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Conserved domains on  [gi|78097112|ref|NP_001030174|]
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outer mitochondrial transmembrane helix translocase [Rattus norvegicus]

Protein Classification

outer mitochondrial transmembrane helix translocase( domain architecture ID 15181063)

outer mitochondrial transmembrane helix translocase (ATAD1) is an outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
92-257 3.43e-120

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: 344.02  E-value: 3.43e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRM 251
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160

                ....*.
gi 78097112 252 PTRFHI 257
Cdd:cd19520 161 PKRFHI 166
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
4-344 7.99e-68

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: 218.63  E-value: 7.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   4 AEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDP 83
Cdd:COG0464  70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  84 LNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:COG0464 150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDhscqVIVMGATNRPQDL 243
Cdd:COG0464 229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLL 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 244 DSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVnstseesh 323
Cdd:COG0464 305 DPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGR-------- 376
                       330       340
                ....*....|....*....|.
gi 78097112 324 dedeiRPVQQQDLHRAIEKMK 344
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; ...
92-257 3.43e-120

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: 344.02  E-value: 3.43e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRM 251
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160

                ....*.
gi 78097112 252 PTRFHI 257
Cdd:cd19520 161 PKRFHI 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
88-350 1.00e-86

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 264.95  E-value: 1.00e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:COG1222  75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSS-DHEATAMMKAQFMSLWDGLDTDHScqVIVMGATNRPQDLDSA 246
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDPA 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 247 IMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstsees 322
Cdd:COG1222 232 LLR--PGRFdrviEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE--------- 300
                       250       260
                ....*....|....*....|....*...
gi 78097112 323 hDEDEIRpvqQQDLHRAIEKMKKSKDAA 350
Cdd:COG1222 301 -GRDTVT---MEDLEKAIEKVKKKTETA 324
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
4-344 7.99e-68

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: 218.63  E-value: 7.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   4 AEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDP 83
Cdd:COG0464  70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  84 LNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:COG0464 150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDhscqVIVMGATNRPQDL 243
Cdd:COG0464 229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLL 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 244 DSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVnstseesh 323
Cdd:COG0464 305 DPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGR-------- 376
                       330       340
                ....*....|....*....|.
gi 78097112 324 dedeiRPVQQQDLHRAIEKMK 344
Cdd:COG0464 377 -----EPVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
88-348 4.58e-66

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 213.93  E-value: 4.58e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:PRK03992 128 VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEAT-AMMkaQFMSLWDGLDTdhSCQVIVMGATNRPQD 242
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsgTSGDREVQrTLM--QLLAEMDGFDP--RGNVKIIAATNRIDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  243 LDSAIMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnst 318
Cdd:PRK03992 283 LDPAILR--PGRFdriiEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD----- 355
                        250       260       270
                 ....*....|....*....|....*....|
gi 78097112  319 seeshDEDEIRpvqQQDLHRAIEKMKKSKD 348
Cdd:PRK03992 356 -----DRTEVT---MEDFLKAIEKVMGKEE 377
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
88-344 6.86e-57

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: 189.24  E-value: 6.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQVIvmGATNRPQDL 243
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsgTSGDREVQRTL-MQLLAELDGFDPRGNVKVI--AATNRPDIL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   244 DSAIMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnsts 319
Cdd:TIGR01242 275 DPALLR--PGRFdriiEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIRE------ 346
                         250       260
                  ....*....|....*....|....*
gi 78097112   320 eeshdedEIRPVQQQDLHRAIEKMK 344
Cdd:TIGR01242 347 -------ERDYVTMDDFIKAVEKVL 364
cell_div_CdvC NF041006
cell division protein CdvC;
88-346 6.72e-55

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 184.17  E-value: 6.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFEnsrlLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFP----LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  168 GESQKLAAAVFSLAIKL-----QPSIIFIDEIDSFLrNRSSSDHEATAMMKAQFMSLWDGL-DTDHSCQVIVMGATNRPQ 241
Cdd:NF041006 176 GEAEKNVAKIFKKAREKskeegKPAIIFIDEIDALL-GVYSSEVGGEVRVRNQFLKEMDGLqDKSENYHVYVIGATNKPW 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  242 DLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNStsee 321
Cdd:NF041006 255 RLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK---- 330
                        250       260
                 ....*....|....*....|....*
gi 78097112  322 shDEDEIRPVQQQDLHRAIEKMKKS 346
Cdd:NF041006 331 --GLGEPRPITMEDFKEVLKIRKPS 353
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
129-257 1.20e-46

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: 155.06  E-value: 1.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEA 208
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 78097112   209 TAMMKAQFMSLWDGLDTDHScQVIVMGATNRPQDLDSAIMRRMPTRFHI 257
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNS-KVIVIAATNRPDKLDPALLGRFDRIIEF 128
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
125-254 1.68e-16

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: 75.87  E-value: 1.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    125 PPKGVLLYGPPGCGKTLIAKATAKEAGC-----------------RFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPS 187
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPpgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78097112    188 IIFIDEIDSFLRNRSSSDheataMMKAQFMSLWDGLDTDHSCQVIvmGATNRPQDLDSAIMRRMPTR 254
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVI--LTTNDEKDLGPALLRRRFDR 140
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
282-321 3.95e-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: 54.47  E-value: 3.95e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 78097112   282 VDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEE 321
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; ...
92-257 3.43e-120

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: 344.02  E-value: 3.43e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRM 251
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160

                ....*.
gi 78097112 252 PTRFHI 257
Cdd:cd19520 161 PKRFHI 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
88-350 1.00e-86

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 264.95  E-value: 1.00e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:COG1222  75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSS-DHEATAMMKAQFMSLWDGLDTDHScqVIVMGATNRPQDLDSA 246
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDPA 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 247 IMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstsees 322
Cdd:COG1222 232 LLR--PGRFdrviEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE--------- 300
                       250       260
                ....*....|....*....|....*...
gi 78097112 323 hDEDEIRpvqQQDLHRAIEKMKKSKDAA 350
Cdd:COG1222 301 -GRDTVT---MEDLEKAIEKVKKKTETA 324
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
93-257 4.57e-76

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: 231.86  E-value: 4.57e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  93 IAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQK 172
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLR--GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 173 LAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRMP 252
Cdd:cd19509  79 IVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFE 158

                ....*
gi 78097112 253 TRFHI 257
Cdd:cd19509 159 KRIYI 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
4-344 7.99e-68

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: 218.63  E-value: 7.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   4 AEAFSRPLSRNEVVGLIFRLTIFGAVTYFTIKWMVDAIDPTRKQKVEAQKQAEKLMKQIGVKNVKLSEYEMSIAAHLVDP 83
Cdd:COG0464  70 LLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  84 LNMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:COG0464 150 ELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDhscqVIVMGATNRPQDL 243
Cdd:COG0464 229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLL 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 244 DSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVnstseesh 323
Cdd:COG0464 305 DPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGR-------- 376
                       330       340
                ....*....|....*....|.
gi 78097112 324 dedeiRPVQQQDLHRAIEKMK 344
Cdd:COG0464 377 -----EPVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
88-348 4.58e-66

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 213.93  E-value: 4.58e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:PRK03992 128 VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEAT-AMMkaQFMSLWDGLDTdhSCQVIVMGATNRPQD 242
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsgTSGDREVQrTLM--QLLAEMDGFDP--RGNVKIIAATNRIDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  243 LDSAIMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnst 318
Cdd:PRK03992 283 LDPAILR--PGRFdriiEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD----- 355
                        250       260       270
                 ....*....|....*....|....*....|
gi 78097112  319 seeshDEDEIRpvqQQDLHRAIEKMKKSKD 348
Cdd:PRK03992 356 -----DRTEVT---MEDFLKAIEKVMGKEE 377
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
92-257 1.39e-57

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: 184.67  E-value: 1.39e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLR--APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRM 251
Cdd:cd19524  79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRF 158

                ....*.
gi 78097112 252 PTRFHI 257
Cdd:cd19524 159 TKRVYV 164
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
88-344 6.86e-57

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: 189.24  E-value: 6.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQVIvmGATNRPQDL 243
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsgTSGDREVQRTL-MQLLAELDGFDPRGNVKVI--AATNRPDIL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   244 DSAIMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnsts 319
Cdd:TIGR01242 275 DPALLR--PGRFdriiEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIRE------ 346
                         250       260
                  ....*....|....*....|....*
gi 78097112   320 eeshdedEIRPVQQQDLHRAIEKMK 344
Cdd:TIGR01242 347 -------ERDYVTMDDFIKAVEKVL 364
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
85-257 4.72e-56

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: 181.34  E-value: 4.72e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  85 NMHVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTD 164
Cdd:cd19525  16 GPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR--GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 165 KWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLD 244
Cdd:cd19525  94 KWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEID 173
                       170
                ....*....|...
gi 78097112 245 SAIMRRMPTRFHI 257
Cdd:cd19525 174 EAARRRLVKRLYI 186
cell_div_CdvC NF041006
cell division protein CdvC;
88-346 6.72e-55

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 184.17  E-value: 6.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFEnsrlLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFP----LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  168 GESQKLAAAVFSLAIKL-----QPSIIFIDEIDSFLrNRSSSDHEATAMMKAQFMSLWDGL-DTDHSCQVIVMGATNRPQ 241
Cdd:NF041006 176 GEAEKNVAKIFKKAREKskeegKPAIIFIDEIDALL-GVYSSEVGGEVRVRNQFLKEMDGLqDKSENYHVYVIGATNKPW 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  242 DLDSAIMRRMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNStsee 321
Cdd:NF041006 255 RLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK---- 330
                        250       260
                 ....*....|....*....|....*
gi 78097112  322 shDEDEIRPVQQQDLHRAIEKMKKS 346
Cdd:NF041006 331 --GLGEPRPITMEDFKEVLKIRKPS 353
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
54-346 1.77e-54

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: 190.50  E-value: 1.77e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    54 QAEKLMKQIgVKNVKLSEYEMSIAAHLVDPLNM--------HVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQP 125
Cdd:TIGR01243 409 EAEEIPAEV-LKELKVTMKDFMEALKMVEPSAIrevlvevpNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGI-RP 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   126 PKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSD 205
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   206 HEA-TAMMKAQFMSLWDGLDTDHScqVIVMGATNRPQDLDSAIMRrmPTRF----HINQPALKQREAILKLILKNENVDR 280
Cdd:TIGR01243 567 DTSvTDRIVNQLLTEMDGIQELSN--VVVIAATNRPDILDPALLR--PGRFdrliLVPPPDEEARKEIFKIHTRSMPLAE 642
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78097112   281 HVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIRP-----VQQQDLHRAIEKMKKS 346
Cdd:TIGR01243 643 DVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFlkdlkVEMRHFLEALKKVKPS 713
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
92-255 3.67e-54

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: 175.56  E-value: 3.67e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGL-KPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHscQVIVMGATNRPQDLDSAIMRrm 251
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG--KVVVIAATNRPDAIDPALRR-- 155

                ....
gi 78097112 252 PTRF 255
Cdd:cd19503 156 PGRF 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
88-358 1.90e-53

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: 187.81  E-value: 1.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFEnsRL-LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKW 166
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFE--HLgIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   167 YGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLdtDHSCQVIVMGATNRPQDLDSA 246
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGL--KGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   247 ImrRMPTRFH----INQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTS--- 319
Cdd:TIGR01243 331 L--RRPGRFDreivIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKinf 408
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 78097112   320 --EESHDE--DEIRpVQQQDLHraiEKMKKSKDAAFQSVLTHV 358
Cdd:TIGR01243 409 eaEEIPAEvlKELK-VTMKDFM---EALKMVEPSAIREVLVEV 447
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
87-257 3.98e-52

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: 170.81  E-value: 3.98e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  87 HVTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKW 166
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNR--KPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 167 YGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHScQVIVMGATNRPQDLDSA 246
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQ-GVLVLGATNIPWQLDSA 159
                       170
                ....*....|.
gi 78097112 247 IMRRMPTRFHI 257
Cdd:cd19521 160 IRRRFEKRIYI 170
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
88-347 1.39e-47

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: 167.85  E-value: 1.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    88 VTWSDIAGLDDVITDLKDTVilpikkKHLFENSRLLQ----PPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:TIGR01241  52 VTFKDVAGIDEAKEELMEIV------DFLKNPSKFTKlgakIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRS---SSDHEATAMMKAQFMSLWDGLDTdhSCQVIVMGATNRP 240
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGT--NTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   241 QDLDSAIMRrmPTRFH----INQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVReyvn 316
Cdd:TIGR01241 204 DVLDPALLR--PGRFDrqvvVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAAR---- 277
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 78097112   317 stseesHDEDEIRpvqQQDLHRAIEKM-----KKSK 347
Cdd:TIGR01241 278 ------KNKTEIT---MNDIEEAIDRViagpeKKSR 304
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
129-257 1.20e-46

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: 155.06  E-value: 1.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEA 208
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 78097112   209 TAMMKAQFMSLWDGLDTDHScQVIVMGATNRPQDLDSAIMRRMPTRFHI 257
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNS-KVIVIAATNRPDKLDPALLGRFDRIIEF 128
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
89-255 4.74e-46

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: 154.80  E-value: 4.74e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  89 TWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYG 168
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGI-EPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 169 ESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQVIvmGATNRPQDLD 244
Cdd:cd19502  80 EGARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsgTGGDREVQRTM-LELLNQLDGFDPRGNIKVI--MATNRPDILD 156
                       170
                ....*....|.
gi 78097112 245 SAIMRrmPTRF 255
Cdd:cd19502 157 PALLR--PGRF 165
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
92-257 4.15e-45

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: 152.45  E-value: 4.15e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRllQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR--RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNR-SSSDHEATAMMKAQFMSLWDGL-----DTDHSCQVIVMGATNRPQDLDS 245
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggaseNDDPSKMVMVLAATNFPWDIDE 158
                       170
                ....*....|..
gi 78097112 246 AIMRRMPTRFHI 257
Cdd:cd19522 159 ALRRRLEKRIYI 170
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
103-255 4.85e-44

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: 149.36  E-value: 4.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 103 LKDTVILPIKKKHLFenSRL-LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLA 181
Cdd:cd19511   5 LKEAVEWPLKHPDAF--KRLgIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78097112 182 IKLQPSIIFIDEIDSFLRNRSSSDH-EATAMMKAQFMSLWDGLDTdhSCQVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSsGVTDRVVSQLLTELDGIES--LKGVVVIAATNRPDMIDPALLR--PGRL 153
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
99-255 6.78e-43

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: 146.27  E-value: 6.78e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  99 VITDLKDTVILPikKKHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVF 178
Cdd:cd19481   1 LKASLREAVEAP--RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIF 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78097112 179 SLAIKLQPSIIFIDEIDSFLRNRSSS-DHEATAMMKAQFMSLWDGLDTDHscQVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19481  79 ERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRS--KVLVIAATNRPDLLDPALLR--PGRF 152
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
88-323 1.38e-42

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: 154.87  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCR----------FINL 157
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELPFLHPELYREYGL-KPPKGVLLYGPPGCGKTLIAKAVANSLAARigaegggksyFLNI 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   158 QPSTLTDKWYGESQKLAAAVFSLAIKL----QPSIIFIDEIDSFLRNRS---SSDHEATAMmkAQFMSLWDGLDTDHScq 230
Cdd:TIGR03689 258 KGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGsgvSSDVETTVV--PQLLAEIDGVESLDN-- 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   231 VIVMGATNRPQDLDSAIMR--RMPTRFHINQPALKQREAILklilknenvDRHV-DLLEVAQETDGFSGSDlkEMCRDAA 307
Cdd:TIGR03689 334 VIVIGASNREDMIDPAILRpgRLDVKIRIERPDAEAAADIF---------AKYLtDDLPLPEDLAAHDGDR--EATAAAL 402
                         250
                  ....*....|....*.
gi 78097112   308 LLCVREYVNSTSEESH 323
Cdd:TIGR03689 403 IQRVVDALYARSEANR 418
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
92-255 1.56e-40

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: 140.26  E-value: 1.56e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFEnSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFK-AIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTdhSCQVIVMGATNRPQDLDSAImrRM 251
Cdd:cd19519  80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQ--RAHVIVMAATNRPNSIDPAL--RR 155

                ....
gi 78097112 252 PTRF 255
Cdd:cd19519 156 FGRF 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
81-355 2.45e-40

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 147.22  E-value: 2.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   81 VDPLN--MHV------TWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGC 152
Cdd:PTZ00361 165 VDPLVsvMKVdkapleSYADIGGLEQQIQEIKEAVELPLTHPELYDDIGI-KPPKGVILYGPPGTGKTLLAKAVANETSA 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  153 RFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDT-DHSCQV 231
Cdd:PTZ00361 244 TFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGfDSRGDV 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  232 IVMGATNRPQDLDSAIMR--RMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALL 309
Cdd:PTZ00361 324 KVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLL 403
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 78097112  310 CVREyvnstseeshdedEIRPVQQQDLHRAIEKMKKSKDAAFQSVL 355
Cdd:PTZ00361 404 ALRE-------------RRMKVTQADFRKAKEKVLYRKKGNIPEGL 436
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
78-347 2.71e-40

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 149.42  E-value: 2.71e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  78 AHLVDPLNMHVTWSDIAGLDDVITDLKDTVilpikkkhlfenSRLLQP----------PKGVLLYGPPGCGKTLIAKATA 147
Cdd:COG0465 129 AKLYDEDKPKVTFDDVAGVDEAKEELQEIV------------DFLKDPekftrlgakiPKGVLLVGPPGTGKTLLAKAVA 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 148 KEAGCRFINLQPSTLTDKWYGesqkLAAA----VFSLAIKLQPSIIFIDEIDSFLRNRSSS------DHEAT-----AMM 212
Cdd:COG0465 197 GEAGVPFFSISGSDFVEMFVG----VGASrvrdLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdEREQTlnqllVEM 272
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 213 kaqfmslwDGLDTDHScqVIVMGATNRPQDLDSAIMRrmPTRF----HINQPALKQREAILKLILKNENVDRHVDLLEVA 288
Cdd:COG0465 273 --------DGFEGNEG--VIVIAATNRPDVLDPALLR--PGRFdrqvVVDLPDVKGREAILKVHARKKPLAPDVDLEVIA 340
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78097112 289 QETDGFSGSDLKEMCRDAALLCVREyvNSTSeeshdedeirpVQQQDLHRAIEKM-----KKSK 347
Cdd:COG0465 341 RRTPGFSGADLANLVNEAALLAARR--NKKA-----------VTMEDFEEAIDRViagpeRKSR 391
ftsH CHL00176
cell division protein; Validated
88-313 1.12e-39

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 148.66  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKDTVILpIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGA-KIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  168 GesqkLAAA----VFSLAIKLQPSIIFIDEIDSFLRNRSS-----SDHEATAMMkaQFMSLWDGL--DTDhscqVIVMGA 236
Cdd:CHL00176 258 G----VGAArvrdLFKKAKENSPCIVFIDEIDAVGRQRGAgigggNDEREQTLN--QLLTEMDGFkgNKG----VIVIAA 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  237 TNRPQDLDSAIMRrmPTRFH----INQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVR 312
Cdd:CHL00176 328 TNRVDILDAALLR--PGRFDrqitVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTAR 405

                 .
gi 78097112  313 E 313
Cdd:CHL00176 406 R 406
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
92-255 1.14e-38

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: 135.71  E-value: 1.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAG-----CRFINLQPSTLTDKW 166
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKI-TPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 167 YGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTdhSCQVIVMGATNRPQDLDSA 246
Cdd:cd19517  80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN--RGQVVVIGATNRPDALDPA 157

                ....*....
gi 78097112 247 ImrRMPTRF 255
Cdd:cd19517 158 L--RRPGRF 164
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
123-350 3.90e-38

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 136.55  E-value: 3.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 123 LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAiKLQPSIIFIDEIDSFLRNRS 202
Cdd:COG1223  32 LWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRG 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 203 SSdhEATAMMKA------QFMslwDGLDTDhscqVIVMGATNRPQDLDSAIMRRMPTRFHINQPALKQREAILKLILKNE 276
Cdd:COG1223 111 DQ--NDVGEVKRvvnallQEL---DGLPSG----SVVIAATNHPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKF 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78097112 277 NVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREyvnstseeshDEDEIRPvqqQDLHRAIEKMKKSKDAA 350
Cdd:COG1223 182 PLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILE----------DREKVTK---EDLEEALKQRKERKKEP 242
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
88-315 3.95e-38

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 140.67  E-value: 3.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY 167
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGI-DPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  168 GESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR----SSSDHEATAMMkAQFMSLWDGLDTDHSCQVIVmgATNRPQDL 243
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaqTGADREVQRIL-LELLNQMDGFDQTTNVKVIM--ATNRADTL 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78097112  244 DSAIMR--RMPTRFHINQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVRE--YV 315
Cdd:PTZ00454 298 DPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKnrYV 373
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
92-249 2.72e-37

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: 132.14  E-value: 2.72e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFENSRLLqPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGL--DTDHSCQVIVMGATNRPQDLDSAIMR 249
Cdd:cd19518  80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnEKTAGGPVLVIGATNRPDSLDPALRR 159
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
96-255 3.41e-37

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: 131.46  E-value: 3.41e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  96 LDDVITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAA 175
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGI-DLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 176 AVFSLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHscQVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19530  80 QVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERS--NVFVIAATNRPDIIDPAMLR--PGRL 155
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
102-255 4.44e-37

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: 131.08  E-value: 4.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 102 DLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLA 181
Cdd:cd19529   4 ELKEAVEWPLLKPEVFKRLGI-RPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78097112 182 IKLQPSIIFIDEIDSFLRNR-SSSDHEATAMMKAQFMSLWDGLDTDHscQVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMN--GVVVIAATNRPDIIDPALLR--AGRF 153
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
88-255 6.33e-36

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: 128.50  E-value: 6.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  88 VTWSDIAGLDDVITDLKDTVilpikkKHLFENSRLLQ----PPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLT 163
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVV------EFLKNPEKFTKlgakIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 164 DKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR---SSSDHEATAMMKAQFMSLWDGLDTDHscQVIVMGATNRP 240
Cdd:cd19501  75 EMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgagLGGGHDEREQTLNQLLVEMDGFESNT--GVIVIAATNRP 152
                       170
                ....*....|....*
gi 78097112 241 QDLDSAIMRrmPTRF 255
Cdd:cd19501 153 DVLDPALLR--PGRF 165
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
99-254 2.93e-35

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: 126.47  E-value: 2.93e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  99 VITDLKDTVILPIKKKHLFENSRLlQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVF 178
Cdd:cd19528   1 VKRELQELVQYPVEHPDKFLKFGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIF 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78097112 179 SLAIKLQPSIIFIDEIDSFLRNRSSS---DHEATAMMKAQFMSLWDGLDTDHScqVIVMGATNRPQDLDSAIMRrmPTR 254
Cdd:cd19528  80 DKARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGMNTKKN--VFIIGATNRPDIIDPAILR--PGR 154
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
78-328 2.38e-34

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 133.62  E-value: 2.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   78 AHLVDPLNMHVTWSDIAGLDDVITDLKDTVilpikkKHLFENSRLLQ----PPKGVLLYGPPGCGKTLIAKATAKEAGCR 153
Cdd:PRK10733 139 ARMLTEDQIKTTFADVAGCDEAKEEVAELV------EYLREPSRFQKlggkIPKGVLMVGPPGTGKTLLAKAIAGEAKVP 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  154 FINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSS---SDHEATAMMKAQFMSLWDGLDTDHScq 230
Cdd:PRK10733 213 FFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFEGNEG-- 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  231 VIVMGATNRPQDLDSAIMRrmPTRFH----INQPALKQREAILKLILKNENVDRHVDLLEVAQETDGFSGSDLKEMCRDA 306
Cdd:PRK10733 291 IIVIAATNRPDVLDPALLR--PGRFDrqvvVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEA 368
                        250       260
                 ....*....|....*....|....
gi 78097112  307 ALLCVR--EYVNSTSEESHDEDEI 328
Cdd:PRK10733 369 ALFAARgnKRVVSMVEFEKAKDKI 392
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
92-257 2.55e-34

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: 124.23  E-value: 2.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDVITDLKDTVILPIKKKHLFenSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQ 171
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAF--SGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 172 KLAAAVFSLAIKLQPSIIFIDEIDSFLRNRsSSDHEATAMMKAQFMSLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRRM 251
Cdd:cd19523  79 KILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYF 157

                ....*.
gi 78097112 252 PTRFHI 257
Cdd:cd19523 158 SKRLLV 163
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
103-255 1.09e-30

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: 114.45  E-value: 1.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 103 LKDTVILPIKKKHLFENSRLLQPpKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVFSLAI 182
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLR-SGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQ 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78097112 183 KLQPSIIFIDEIDSFLRNRSSSDHEATAMMKAQFMSLWDGLDTDHScqVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19526  84 SAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDG--VYVLAATSRPDLIDPALLR--PGRL 152
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
99-255 3.01e-29

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: 110.68  E-value: 3.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  99 VITDLKDTVILPIKKKHLFenSRLLQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGESQKLAAAVF 178
Cdd:cd19527   1 VKKEILDTIQLPLEHPELF--SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVF 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78097112 179 SLAIKLQPSIIFIDEIDSFLRNRSSSDHEATAMMK--AQFMSLWDGLDTDHScQVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19527  79 QKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDRvvSQLLAELDGMSSSGQ-DVFVIGATNRPDLLDPALLR--PGRF 154
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
114-259 5.10e-22

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: 91.05  E-value: 5.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 114 KHLFENSRLLQPPKGVLLYGPPGCGKTLIAKATAKEA---GCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKL---QPS 187
Cdd:cd00009   7 IEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAekaKPG 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78097112 188 IIFIDEIDSFlrnrSSSDHEATAMMKAQFMSLWDGLDTdhscqVIVMGATNRP--QDLDSAIMRRMPTRFHINQ 259
Cdd:cd00009  87 VLFIDEIDSL----SRGAQNALLRVLETLNDLRIDREN-----VRVIGATNRPllGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
92-250 2.85e-17

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 78.18  E-value: 2.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  92 DIAGLDDvitdLKDtvILPIKKKHLFENSRL--LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGE 169
Cdd:cd19507   1 DVGGLDN----LKD--WLKKRKAAFSKQASAygLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 170 SQKLAAAVFSLAIKLQPSIIFIDEIDSFLRNR-SSSDHEATAMMKAQFMSlWdglDTDHSCQVIVMGATNRPQDLDSAIM 248
Cdd:cd19507  75 SESRLRQMIQTAEAIAPCVLWIDEIEKGFSNAdSKGDSGTSSRVLGTFLT-W---LQEKKKPVFVVATANNVQSLPPELL 150

                ..
gi 78097112 249 RR 250
Cdd:cd19507 151 RK 152
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
125-254 1.68e-16

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: 75.87  E-value: 1.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112    125 PPKGVLLYGPPGCGKTLIAKATAKEAGC-----------------RFINLQPSTLTDKWYGESQKLAAAVFSLAIKLQPS 187
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPpgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78097112    188 IIFIDEIDSFLRNRSSSDheataMMKAQFMSLWDGLDTDHSCQVIvmGATNRPQDLDSAIMRRMPTR 254
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVI--LTTNDEKDLGPALLRRRFDR 140
ycf46 CHL00195
Ycf46; Provisional
88-301 3.50e-16

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 79.29  E-value: 3.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   88 VTWSDIAGLDDVITDLKdtvilpiKKKHLFENSRL---LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTD 164
Cdd:CHL00195 225 EKISDIGGLDNLKDWLK-------KRSTSFSKQASnygLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFG 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  165 KWYGESQKLAAAVFSLAIKLQPSIIFIDEID-SFLRNRSSSDHEATAMMKAQFMSlWdgLDTDHScQVIVMGATNRPQDL 243
Cdd:CHL00195 298 GIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFIT-W--LSEKKS-PVFVVATANNIDLL 373
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78097112  244 DSAIMR--RMPTRFHINQPALKQREAILKLILKNENVD--RHVDLLEVAQETDGFSGSDLKE 301
Cdd:CHL00195 374 PLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQ 435
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
119-257 2.55e-15

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: 73.29  E-value: 2.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 119 NSRLLQPP----------KGVLLYGPPGCGKTLIAKATAKEAGCR---FINlQPSTLtDKWYGESQKLAAAVFSLAIKLQ 185
Cdd:cd19504  18 ASRVFPPEiveqlgckhvKGILLYGPPGTGKTLMARQIGKMLNARepkIVN-GPEIL-NKYVGESEANIRKLFADAEEEQ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 186 PS--------IIFIDEIDSFLRNRSSS--DHEATAMMKAQFMSLWDGLDTDHScqVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19504  96 RRlgansglhIIIFDEIDAICKQRGSMagSTGVHDTVVNQLLSKIDGVEQLNN--ILVIGMTNRKDLIDEALLR--PGRL 171

                ..
gi 78097112 256 HI 257
Cdd:cd19504 172 EV 173
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
127-251 4.33e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 60.62  E-value: 4.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 127 KGVLLYGPPGCGKTLIAKATAKEAGCRFinlqpSTLTDkwyGESQKLAA-------AVFSLAIKLQPS-IIFIDEIDSFL 198
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDY-----AIMTG---GDVAPMGRegvtaihKVFDWANTSRRGlLLFVDEADAFL 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 78097112 199 RNRSSsdheaTAMMKAQFMSLWDGL--DTDHSCQVIVMGATNRPQDLDSAIMRRM 251
Cdd:cd19512  95 RKRST-----EKISEDLRAALNAFLyrTGEQSNKFMLVLASNQPEQFDWAINDRI 144
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
108-244 2.96e-10

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: 58.31  E-value: 2.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 108 ILPIKKKHLFENSRLLqppKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYGES--QKLAAAVFSLAIKLQ 185
Cdd:cd19506  11 ILPLGSQAVHEKAPLV---KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQ 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78097112 186 PSIIFIDEID-SFLRNRSSSDHEAT-AMMKAQFMSLWDGLDTDHscQVIVMGATNRPQDLD 244
Cdd:cd19506  88 PSVIWIGDAEkTFYKKVPKTEKQLDpKRLKKDLPKILKSLKPED--RVLIVGTTSRPFEAD 146
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
282-321 3.95e-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: 54.47  E-value: 3.95e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 78097112   282 VDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEE 321
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
127-257 3.62e-09

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: 55.05  E-value: 3.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 127 KGVLLYGPPGCGKTLIAKATAKEAGCRF--INLQPSTLTDkwygESQKLAaavfsLAIKLQPSIIFIDEIDSFLrnrSSS 204
Cdd:cd19510  24 RGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVLTD----DRLNHL-----LNTAPKQSIILLEDIDAAF---ESR 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78097112 205 DHEATAMMKAQFMS------LWDGLD--TDHSCQVIVMgATNRPQDLDSAIMR--RMPTRFHI 257
Cdd:cd19510  92 EHNKKNPSAYGGLSrvtfsgLLNALDgvASSEERIVFM-TTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
119-257 6.14e-09

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 55.15  E-value: 6.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 119 NSRLLQPPKGVLLYGPPGCGKTLIAKATAKE---------AGCRFINLQPSTLTDKWYGESQKLAAAVFSLA---IKLQP 186
Cdd:cd19508  45 NTNLITWNRLVLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIqelIDDKD 124
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78097112 187 SIIF--IDEIDSFL--RNRSSSDHEATAMMKA--QFMSLWDGLDTDHScqVIVMGATNRPQDLDSAIMRRMPTRFHI 257
Cdd:cd19508 125 ALVFvlIDEVESLAaaRSASSSGTEPSDAIRVvnAVLTQIDRIKRYHN--NVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
126-254 1.42e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 53.92  E-value: 1.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 126 PKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWYgesqkLAAAVFSLAIKLQPSIIFIDEIDSFLRNRSSSD 205
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGY-----VGRDVESIIRDLVEGIVFIDEIDKIAKRGGSSG 120
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78097112 206 HEATAM-MKAQFMSLWDG---------LDTDHsCQVIVMGATN--RPQDLDSAIMRRMPTR 254
Cdd:cd19498 121 PDVSREgVQRDLLPIVEGstvstkygpVKTDH-ILFIAAGAFHvaKPSDLIPELQGRFPIR 180
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
129-198 4.87e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 54.32  E-value: 4.87e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78097112  129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKwygESQKLAAAVFSLAIKLQPSIIFIDEI--------DSFL 198
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTSGVK---DLREVIEEARQRRSAGRRTILFIDEIhrfnkaqqDALL 113
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
129-198 9.64e-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: 9.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLqpstltdkwygesqklaAAVFS--------------LAIKLQPSIIFIDEI 194
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVAL-----------------SAVTSgvkdirevieeareRRAYGRRTILFVDEI 114
                        90
                ....*....|..
gi 78097112 195 --------DSFL 198
Cdd:COG2256 115 hrfnkaqqDALL 126
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
129-195 3.19e-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: 47.98  E-value: 3.19e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78097112 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKWY-GES-----QKL-AAAVFSLAiKLQPSIIFIDEID 195
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYvGEDvenilLKLlQAADYDVE-RAQRGIVYIDEID 125
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
129-195 1.39e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.31  E-value: 1.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78097112 129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQ------PSTLT-----DKWYGESQKLAAAVFSlaiklqpSIIFIDEID 195
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILgtyiyDQQTGEFEFRPGPLFA-------NVLLADEIN 104
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
129-195 1.80e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 46.31  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  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 3.24e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 45.68  E-value: 3.24e-05
                         10        20
                 ....*....|....*....|....*...
gi 78097112  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 6.36e-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: 6.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78097112   129 VLLYGPPGCGKTLIAKATAKEAGcrfINLQPST--LTDKwygeSQKLAAavfsLAIKLQP-SIIFIDEI 194
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMG---VNIRITSgpAIER----PGDLAA----ILTNLEPgDVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
129-194 1.18e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.58  E-value: 1.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78097112  129 VLLYGPPGCGKTLIAKATAKE--AGCRFIN---LQ-PSTLtdkwygesqklaAAVFSLaikLQP-SIIFIDEI 194
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEmgVNIRITSgpaLEkPGDL------------AAILTN---LEEgDVLFIDEI 111
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
123-255 2.18e-04

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: 41.21  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 123 LQPPKGVLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLTDKW--------------YGESQKLAAAVFSLAIKLQPSI 188
Cdd:cd19505   9 LSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCI 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78097112 189 IFIDEIDSFLRNRSSSDHEATAMMKAQFM--SLWDGLDTDHSCQVIVMGATNRPQDLDSAIMRrmPTRF 255
Cdd:cd19505  89 IWIPNIHELNVNRSTQNLEEDPKLLLGLLlnYLSRDFEKSSTRNILVIASTHIPQKVDPALIA--PNRL 155
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
126-195 2.88e-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: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112   126 PKGV-LLYGPPGCGKTLIAKATAKEAG---CRFINLQPSTLTDKW--------------YGESQKLAAAVfslaIKLQPS 187
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMEEHsvsrligappgyvgYEEGGQLTEAV----RRKPYS 77

                  ....*...
gi 78097112   188 IIFIDEID 195
Cdd:pfam07724  78 IVLIDEIE 85
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
129-195 3.52e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 42.34  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 129 VLLYGPPGCGKTLIAKATAkeagcRFINLqP------STLTDKWY-GES-----QKL-AAAVFSLAiKLQPSIIFIDEID 195
Cdd:COG1219 112 ILLIGPTGSGKTLLAQTLA-----RILDV-PfaiadaTTLTEAGYvGEDvenilLKLlQAADYDVE-KAERGIIYIDEID 184
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
127-151 5.12e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 5.12e-04
                        10        20
                ....*....|....*....|....*
gi 78097112 127 KGVLLYGPPGCGKTLIAKATAKEAG 151
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELG 89
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
129-194 5.63e-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: 41.13  E-value: 5.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78097112   129 VLLYGPPGCGKTLIAKATAKEAGCRFINLQPSTLtdkwygESQKLAAAVFSLaikLQP-SIIFIDEI 194
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL------EKPGDLAAILTN---LEEgDVLFIDEI 90
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
122-160 8.73e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 41.29  E-value: 8.73e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 78097112 122 LLQPPKGVLLYGPPGCGKTLIAKATAKEAG------CRFINLQPS 160
Cdd:COG1401 217 ALKTKKNVILAGPPGTGKTYLARRLAEALGgedngrIEFVQFHPS 261
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
108-194 1.03e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 40.70  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 108 ILPIKKKHLFEN-SRLLQPPKGVLLYGPPGCGKTLIAKATAKE-AGCRFINLQPSTLTDKWYGESQKLAAAVFSLAIKlq 185
Cdd:COG1373   1 VMIMIKRKILDKlLKLLDNRKAVVITGPRQVGKTTLLKQLAKElENILYINLDDPRLRALAEEDPDDLLEALKELYPG-- 78

                ....*....
gi 78097112 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 1.16e-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: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 78097112   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 1.92e-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: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112 123 LQPPKG--VLLYGPPGCGKTLIAKATA----KEAGCRFINLQPSTLTDKW-------------YGESQKLAAAvfsLAIK 183
Cdd:cd00267  20 LTLKAGeiVALVGPNGSGKSTLLRAIAgllkPTSGEILIDGKDIAKLPLEelrrrigyvpqlsGGQRQRVALA---RALL 96
                        90
                ....*....|....*
gi 78097112 184 LQPSIIFIDEIDSFL 198
Cdd:cd00267  97 LNPDLLLLDEPTSGL 111
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
129-194 3.45e-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: 38.91  E-value: 3.45e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78097112 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 4.06e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 38.68  E-value: 4.06e-03
                        10        20
                ....*....|....*....|....*.
gi 78097112 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 4.84e-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: 4.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 78097112   124 QPPKGVLLYGPPGCGKTLIAKATAKEA 150
Cdd:TIGR02928  38 SRPSNVFIYGKTGTGKTAVTKYVMKEL 64
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
129-145 5.44e-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: 5.44e-03
                          10
                  ....*....|....*..
gi 78097112   129 VLLYGPPGCGKTLIAKA 145
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
129-156 5.44e-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: 5.44e-03
                        10        20
                ....*....|....*....|....*...
gi 78097112 129 VLLYGPPGCGKTLIAKATAKEAGCRFIN 156
Cdd:cd02021   2 IVVMGVSGSGKSTVGKALAERLGAPFID 29
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
126-153 5.91e-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: 5.91e-03
                        10        20
                ....*....|....*....|....*...
gi 78097112 126 PKGVLLYGPPGCGKTLIAKATAKEAGCR 153
Cdd:COG0470  18 PHALLLHGPPGIGKTTLALALARDLLCE 45
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
89-148 6.24e-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: 6.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 78097112  89 TWSDIAGLDDVITDLKdtvilpikkkHLFENSRLlqpPKGVLLYGPPGCGKTLIAKATAK 148
Cdd:COG2812   8 TFDDVVGQEHVVRTLK----------NALASGRL---AHAYLFTGPRGVGKTTLARILAK 54
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
127-151 8.74e-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: 8.74e-03
                          10        20
                  ....*....|....*....|....*
gi 78097112   127 KGVLLYGPPGCGKTLIAKATAKEAG 151
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELG 75
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
127-153 8.82e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 37.45  E-value: 8.82e-03
                        10        20
                ....*....|....*....|....*..
gi 78097112 127 KGVLLYGPPGCGKTLIAKATAKEAgCR 153
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEA-CR 125
 
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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