQ------PSTLT-----DKWYGESQKLAAAVFSlaiklqpSIIFIDEID 195
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILgtyiyDQQTGEFEFRPGPLFA-------NVLLADEIN 104
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
129-195 1.97e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.92  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 129 VLLYGPPGCGKTLIAKATAkeagcRFINLqP------STLTDKWY-GES-----QKL-AAAVFSLAiKLQPSIIFIDEID 195
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLA-----RILDV-PfaiadaTTLTEAGYvGEDvenilLKLlQAADYDVE-KAQRGIVYIDEID 183
PRK04195 PRK04195
replication factor C large subunit; Provisional
 124-151 3.18e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 45.30  E-value: 3.18e-05
                          10        20
                  ....*....|....*....|....*...
gi 1013362348 124 QPPKGVLLYGPPGCGKTLIAKATAKEAG 151
Cdd:PRK04195   37 KPKKALLLYGPPGVGKTSLAHALANDYG 64
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 129-194 4.82e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 42.87  E-value: 4.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGcrfINLQPST--LTDKwygeSQKLAAavfsLAIKLQP-SIIFIDEI 194
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMG---VNIRITSgpAIER----PGDLAA----ILTNLEPgDVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
129-194 8.28e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.58  E-value: 8.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKE--AGCRFIN---LQ-PSTLtdkwygesqklaAAVFSLaikLQP-SIIFIDEI 194
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEmgVNIRITSgpaLEkPGDL------------AAILTN---LEEgDVLFIDEI 111
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 126-195 2.38e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 41.03  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 126 PKGV-LLYGPPGCGKTLIAKATAKEAG---CRFINLQPSTLTDKW--------------YGESQKLAAAVfslaIKLQPS 187
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMEEHsvsrligappgyvgYEEGGQLTEAV----RRKPYS 77


                  ....*...
gi 1013362348 188 IIFIDEID 195
Cdd:pfam07724  78 IVLIDEIE 85
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 129-195 3.54e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 41.96  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 129 VLLYGPPGCGKTLIAKATAkeagcRFINLqP------STLTDKWY-GES-----QKL-AAAVFSLAiKLQPSIIFIDEID 195
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTLA-----RILDV-PfaiadaTTLTEAGYvGEDvenilLKLlQAADYDVE-KAERGIIYIDEID 184
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 129-194 4.04e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.52  E-value: 4.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLtdkwygESQKLAAAVFSLaikLQP-SIIFIDEI 194
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL------EKPGDLAAILTN---LEEgDVLFIDEI 90
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
127-151 4.43e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 4.43e-04
                          10        20
                  ....*....|....*....|....*
gi 1013362348 127 KGVLLYGPPGCGKTLIAKATAKEAG 151
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELG 89
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 122-160 8.14e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 8.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1013362348 122 LLQPPKGVLLYGPPGCGKTLIAKATAKEAG------CRFINLQPS 160
Cdd:COG1401   217 ALKTKKNVILAGPPGTGKTYLARRLAEALGgedngrIEFVQFHPS 261
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
108-194 9.33e-04

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 40.70  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 108 ILPIKKKHLFEN-SRLLQPPKGVLLYGPPGCGKTLIAKATAKE-AGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKlq 185
Cdd:COG1373     1 VMIMIKRKILDKlLKLLDNRKAVVITGPRQVGKTTLLKQLAKElENILYINLDDPRLRALAEEDPDDLLEALKELYPG-- 78


                  ....*....
gi 1013362348 186 PSIIFIDEI 194
Cdd:COG1373    79 KTYLFLDEI 87
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 129-168 1.05e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT-----DKWYG 168
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVYSrnpddDFWDG 45
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 123-198 1.68e-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: 38.38  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 123 LQPPKG--VLLYGPPGCGKTLIAKATA----KEAGCRFINLQPSTLTDKW-------------YGESQKLAAAvfsLAIK 183
Cdd:cd00267    20 LTLKAGeiVALVGPNGSGKSTLLRAIAgllkPTSGEILIDGKDIAKLPLEelrrrigyvpqlsGGQRQRVALA---RALL 96

                          90
                  ....*....|....*
gi 1013362348 184 LQPSIIFIDEIDSFL 198
Cdd:cd00267    97 LNPDLLLLDEPTSGL 111
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 129-194 2.49e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 2.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFI-----NLQ-PSTLtdkwygesqklaAAVFSlaiKLQP-SIIFIDEI 194
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRitsgpAIEkPGDL------------AAILT---NLEEgDVLFIDEI 114
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
124-149 3.40e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 39.06  E-value: 3.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1013362348 124 QPPKGVLLYGPPGCGKTLIAKATAKE 149
Cdd:COG1474    49 ERPSNVLIYGPTGTGKTAVAKYVLEE 74
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 124-150 4.28e-03

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 38.38  E-value: 4.28e-03
                          10        20
                  ....*....|....*....|....*..
gi 1013362348 124 QPPKGVLLYGPPGCGKTLIAKATAKEA 150
Cdd:TIGR02928  38 SRPSNVFIYGKTGTGKTAVTKYVMKEL 64
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 129-156 4.73e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 36.85  E-value: 4.73e-03
                          10        20
                  ....*....|....*....|....*...
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEAGCRFIN 156
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFID 29
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 129-145 4.81e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.51  E-value: 4.81e-03
                          10
                  ....*....|....*..
gi 1013362348 129 VLLYGPPGCGKTLIAKA 145
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
89-148 5.29e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 38.25  E-value: 5.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348  89 TWSDIAGLDDVITDLKdtvilpikkkHLFENSRLlqpPKGVLLYGPPGCGKTLIAKATAK 148
Cdd:COG2812     8 TFDDVVGQEHVVRTLK----------NALASGRL---AHAYLFTGPRGVGKTTLARILAK 54
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
126-153 5.35e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 38.03  E-value: 5.35e-03
                          10        20
                  ....*....|....*....|....*...
gi 1013362348 126 PKGVLLYGPPGCGKTLIAKATAKEAGCR 153
Cdd:COG0470    18 PHALLLHGPPGIGKTTLALALARDLLCE 45
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
127-153 7.68e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 37.45  E-value: 7.68e-03
                          10        20
                  ....*....|....*....|....*..
gi 1013362348 127 KGVLLYGPPGCGKTLIAKATAKEAgCR 153
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEA-CR 125
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 127-151 7.75e-03

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 37.67  E-value: 7.75e-03
                          10        20
                  ....*....|....*....|....*
gi 1013362348 127 KGVLLYGPPGCGKTLIAKATAKEAG 151
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELG 75
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 123-208 8.87e-03

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: 36.58  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 123 LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKW--------------YGESQKLAAAVFSLAIKLQPSI 188
Cdd:cd19505     9 LSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCI 88

                          90       100
                  ....*....|....*....|
gi 1013362348 189 IFIDEIDSFLRNRSSSDHEA 208
Cdd:cd19505    89 IWIPNIHELNVNRSTQNLEE 108
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 129-219 8.91e-03

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: 35.56  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013362348 129 VLLYGPPGCGKTLIAKATAKEA---GCRFINLqpSTLtdkwygesQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSsd 205
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFI--SFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQG-- 68

                          90
                  ....*....|....
gi 1013362348 206 hEATAMMKAQFMSL 219
Cdd:cd01120    69 -DRSSELLEDLAKL 81
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 92-155 9.17e-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: 36.77  E-value: 9.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1013362348  92 DIAGLDDVitdlKDTVI--LPIKKkhlfensrLLQPPKG--VLLYGPPGCGKTLIAKATAKEAGCRFI 155
Cdd:cd19500    11 DHYGLEDV----KERILeyLAVRK--------LKGSMKGpiLCLVGPPGVGKTSLGKSIARALGRKFV 66
 
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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