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Conserved domains on  [gi|2130450631|ref|WP_228273658|]
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AAA family ATPase [Rhodocyclus tenuis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
clpX super family cl35307
ATP-dependent Clp protease ATP-binding subunit ClpX;
2-315 4.61e-147

ATP-dependent Clp protease ATP-binding subunit ClpX;


The actual alignment was detected with superfamily member PRK05342:

Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 419.95  E-value: 4.61e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKLAKAREAGLD--IAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTAD 79
Cdd:PRK05342   61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDveLQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  80 ATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKL--KSSAGQI------EGsagvrVQHALLKIMEGS- 150
Cdd:PRK05342  141 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIarKSENPSItrdvsgEG-----VQQALLKILEGTv 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 151 -RIKLGGGR--------DIDTSDILFIGGGAFVGLDKIAARS---HSYGFISTSAGQS-QSVLDRLNARTKPTDLIEFGL 217
Cdd:PRK05342  216 aSVPPQGGRkhpqqefiQVDTTNILFICGGAFDGLEKIIKQRlgkKGIGFGAEVKSKKeKRTEGELLKQVEPEDLIKFGL 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 218 IPEFTGRLPIIARFGELSRDALAKIMVEPRNSIYQQFREMLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEML 297
Cdd:PRK05342  296 IPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEIL 375

                         330
                  ....*....|....*...
gi 2130450631 298 SPVLYQLPDRPEIRRVLI 315
Cdd:PRK05342  376 LDVMFELPSREDVEKVVI 393
 
Name Accession Description Interval E-value
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
2-315 4.61e-147

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 419.95  E-value: 4.61e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKLAKAREAGLD--IAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTAD 79
Cdd:PRK05342   61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDveLQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  80 ATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKL--KSSAGQI------EGsagvrVQHALLKIMEGS- 150
Cdd:PRK05342  141 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIarKSENPSItrdvsgEG-----VQQALLKILEGTv 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 151 -RIKLGGGR--------DIDTSDILFIGGGAFVGLDKIAARS---HSYGFISTSAGQS-QSVLDRLNARTKPTDLIEFGL 217
Cdd:PRK05342  216 aSVPPQGGRkhpqqefiQVDTTNILFICGGAFDGLEKIIKQRlgkKGIGFGAEVKSKKeKRTEGELLKQVEPEDLIKFGL 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 218 IPEFTGRLPIIARFGELSRDALAKIMVEPRNSIYQQFREMLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEML 297
Cdd:PRK05342  296 IPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEIL 375

                         330
                  ....*....|....*...
gi 2130450631 298 SPVLYQLPDRPEIRRVLI 315
Cdd:PRK05342  376 LDVMFELPSREDVEKVVI 393
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 2-315 2.88e-130

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 377.08  E-value: 2.88e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKL--AKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTAD 79
Cdd:COG1219    62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLnsGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  80 ATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKL--KSSAGQI------EGsagvrVQHALLKIMEGSR 151
Cdd:COG1219   142 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIarKSENPSItrdvsgEG-----VQQALLKILEGTV 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 152 IKL--GGGR--------DIDTSDILFIGGGAFVGLDKIAAR---SHSYGFISTSAGQSQSVLDRLNARTKPTDLIEFGLI 218
Cdd:COG1219   217 ANVppQGGRkhpqqefiQIDTTNILFICGGAFDGLEKIIERrlgKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLI 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 219 PEFTGRLPIIARFGELSRDALAKIMVEPRNSIYQQFREMLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEMLS 298
Cdd:COG1219   297 PEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILL 376

                         330
                  ....*....|....*..
gi 2130450631 299 PVLYQLPDRPEIRRVLI 315
Cdd:COG1219   377 DVMYELPSRKDVKKVVI 393
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 2-231 1.08e-91

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: 273.32  E-value: 1.08e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKL---AKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTA 78
Cdd:cd19497     2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIrnnLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  79 DATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKLKSSAGQIEGS---AGVRVQHALLKIMEGS--RIK 153
Cdd:cd19497    82 DATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITrdvSGEGVQQALLKILEGTvaNVP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 154 LGGGR--------DIDTSDILFIGGGAFVGLDKIAAR---SHSYGFIS-TSAGQSQSVLDRLNARTKPTDLIEFGLIPEF 221
Cdd:cd19497   162 PQGGRkhpqqefiQVDTTNILFICGGAFVGLEKIIARrlgKKSLGFGAeTSSEKDEKERDELLSKVEPEDLIKFGLIPEF 241

                         250
                  ....*....|
gi 2130450631 222 TGRLPIIARF 231
Cdd:cd19497   242 VGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 47-228 3.13e-34

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: 123.07  E-value: 3.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  47 KSNILLIGPTGSGKTLLCETLSRGLGL---PFVTADATSLAQSKYVNEEIEAvllrlldrADGNMAKAQRG--------- 114
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGA--------PPGYVGYEEGGqlteavrrk 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 115 ---IVFIDEIDKlkssagqiegsAGVRVQHALLKIMEGSRIKLGGGRDIDTSDILFIGGGAFVGLDKIAARshsygfist 191
Cdd:pfam07724  75 pysIVLIDEIEK-----------AHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDAS--------- 134

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2130450631 192 sagQSQSVLDRLNARTKPTDLIEFGLIPEFTGRLPII 228
Cdd:pfam07724 135 ---RLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 234-313 1.32e-08

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 51.29  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  234 LSRDALAKIMVEPRNSIYQQfremLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEMLSPVLYQLPDRPEIRRV 313
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKR----LAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDG 76
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 50-149 9.57e-08

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: 53.37  E-value: 9.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLaQSKYVNEEiEAVLLRLLDRADGNMAkaqrGIVFIDEIDKLKSSAG 129
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI-MSKYYGES-EERLREIFKEAEENAP----SIIFIDEIDAIAPKRE 288

                          90       100
                  ....*....|....*....|
gi 2130450631 130 QIEGSAGVRVQHALLKIMEG 149
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDG 308
 
Name Accession Description Interval E-value
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
2-315 4.61e-147

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 419.95  E-value: 4.61e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKLAKAREAGLD--IAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTAD 79
Cdd:PRK05342   61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDveLQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  80 ATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKL--KSSAGQI------EGsagvrVQHALLKIMEGS- 150
Cdd:PRK05342  141 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIarKSENPSItrdvsgEG-----VQQALLKILEGTv 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 151 -RIKLGGGR--------DIDTSDILFIGGGAFVGLDKIAARS---HSYGFISTSAGQS-QSVLDRLNARTKPTDLIEFGL 217
Cdd:PRK05342  216 aSVPPQGGRkhpqqefiQVDTTNILFICGGAFDGLEKIIKQRlgkKGIGFGAEVKSKKeKRTEGELLKQVEPEDLIKFGL 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 218 IPEFTGRLPIIARFGELSRDALAKIMVEPRNSIYQQFREMLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEML 297
Cdd:PRK05342  296 IPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEIL 375

                         330
                  ....*....|....*...
gi 2130450631 298 SPVLYQLPDRPEIRRVLI 315
Cdd:PRK05342  376 LDVMFELPSREDVEKVVI 393
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 2-315 2.88e-130

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 377.08  E-value: 2.88e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKL--AKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTAD 79
Cdd:COG1219    62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLnsGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  80 ATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKL--KSSAGQI------EGsagvrVQHALLKIMEGSR 151
Cdd:COG1219   142 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIarKSENPSItrdvsgEG-----VQQALLKILEGTV 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 152 IKL--GGGR--------DIDTSDILFIGGGAFVGLDKIAAR---SHSYGFISTSAGQSQSVLDRLNARTKPTDLIEFGLI 218
Cdd:COG1219   217 ANVppQGGRkhpqqefiQIDTTNILFICGGAFDGLEKIIERrlgKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLI 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 219 PEFTGRLPIIARFGELSRDALAKIMVEPRNSIYQQFREMLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEMLS 298
Cdd:COG1219   297 PEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILL 376

                         330
                  ....*....|....*..
gi 2130450631 299 PVLYQLPDRPEIRRVLI 315
Cdd:COG1219   377 DVMYELPSRKDVKKVVI 393
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 2-231 1.08e-91

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: 273.32  E-value: 1.08e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKL---AKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTA 78
Cdd:cd19497     2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIrnnLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  79 DATSLAQSKYVNEEIEAVLLRLLDRADGNMAKAQRGIVFIDEIDKLKSSAGQIEGS---AGVRVQHALLKIMEGS--RIK 153
Cdd:cd19497    82 DATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITrdvSGEGVQQALLKILEGTvaNVP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 154 LGGGR--------DIDTSDILFIGGGAFVGLDKIAAR---SHSYGFIS-TSAGQSQSVLDRLNARTKPTDLIEFGLIPEF 221
Cdd:cd19497   162 PQGGRkhpqqefiQVDTTNILFICGGAFVGLEKIIARrlgKKSLGFGAeTSSEKDEKERDELLSKVEPEDLIKFGLIPEF 241

                         250
                  ....*....|
gi 2130450631 222 TGRLPIIARF 231
Cdd:cd19497   242 VGRLPVIVTL 251
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 2-227 2.81e-36

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: 129.04  E-value: 2.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   2 TPSSIVRYLDQYMVGQEAAKKTVAVAVYSHYQKLAKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADAT 81
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  82 SLAQSKYVNEEIEAVLLRLLDradgnmakaqrGIVFIDEIDKLKSSAGqiEGSAGVR---VQHALLKIMEGSRIKLGGGR 158
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE-----------GIVFIDEIDKIAKRGG--SSGPDVSregVQRDLLPIVEGSTVSTKYGP 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130450631 159 dIDTSDILFIGGGAFvgldkiaarsHSygfistsagqsqsvldrlnarTKPTDliefgLIPEFTGRLPI 227
Cdd:cd19498   148 -VKTDHILFIAAGAF----------HV---------------------AKPSD-----LIPELQGRFPI 179
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-309 4.84e-35

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 132.12  E-value: 4.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   1 MTPSSIVRYLDQYMVGQEAAKKTVAVAVYSHY--QKLAKA-REaglDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVT 77
Cdd:PRK05201    4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWrrMQLPEElRD---EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  78 ADATSLAQSKYV--------------------NEEIEAV-----------LLRLL------------------------- 101
Cdd:PRK05201   81 VEATKFTEVGYVgrdvesiirdlveiavkmvrEEKREKVrekaeeaaeerILDALlppaknnwgeeeekeeisatrqkfr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 102 ---------DR------AD------------------------GNM---------------------------------- 108
Cdd:PRK05201  161 kklregeldDKeieievAEaapmmeimgppgmeemtiqlqdmfGNLgpkkkkkrklkvkearkilieeeaaklidmeeik 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 109 AKA-----QRGIVFIDEIDKLKSSAGqiEGSAGV-R--VQHALLKIMEGSRI--KLGggrDIDTSDILFIGGGAFvgldk 178
Cdd:PRK05201  241 QEAierveQNGIVFIDEIDKIAARGG--SSGPDVsRegVQRDLLPLVEGSTVstKYG---MVKTDHILFIASGAF----- 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 179 iaarsHsygfIStsagqsqsvldrlnartKPTDliefgLIPEFTGRLPIIARFGELSRDALAKIMVEPRNSIYQQFREML 258
Cdd:PRK05201  311 -----H----VS-----------------KPSD-----LIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALL 359

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2130450631 259 KHEGVELCIEAPVFDQIAELAseYQV-------GARSLRGIFEEMLSPVLYQLPDRPE 309
Cdd:PRK05201  360 ATEGVTLEFTDDAIRRIAEIA--YQVnekteniGARRLHTVMEKLLEDISFEAPDMSG 415
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 47-228 3.13e-34

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: 123.07  E-value: 3.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  47 KSNILLIGPTGSGKTLLCETLSRGLGL---PFVTADATSLAQSKYVNEEIEAvllrlldrADGNMAKAQRG--------- 114
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGA--------PPGYVGYEEGGqlteavrrk 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 115 ---IVFIDEIDKlkssagqiegsAGVRVQHALLKIMEGSRIKLGGGRDIDTSDILFIGGGAFVGLDKIAARshsygfist 191
Cdd:pfam07724  75 pysIVLIDEIEK-----------AHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDAS--------- 134

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2130450631 192 sagQSQSVLDRLNARTKPTDLIEFGLIPEFTGRLPII 228
Cdd:pfam07724 135 ---RLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-309 9.65e-33

ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 125.93  E-value: 9.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   1 MTPSSIVRYLDQYMVGQEAAKKTVAVAVYSHY--QKLAKA-REaglDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVT 77
Cdd:COG1220     4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWrrQQLPEElRD---EITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  78 ADATslaqsK-----YV--------------------NEEIEAVLLRLLDRAD--------------------------- 105
Cdd:COG1220    81 VEAT-----KftevgYVgrdvesmirdlveiavkmvrEEKMEKVREKAEEAAEerildlllpppkkkagsnnpfeeeeee 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 106 -----------------------------------------------------------GNM------------AKA--- 111
Cdd:COG1220   156 eeeeeeisrtrekfrkklregelddreieieveessspgveimgppgmeemgmnlqdmfGNLmpkkkkkrkvkvKEArki 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 112 ------------------------QRGIVFIDEIDKLKSSAGQieGSAGV-R--VQHALLKIMEGSRI--KLGggrDIDT 162
Cdd:COG1220   236 ltqeeaaklidmdevkqeaieraeQNGIIFIDEIDKIASRGGG--SGPDVsRegVQRDLLPIVEGSTVntKYG---MVKT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 163 SDILFIGGGAFvgldkiaarsHsygfistsagqsqsvldrlnaRTKPTDliefgLIPEFTGRLPIIARFGELSRDALAKI 242
Cdd:COG1220   311 DHILFIAAGAF----------H---------------------VSKPSD-----LIPELQGRFPIRVELDSLTEEDFVRI 354

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130450631 243 MVEPRNSIYQQFREMLKHEGVELCIEAPVFDQIAELAseYQV-------GARSLRGIFEEMLSPVLYQLPDRPE 309
Cdd:COG1220   355 LTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIA--FEVnerteniGARRLHTVMEKLLEDISFEAPDLSG 426
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 26-169 1.17e-18

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: 81.56  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  26 VAVYSHYQKLAKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDRAD 105
Cdd:cd19481     5 LREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLL-SKYVGES-EKNLRKIFERAR 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130450631 106 gnmaKAQRGIVFIDEIDKL-KSSAGQIEGSAGVRVQHALLKIMEGSRIklgggrdidTSDILFIG 169
Cdd:cd19481    83 ----RLAPCILFIDEIDAIgRKRDSSGESGELRRVLNQLLTELDGVNS---------RSKVLVIA 134
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 14-151 6.01e-16

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: 77.64  E-value: 6.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  14 MVGQEAAKKTV--AVAVYSHYQKLAkaREAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVnE 91
Cdd:COG0464   159 LGGLEEVKEELreLVALPLKRPELR--EEYGLPPPRG-LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYV-G 233

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  92 EIEAVLLRLLDRADGNmakaQRGIVFIDEIDKLKSSAGQIEGSAGVRVQHALLKIMEGSR 151
Cdd:COG0464   234 ETEKNLREVFDKARGL----APCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR 289
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 50-169 1.78e-15

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: 71.86  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVLLRLldradgNMAKAQR-GIVFIDEIDKLKSSA 128
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELV-SKYVGESEKRLRELF------EAAKKLApCVIFIDEIDALAGSR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2130450631 129 GQIEGSAGVRVQHALLKIMEGSRiklgggrdIDTSDILFIG 169
Cdd:pfam00004  74 GSGGDSESRRVVNQLLTELDGFT--------SSNSKVIVIA 106
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
14-169 8.65e-14

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 69.91  E-value: 8.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  14 MVGQEAAKKTVAVAVysHYQKLAKA-REAGLdIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVnEE 92
Cdd:COG1223     4 VVGQEEAKKKLKLII--KELRRRENlRKFGL-WPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI-GSYL-GE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130450631  93 IEAVLLRLLDRAdgnmaKAQRGIVFIDEIDKL-KSSAGQIEGSAGVRVQHALLKIMEGsriklgggrdiDTSDILFIG 169
Cdd:COG1223    79 TARNLRKLFDFA-----RRAPCVIFFDEFDAIaKDRGDQNDVGEVKRVVNALLQELDG-----------LPSGSVVIA 140
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 50-149 6.20e-13

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: 65.78  E-value: 6.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLaQSKYVNEEiEAVLLRLLDRAdgnmAKAQRGIVFIDEIDKLKSSAG 129
Cdd:cd19503    37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSI-VSKYLGES-EKNLREIFEEA----RSHAPSIIFIDEIDALAPKRE 110

                          90       100
                  ....*....|....*....|
gi 2130450631 130 QIEGSAGVRVQHALLKIMEG 149
Cdd:cd19503   111 EDQREVERRVVAQLLTLMDG 130
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 15-130 1.47e-12

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: 64.47  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  15 VGQEAAKKTVAVAVYSHYqklakareagldiaKSNILLIGPTGSGKTLLCETLSRGL---GLPFVTADATSLAQSKYVNE 91
Cdd:cd00009     1 VGQEEAIEALREALELPP--------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2130450631  92 EIEAVLLRLLDRAdgnMAKAQRGIVFIDEIDKLKSSAGQ 130
Cdd:cd00009    67 LFGHFLVRLLFEL---AEKAKPGVLFIDEIDSLSRGAQN 102
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 50-149 4.86e-10

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: 57.36  E-value: 4.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVllrlldRADGNMA-KAQRGIVFIDEIDKLKSSA 128
Cdd:cd19509    35 ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGESEKIV------RALFALArELQPSIIFIDEIDSLLSER 107

                          90       100
                  ....*....|....*....|.
gi 2130450631 129 GQIEGSAGVRVQHALLKIMEG 149
Cdd:cd19509   108 GSGEHEASRRVKTEFLVQMDG 128
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 50-149 4.31e-09

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: 54.60  E-value: 4.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDRAdgnmAKAQRGIVFIDEIDKLKSSAG 129
Cdd:cd19511    30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELF-SKYVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLAPRRG 103

                          90       100
                  ....*....|....*....|..
gi 2130450631 130 QiEGSAGV--RVQHALLKIMEG 149
Cdd:cd19511   104 Q-SDSSGVtdRVVSQLLTELDG 124
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 7-149 7.07e-09

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 56.17  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   7 VRYLDqyMVGQEAAKKTVAVAVYSHYQKLAKAREAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLaQS 86
Cdd:COG1222    75 VTFDD--IGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKG-VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL-VS 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130450631  87 KYVNEeiEAVLLR-LLDRAdgnmAKAQRGIVFIDEIDKLKSSAGQ-IEGSAGVRVQHALLKIMEG 149
Cdd:COG1222   151 KYIGE--GARNVReVFELA----REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDG 209
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 42-149 1.10e-08

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: 54.22  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  42 GLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVllrlldRADGNMAKAQR-GIVFIDE 120
Cdd:cd19525    50 GLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEGEKMV------RALFSVARCKQpAVIFIDE 122

                          90       100
                  ....*....|....*....|....*....
gi 2130450631 121 IDKLKSSAGQIEGSAGVRVQHALLKIMEG 149
Cdd:cd19525   123 IDSLLSQRGEGEHESSRRIKTEFLVQLDG 151
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 50-163 1.12e-08

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: 53.83  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEavLLRLLdradGNMAKAQR-GIVFIDEIDKLKSSA 128
Cdd:cd19522    36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGESEK--LVRLL----FEMARFYApTTIFIDEIDSICSRR 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2130450631 129 G-QIEGSAGVRVQHALLKIMEGsrikLGGGRDIDTS 163
Cdd:cd19522   109 GtSEEHEASRRVKSELLVQMDG----VGGASENDDP 140
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 5-168 1.25e-08

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 53.72  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   5 SIVRYLDQYMVGQEAAKKTVAVAVYSHyQKLAKAREAGLdiakSNILLIGPTGSGKTLLCETLSR---GLGLPFVTADAT 81
Cdd:cd19499     4 NLEERLHERVVGQDEAVKAVSDAIRRA-RAGLSDPNRPI----GSFLFLGPTGVGKTELAKALAEllfGDEDNLIRIDMS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  82 SLAQSKYVNEEIEAVLLRLLDRADGNMAKAQR----GIVFIDEIDKlkssagqiegsAGVRVQHALLKIMEGSRIKLGGG 157
Cdd:cd19499    79 EYMEKHSVSRLIGAPPGYVGYTEGGQLTEAVRrkpySVVLLDEIEK-----------AHPDVQNLLLQVLDDGRLTDSHG 147

                         170
                  ....*....|.
gi 2130450631 158 RDIDTSDILFI 168
Cdd:cd19499   148 RTVDFKNTIII 158
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 234-313 1.32e-08

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 51.29  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  234 LSRDALAKIMVEPRNSIYQQfremLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEMLSPVLYQLPDRPEIRRV 313
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKR----LAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDG 76
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 42-149 6.90e-08

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: 51.33  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  42 GLDiAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVLlRLLDRAdgnmAKAQRGIVFIDEI 121
Cdd:cd19530    26 GID-LPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELL-NKYVGESERAVR-QVFQRA----RASAPCVIFFDEV 98

                          90       100
                  ....*....|....*....|....*...
gi 2130450631 122 DKLKSSAGQIEGSAGVRVQHALLKIMEG 149
Cdd:cd19530    99 DALVPKRGDGGSWASERVVNQLLTEMDG 126
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 50-149 9.57e-08

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: 53.37  E-value: 9.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLaQSKYVNEEiEAVLLRLLDRADGNMAkaqrGIVFIDEIDKLKSSAG 129
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI-MSKYYGES-EERLREIFKEAEENAP----SIIFIDEIDAIAPKRE 288

                          90       100
                  ....*....|....*....|
gi 2130450631 130 QIEGSAGVRVQHALLKIMEG 149
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDG 308
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 50-122 2.38e-07

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: 49.71  E-value: 2.38e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAQSkyVNEEIEAVLLRLLDRADGNMAkaqrGIVFIDEID 122
Cdd:cd19518    37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSG--VSGESEEKIRELFDQAISNAP----CIVFIDEID 103
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 47-149 3.77e-07

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: 48.96  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  47 KSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVLLrLLDRAdgnmAKAQRGIVFIDEIDKLKS 126
Cdd:cd19526    27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVRD-LFSRA----QSAKPCILFFDEFDSIAP 100

                          90       100
                  ....*....|....*....|....*
gi 2130450631 127 SAGQieGSAGV--RVQHALLKIMEG 149
Cdd:cd19526   101 KRGH--DSTGVtdRVVNQLLTQLDG 123
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 1-148 7.28e-07

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: 49.78  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   1 MTPSSIVRYLDQYMVGQEAAKKTVAVAVyshyqklakareagldIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVT--- 77
Cdd:COG0714     1 MTEARLRAEIGKVYVGQEELIELVLIAL----------------LAGGHLLLEGVPGVGKTTLAKALARALGLPFIRiqf 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  78 ------ADAT--SLAQSKYVNEEIE--AVLlrlldradgnmakaqRGIVFIDEIDKlkssagqiegsAGVRVQHALLKIM 147
Cdd:COG0714    65 tpdllpSDILgtYIYDQQTGEFEFRpgPLF---------------ANVLLADEINR-----------APPKTQSALLEAM 118


                  .
gi 2130450631 148 E 148
Cdd:COG0714   119 E 119
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 48-149 1.03e-06

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: 47.93  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  48 SNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDradgnMAKAQR-GIVFIDEIDKLKS 126
Cdd:cd19521    41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFA-----MARENKpSIIFIDEVDSLCG 113

                          90       100
                  ....*....|....*....|...
gi 2130450631 127 SAGQIEGSAGVRVQHALLKIMEG 149
Cdd:cd19521   114 TRGEGESEASRRIKTELLVQMNG 136
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 48-148 1.27e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  48 SNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSlaQSKyvnEEIEAVllrlLDRADGNMAKAQRGIVFIDEI---DKL 124
Cdd:PRK13342   37 SSMILWGPPGTGKTTLARIIAGATDAPFEALSAVT--SGV---KDLREV----IEEARQRRSAGRRTILFIDEIhrfNKA 107

                          90       100
                  ....*....|....*....|....
gi 2130450631 125 KssagqiegsagvrvQHALLKIME 148
Cdd:PRK13342  108 Q--------------QDALLPHVE 117
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 47-152 2.00e-06

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: 46.98  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   47 KSNILLIGPTGSGKTLLCETLSRGL---GLPFVTADATSLAQSKYVNEEIEAVLLRLLDRADGNMA--------KAQRGI 115
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlalalarKLKPDV 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2130450631  116 VFIDEIDKLKSSAGQIEGSAGVRVQHALLKIMEGSRI 152
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 50-149 3.67e-06

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: 46.28  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLaQSKYVNEEiEAVLLRLLDRADGNMAkaqrGIVFIDEIDKLKSSAG 129
Cdd:cd19519    37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEI-MSKLAGES-ESNLRKAFEEAEKNAP----AIIFIDEIDAIAPKRE 110

                          90       100
                  ....*....|....*....|
gi 2130450631 130 QIEGSAGVRVQHALLKIMEG 149
Cdd:cd19519   111 KTHGEVERRIVSQLLTLMDG 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 20-149 4.84e-06

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: 45.95  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  20 AKKTVAVAVYSHYQKLAKAREAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVllR 99
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGIRPPKG-ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGESEKAI--R 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2130450631 100 LLDRADGNMAKAqrgIVFIDEIDKLKSSAGQIeGSAGV--RVQHALLKIMEG 149
Cdd:cd19529    77 EIFRKARQVAPC---VIFFDEIDSIAPRRGTT-GDSGVteRVVNQLLTELDG 124
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 39-147 5.60e-06

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: 45.79  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  39 REAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAQsKYVNEeiEAVLLRLLDRadgnMAKAQR-GIVF 117
Cdd:cd19502    30 EELGIEPPKG-VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIGE--GARLVRELFE----MAREKApSIIF 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 2130450631 118 IDEIDKLKSSAGQIEGSAGVRVQHALLKIM 147
Cdd:cd19502   102 IDEIDAIGAKRFDSGTGGDREVQRTMLELL 131
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 47-149 9.18e-06

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: 45.20  E-value: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  47 KSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDRAdgnmAKAQRGIVFIDEIDKLKS 126
Cdd:cd19527    26 RSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELI-NMYIGES-EANVREVFQKA----RDAKPCVIFFDELDSLAP 99

                          90       100
                  ....*....|....*....|....*
gi 2130450631 127 SAGQIEGSAGV--RVQHALLKIMEG 149
Cdd:cd19527   100 SRGNSGDSGGVmdRVVSQLLAELDG 124
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 42-151 1.65e-05

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: 44.46  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  42 GLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEIEAVllrlldRADGNMAKA-QRGIVFIDE 120
Cdd:cd19524    28 GLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEGEKLV------RALFAVARElQPSIIFIDE 100

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2130450631 121 IDKLKSSAGQIEGSAGVRVQHALLKIMEGSR 151
Cdd:cd19524   101 VDSLLSERSEGEHEASRRLKTEFLIEFDGVQ 131
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 50-149 3.34e-05

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: 43.65  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDRADGnmakAQRGIVFIDEIDKL-KSSA 128
Cdd:cd19528    30 VLFYGPPGCGKTLLAKAIANECQANFISVKGPELL-TMWFGES-EANVRDIFDKARA----AAPCVLFFDELDSIaKARG 103

                          90       100
                  ....*....|....*....|...
gi 2130450631 129 GQIEGSAGV--RVQHALLKIMEG 149
Cdd:cd19528   104 GNIGDAGGAadRVINQILTEMDG 126
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 50-149 4.35e-05

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: 45.28  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDRAdgnmAKAQRGIVFIDEIDKLKSSAG 129
Cdd:TIGR01243 490 VLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL-SKWVGES-EKAIREIFRKA----RQAAPAIIFFDEIDAIAPARG 563

                          90       100
                  ....*....|....*....|.
gi 2130450631 130 QIEGSAGV-RVQHALLKIMEG 149
Cdd:TIGR01243 564 ARFDTSVTdRIVNQLLTEMDG 584
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 7-149 1.29e-04

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: 41.83  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   7 VRYLDqyMVGQEAAKKTVAVAVySHYQKLAKAREAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVtadatSLAQS 86
Cdd:cd19501     1 VTFKD--VAGCEEAKEELKEVV-EFLKNPEKFTKLGAKIPKG-VLLVGPPGTGKTLLAKAVAGEAGVPFF-----SISGS 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130450631  87 KYVNE--EIEAVLLR-LLDRADgnmaKAQRGIVFIDEIDKLKSSAGQIE-GSAGVRVQ--HALLKIMEG 149
Cdd:cd19501    72 DFVEMfvGVGASRVRdLFEQAK----KNAPCIVFIDEIDAVGRKRGAGLgGGHDEREQtlNQLLVEMDG 136
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
14-129 1.43e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 43.48  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  14 MVGQEAAKKTVAVAVySHYQKLAKAREAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVTadatsLAQSKYVNEEI 93
Cdd:PRK10733  154 VAGCDEAKEEVAELV-EYLREPSRFQKLGGKIPKG-VLMVGPPGTGKTLLAKAIAGEAKVPFFT-----ISGSDFVEMFV 226

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2130450631  94 EAVLLRLLDRADgNMAKAQRGIVFIDEIDKLKSSAG 129
Cdd:PRK10733  227 GVGASRVRDMFE-QAKKAAPCIIFIDEIDAVGRQRG 261
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 38-129 1.75e-04

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: 41.20  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  38 AREAGLDIAKSnILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiEAVLLRLLDRADGnMAKAqrgIVF 117
Cdd:cd19507    23 ASAYGLPTPKG-LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGES-ESRLRQMIQTAEA-IAPC---VLW 95

                          90
                  ....*....|..
gi 2130450631 118 IDEIDKLKSSAG 129
Cdd:cd19507    96 IDEIEKGFSNAD 107
ftsH CHL00176
cell division protein; Validated
 50-122 2.15e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 42.73  E-value: 2.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGLPFVtadatSLAQSKYVNEEIEAVLLRLLDRadgnMAKAQRG---IVFIDEID 122
Cdd:CHL00176  219 VLLVGPPGTGKTLLAKAIAGEAEVPFF-----SISGSEFVEMFVGVGAARVRDL----FKKAKENspcIVFIDEID 285
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 46-122 3.24e-04

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: 40.87  E-value: 3.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130450631  46 AKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNE--EIEAVLLRLldradgnMAKAQRGIVFIDEID 122
Cdd:cd19520    34 PPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLT-DKWYGEsqKLVAAVFSL-------ASKLQPSIIFIDEID 104
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 16-149 4.51e-04

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: 40.25  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  16 GQEAAKKTVAVAVYshYQKLAKAREAGLDIAKSNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAqSKYVNEEiea 95
Cdd:cd19523     4 GLGALKAAIKEEVL--WPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLV-AKWAGEG--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2130450631  96 vlLRLLDRADGNMAKAQRGIVFIDEIDKLKSSagQIEG-SAGVRVQHALLKIMEG 149
Cdd:cd19523    78 --EKILQASFLAARCRQPSVLFISDLDALLSS--QDDEaSPVGRLQVELLAQLDG 128
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 6-148 6.56e-04

MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350658 [Multi-domain]  Cd Length: 311  Bit Score: 40.79  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   6 IVRYLDQYMVGQEAAKKTVAVAVYSHYQKLAKAReaGLDIAKSNILLIGPTGSGKTLL----CETLSRGLglpFVTADAT 81
Cdd:cd17706     2 LADSIAPSIYGHEDVKKAVLLQLFGGVQKILEDG--TRIRGDIHILLVGDPGTAKSQIlkyvLKIAPRGV---YTSGKGS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130450631  82 SLAqskyvneEIEAVLLRllDRADGNMA-------KAQRGIVFIDEIDKLKSSAgqiegsagvrvQHALLKIME 148
Cdd:cd17706    77 SGA-------GLTAAVVR--DSETGEWYleagalvLADGGVCCIDEFDKMKELD-----------RTALHEAME 130
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
8-121 1.19e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631   8 RYLDQYmVGQEAAKKTVAVAVyshyqKLAKAREAGLDiaksNILLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAQSK 87
Cdd:PRK00080   22 KSLDEF-IGQEKVKENLKIFI-----EAAKKRGEALD----HVLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKPG 91

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2130450631  88 YVneeieAVLLRLLDRADgnmakaqrgIVFIDEI 121
Cdd:PRK00080   92 DL-----AAILTNLEEGD---------VLFIDEI 111
AAA_22 pfam13401
AAA domain;
47-125 1.58e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  47 KSNILLIGPTGSGKTLLCETLSRGLGL---PFVTADATSLAQSKYVNEEI-EAVLLRLLDRADGNMAKAQ---------- 112
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPEvrdSVVFVDLPSGTSPKDLLRALlRALGLPLSGRLSKEELLAAlqqlllalav 84

                          90
                  ....*....|...
gi 2130450631 113 RGIVFIDEIDKLK 125
Cdd:pfam13401  85 AVVLIIDEAQHLS 97
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 49-128 1.60e-03

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 38.04  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  49 NILLIGPTGSGKTLLCETLSRGL-GLPFV----TADATSlaqskyvnEEIE---AVLLRLLDRADGN-MAKAQRG-IVFI 118
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFyvqlTRDTTE--------EDLFgrrNIDPGGASWVDGPlVRAAREGeIAVL 72

                          90
                  ....*....|
gi 2130450631 119 DEIDKLKSSA 128
Cdd:pfam07728  73 DEINRANPDV 82
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 50-149 1.84e-03

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: 38.62  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  50 ILLIGPTGSGKTLLCETLSRGLGL--PFVTADATSLaqSKYVNEEiEAVLLRLLdrADGNMAKAQRG------IVFIDEI 121
Cdd:cd19504    38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEIL--NKYVGES-EANIRKLF--ADAEEEQRRLGansglhIIIFDEI 112

                          90       100       110
                  ....*....|....*....|....*....|
gi 2130450631 122 DKLKSSAGQIEGSAGV--RVQHALLKIMEG 149
Cdd:cd19504   113 DAICKQRGSMAGSTGVhdTVVNQLLSKIDG 142
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 51-297 4.78e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 38.66  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  51 LLIGPTGSGKTLLCETLSRGLGLPFVTADATSLAQSKYVNeeieavllRLLDRADGNMAKAQRG------------IVFI 118
Cdd:PRK11034  492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVS--------RLIGAPPGYVGFDQGGlltdavikhphaVLLL 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 119 DEIDKlkssagqiegsAGVRVQHALLKIMEGSRIKLGGGRDIDTSDILFIgggafvgldkiaarshsygfISTSAG---- 194
Cdd:PRK11034  564 DEIEK-----------AHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLV--------------------MTTNAGvret 612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631 195 QSQSV-LDRLNARTKPTDLIEFGLIPEFTGRLPIIARFGELSRDALAKIMveprNSIYQQFREMLKHEGVELCIEAPVFD 273
Cdd:PRK11034  613 ERKSIgLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVV----DKFIVELQAQLDQKGVSLEVSQEARD 688

                         250       260
                  ....*....|....*....|....
gi 2130450631 274 QIAELASEYQVGARSLRGIFEEML 297
Cdd:PRK11034  689 WLAEKGYDRAMGARPMARVIQDNL 712
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 234-305 5.76e-03

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.


Pssm-ID: 463090 [Multi-domain]  Cd Length: 81  Bit Score: 35.07  E-value: 5.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130450631 234 LSRDALAKI---MVeprnsiyQQFREMLKHEGVELCIEAPVFDQIAELASEYQVGARSLRGIFEEMLSPVLYQLP 305
Cdd:pfam10431   1 LSKEELRKIvdlQL-------KELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEI 68
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 49-79 7.86e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 36.38  E-value: 7.86e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2130450631  49 NILLIGPTGSGKTLLCETLSRGLGLPFVTAD 79
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD 31
PRK13341 PRK13341
AAA family ATPase;
48-127 8.37e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 37.73  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  48 SNILLIGPTGSGKTLLCETLSRGLGLPFVTADATsLAQSKYVNEEIEAVLLRLlDRADgnmakaQRGIVFIDEIDKLKSS 127
Cdd:PRK13341   53 GSLILYGPPGVGKTTLARIIANHTRAHFSSLNAV-LAGVKDLRAEVDRAKERL-ERHG------KRTILFIDEVHRFNKA 124
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
48-129 9.62e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 37.52  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130450631  48 SNILLIGPTGSGKTL----LCETL---SRGLGLPFVTAdatslaqskYVNEEIE----AVLLRLLDRADGNMAKAQRG-- 114
Cdd:COG1474    52 SNVLIYGPTGTGKTAvakyVLEELeeeAEERGVDVRVV---------YVNCRQAstryRVLSRILEELGSGEDIPSTGls 122

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2130450631 115 -------------------IVFIDEIDKLKSSAG 129
Cdd:COG1474   123 tdelfdrlyealderdgvlVVVLDEIDYLVDDEG 156
 
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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