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Conserved domains on  [gi|499665579|ref|WP_011346313|]
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MULTISPECIES: ATP-dependent protease ATPase subunit HslU [Xanthomonas]

Protein Classification

ATP-dependent protease ATPase subunit HslU( domain architecture ID 11480440)

ATP-dependent protease ATPase subunit HslU is the ATPase component of a proteasome-like degradation complex and has chaperone activity

CATH:  1.10.8.10|3.40.50.300|1.10.8.60
Gene Ontology:  GO:0006508|GO:0004176|GO:0005524|GO:0016887|GO:0036402
SCOP:  4000283

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
8-455 0e+00

ATP-dependent protease ATPase subunit HslU;


:

Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 876.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   8 TMTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:PRK05201   3 ELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPRRAAGIGFdpeaarNEPSSQDNETR 167
Cdd:PRK05201  83 ATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGE------EEEKEEISATR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 168 IKFRRMLRNGELDEREIELDVAVNAS-MDIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAGKLVNE 246
Cdd:PRK05201 157 QKFRKKLREGELDDKEIEIEVAEAAPmMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDM 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 247 DDVRTAAIEACEQHGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAK 326
Cdd:PRK05201 237 EEIKQEAIERVEQNGIVFIDEIDKIAARG--GSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 327 PSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQENIGARR 406
Cdd:PRK05201 315 PSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARR 394

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 499665579 407 LHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:PRK05201 395 LHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
8-455 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 876.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   8 TMTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:PRK05201   3 ELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPRRAAGIGFdpeaarNEPSSQDNETR 167
Cdd:PRK05201  83 ATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGE------EEEKEEISATR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 168 IKFRRMLRNGELDEREIELDVAVNAS-MDIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAGKLVNE 246
Cdd:PRK05201 157 QKFRKKLREGELDDKEIEIEVAEAAPmMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDM 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 247 DDVRTAAIEACEQHGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAK 326
Cdd:PRK05201 237 EEIKQEAIERVEQNGIVFIDEIDKIAARG--GSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 327 PSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQENIGARR 406
Cdd:PRK05201 315 PSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARR 394

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 499665579 407 LHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:PRK05201 395 LHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 8-455 0e+00

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 876.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   8 TMTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:COG1220    3 ELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPRRAAGIG----FDPEAARNEPSSQD 163
Cdd:COG1220   83 ATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGsnnpFEEEEEEEEEEEEI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 164 NETRIKFRRMLRNGELDEREIELDVAVNAS--MDIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAG 241
Cdd:COG1220  163 SRTREKFRKKLREGELDDREIEIEVEESSSpgVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEEAA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 242 KLVNEDDVRTAAIEACEQHGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGA 321
Cdd:COG1220  243 KLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRG--GGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 322 FHLAKPSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQEN 401
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499665579 402 IGARRLHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:COG1220  401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 9-455 0e+00

ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of HslVU, while the proteasome-related peptidase subunit is HslV. Residues 54-61 of the model contain a P-loop ATP-binding motif. Cys-287 of E. coli (position 308 in the seed alignment) is Ser in other members of the seed alignment. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273052 [Multi-domain]  Cd Length: 441  Bit Score: 644.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579    9 MTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEA 88
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   89 TRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPrrAAGIGFDPEAARNEPSSQdnetRI 168
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLP--PAKNQWGQTEQQQEPESA----RE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  169 KFRRMLRNGELDEREIELDVAVNASM--DIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAGKLVNE 246
Cdd:TIGR00390 155 AFRKKLREGELDDKEIEIDVSAKMPSgiEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  247 DDVRTAAIEACEQHGIVFIDEIDKVAKRGEagSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAK 326
Cdd:TIGR00390 235 EEIKQEAIDAVEQSGIIFIDEIDKIAKKGE--SSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAK 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  327 PSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQENIGARR 406
Cdd:TIGR00390 313 PSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARR 392

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 499665579  407 LHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:TIGR00390 393 LHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 10-344 1.48e-105

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: 310.85  E-value: 1.48e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  10 TPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEAT 89
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  90 RFTEVGYVGKDVEQIIRDLADtsvklyreqakvrvrnqaeeraedrildallprraagigfdpeaarnepssqdnetrik 169
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 170 frrmlrngeldereieldvavnasmdimtppgmeemgqqlrqmfsnlgsgksqkrkltikaarpllieeeagklvneddv 249
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 250 rtaaieaceqhGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAKPSD 329
Cdd:cd19498  102 -----------GIVFIDEIDKIAKRG--GSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSD 168

                        330
                 ....*....|....*
gi 499665579 330 LIPELQGRFPIRVEL 344
Cdd:cd19498  169 LIPELQGRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 198-341 1.35e-27

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: 108.05  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  198 TPPGMEEMGQQLRQMFSNLgsgksqKRKLTIKAARPLLIEeeagKLVNEDDVRTAAIEACEQHG------------IVFI 265
Cdd:pfam07724  12 TGVGKTELAKALAELLFGD------ERALIRIDMSEYMEE----HSVSRLIGAPPGYVGYEEGGqlteavrrkpysIVLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  266 DEIDKVAKrgeagssggdvsreGVQRDLLPLVEGSNVSTKYG-TVKTDHILFIASGAFHLAKPSD--------------- 329
Cdd:pfam07724  82 DEIEKAHP--------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellke 147

                         170       180
                  ....*....|....*....|.
gi 499665579  330 ---------LIPELQGRFPIR 341
Cdd:pfam07724 148 evmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 347-434 5.51e-14

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: 67.08  E-value: 5.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   347 LTKADFVRILTEPKAALIKQYEallqTEGVALTFAPDAVDRLAEIAAqvnerQENIGARRLHTVLERLLDVLSYEAP--- 423
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGY-----DPKYGARPLRRIIQRELEDPLAELIlsg 71

                           90
                   ....*....|..
gi 499665579   424 -DRDGQSVTVDA 434
Cdd:smart01086  72 eLKDGDTVVVDV 83
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
8-455 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 876.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   8 TMTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:PRK05201   3 ELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPRRAAGIGFdpeaarNEPSSQDNETR 167
Cdd:PRK05201  83 ATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGE------EEEKEEISATR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 168 IKFRRMLRNGELDEREIELDVAVNAS-MDIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAGKLVNE 246
Cdd:PRK05201 157 QKFRKKLREGELDDKEIEIEVAEAAPmMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDM 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 247 DDVRTAAIEACEQHGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAK 326
Cdd:PRK05201 237 EEIKQEAIERVEQNGIVFIDEIDKIAARG--GSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 327 PSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQENIGARR 406
Cdd:PRK05201 315 PSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARR 394

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 499665579 407 LHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:PRK05201 395 LHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 8-455 0e+00

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 876.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   8 TMTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:COG1220    3 ELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPRRAAGIG----FDPEAARNEPSSQD 163
Cdd:COG1220   83 ATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGsnnpFEEEEEEEEEEEEI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 164 NETRIKFRRMLRNGELDEREIELDVAVNAS--MDIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAG 241
Cdd:COG1220  163 SRTREKFRKKLREGELDDREIEIEVEESSSpgVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEEAA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 242 KLVNEDDVRTAAIEACEQHGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGA 321
Cdd:COG1220  243 KLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRG--GGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 322 FHLAKPSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQEN 401
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499665579 402 IGARRLHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:COG1220  401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 9-455 0e+00

ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of HslVU, while the proteasome-related peptidase subunit is HslV. Residues 54-61 of the model contain a P-loop ATP-binding motif. Cys-287 of E. coli (position 308 in the seed alignment) is Ser in other members of the seed alignment. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273052 [Multi-domain]  Cd Length: 441  Bit Score: 644.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579    9 MTPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEA 88
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   89 TRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQAEERAEDRILDALLPrrAAGIGFDPEAARNEPSSQdnetRI 168
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLP--PAKNQWGQTEQQQEPESA----RE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  169 KFRRMLRNGELDEREIELDVAVNASM--DIMTPPGMEEMGQQLRQMFSNLGSGKSQKRKLTIKAARPLLIEEEAGKLVNE 246
Cdd:TIGR00390 155 AFRKKLREGELDDKEIEIDVSAKMPSgiEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  247 DDVRTAAIEACEQHGIVFIDEIDKVAKRGEagSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAK 326
Cdd:TIGR00390 235 EEIKQEAIDAVEQSGIIFIDEIDKIAKKGE--SSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAK 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  327 PSDLIPELQGRFPIRVELTALTKADFVRILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAQVNERQENIGARR 406
Cdd:TIGR00390 313 PSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARR 392

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 499665579  407 LHTVLERLLDVLSYEAPDRDGQSVTVDAAYVDAQLGELVQDPDLSRYIL 455
Cdd:TIGR00390 393 LHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 10-344 1.48e-105

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: 310.85  E-value: 1.48e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  10 TPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEAT 89
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  90 RFTEVGYVGKDVEQIIRDLADtsvklyreqakvrvrnqaeeraedrildallprraagigfdpeaarnepssqdnetrik 169
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 170 frrmlrngeldereieldvavnasmdimtppgmeemgqqlrqmfsnlgsgksqkrkltikaarpllieeeagklvneddv 249
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 250 rtaaieaceqhGIVFIDEIDKVAKRGeaGSSGGDVSREGVQRDLLPLVEGSNVSTKYGTVKTDHILFIASGAFHLAKPSD 329
Cdd:cd19498  102 -----------GIVFIDEIDKIAKRG--GSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSD 168

                        330
                 ....*....|....*
gi 499665579 330 LIPELQGRFPIRVEL 344
Cdd:cd19498  169 LIPELQGRFPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
10-445 1.33e-70

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 229.28  E-value: 1.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  10 TPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEV-MPK-NILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:PRK05342  61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVeLQKsNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIRDL---ADtsvklyreqakvrvrnqaeeraedrildallprraagigFDPEAArnepssqdn 164
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILLKLlqaAD---------------------------------------YDVEKA--------- 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 165 etrikfrrmlrngeldereieldvavnasmdimtppgmeemgqqlrqmfsnlgsgksqkrkltikaarpllieeeagklv 244
Cdd:PRK05342     --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 245 neddvrtaaieaceQHGIVFIDEIDKVAKRGEAGSSGGDVSREGVQRDLLPLVEGS--NVSTKYG---------TVKTDH 313
Cdd:PRK05342 173 --------------QRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTvaSVPPQGGrkhpqqefiQVDTTN 238

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 314 ILFIASGAF-----------------------------------HLAKPSDL-----IPELQGRFPIRVELTALTKADFV 353
Cdd:PRK05342 239 ILFICGGAFdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLPVVATLEELDEEALV 318

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 354 RILTEPKAALIKQYEALLQTEGVALTFAPDAVDRLAEIAAqvnERqeNIGARRLHTVLER-LLDVLsYEAPDRDG-QSVT 431
Cdd:PRK05342 319 RILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAI---ER--KTGARGLRSILEEiLLDVM-FELPSREDvEKVV 392

                        490
                 ....*....|....
gi 499665579 432 VDAAYVDAQLGELV 445
Cdd:PRK05342 393 ITKEVVEGKAKPLL 406
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 10-438 1.31e-69

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 226.47  E-value: 1.31e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  10 TPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRNEV-MPK-NILMIGPTGVGKTEIARRLATLANAPFVKVE 87
Cdd:COG1219   62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVeLEKsNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  88 ATRFTEVGYVGKDVEQIIrdladtsVKLYReqakvrvrnqaeeraedrildallprrAAGigFDPEAArnepssqdnetr 167
Cdd:COG1219  142 ATTLTEAGYVGEDVENIL-------LKLLQ---------------------------AAD--YDVEKA------------ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 168 ikfrrmlrngeldereieldvavnasmdimtppgmeemgqqlrqmfsnlgsgksqkrkltikaarpllieeeagklvned 247
Cdd:COG1219      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 248 dvrtaaieaceQHGIVFIDEIDKVAKRGEAGSSGGDVSREGVQRDLLPLVEGS--NVSTKYG---------TVKTDHILF 316
Cdd:COG1219  174 -----------ERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTvaNVPPQGGrkhpqqefiQIDTTNILF 242

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 317 IASGAF----------------------------------HLAKPSDL-----IPELQGRFPIRVELTALTKADFVRILT 357
Cdd:COG1219  243 ICGGAFdglekiierrlgkksigfgaevkskkekdegellKQVEPEDLikfglIPEFIGRLPVIATLEELDEEALVRILT 322

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 358 EPKAALIKQYEALLQTEGVALTFAPDAvdrLAEIAAQVNERqeNIGARRLHTVLER-LLDVLsYEAPDRDG-QSVTVDAA 435
Cdd:COG1219  323 EPKNALVKQYQKLFEMDGVELEFTDEA---LEAIAKKAIER--KTGARGLRSILEEiLLDVM-YELPSRKDvKKVVITKE 396


                 ...
gi 499665579 436 YVD 438
Cdd:COG1219  397 VVE 399
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 10-441 5.36e-45

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 161.86  E-value: 5.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   10 TPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRN----EVMPKNILMIGPTGVGKTEIARRLATLANAPFVK 85
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   86 VEATRFTEVGYVGKDVEQIIrdladtsvklyreqakvrvrnqaeeraedrildallprraagigfdpeaarnepssqdne 165
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENIL------------------------------------------------------------ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  166 trikfRRMLRNGELDereieldvavnasmdimtppgmeemgqqlrqmfsnlgsgksqkrkltikaarplliEEEAgklvn 245
Cdd:TIGR00382 167 -----LKLLQAADYD--------------------------------------------------------VEKA----- 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  246 eddvrtaaieaceQHGIVFIDEIDKVAKRGEAGSSGGDVSREGVQRDLLPLVEGS--NVSTKYG---------TVKTDHI 314
Cdd:TIGR00382 181 -------------QKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTvaNVPPQGGrkhpyqefiQIDTSNI 247

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  315 LFIASGAF---------------------------------HLAKPSD-----LIPELQGRFPIRVELTALTKADFVRIL 356
Cdd:TIGR00382 248 LFICGGAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLIPEFIGRLPVIATLEKLDEEALIAIL 327

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  357 TEPKAALIKQYEALLQTEGVALTFAPDAVDrlaEIAAQVNERqeNIGARRLHTVLERLLDVLSYEAPDR-DGQSVTVDAA 435
Cdd:TIGR00382 328 TKPKNALVKQYQALFKMDNVELDFEEEALK---AIAKKALER--KTGARGLRSIVEGLLLDVMFDLPSLeDLEKVVITKE 402


                  ....*.
gi 499665579  436 YVDAQL 441
Cdd:TIGR00382 403 TVLKQS 408
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 10-344 1.88e-34

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: 129.26  E-value: 1.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  10 TPREIVQELDRHIVGQHDAKRAVAIALRNRWRRMQLPEELRN---EVMPKNILMIGPTGVGKTEIARRLATLANAPFVKV 86
Cdd:cd19497    2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  87 EATRFTEVGYVGKDVEQIIrdladtsvklyreqakvrvrnqaeeraedrildallprraagigfdpeaarnepssqdnet 166
Cdd:cd19497   82 DATTLTEAGYVGEDVENIL------------------------------------------------------------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 167 rikfRRMLRNGELDereieldvavnasmdimtppgmeemgqqlrqmfsnlgsgksqkrkltikaarpllieeeagklvne 246
Cdd:cd19497  101 ----LKLLQAADYD------------------------------------------------------------------ 110

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 247 ddvrtaaIEACEQhGIVFIDEIDKVAKRGEAGSSGGDVSREGVQRDLLPLVEGS--NVSTKYG---------TVKTDHIL 315
Cdd:cd19497  111 -------VERAQR-GIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTvaNVPPQGGrkhpqqefiQVDTTNIL 182

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499665579 316 FIASGAF-----------------------------------HLAKPSDL-----IPELQGRFPIRVEL 344
Cdd:cd19497  183 FICGGAFvglekiiarrlgkkslgfgaetssekdekerdellSKVEPEDLikfglIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 198-341 1.35e-27

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: 108.05  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  198 TPPGMEEMGQQLRQMFSNLgsgksqKRKLTIKAARPLLIEeeagKLVNEDDVRTAAIEACEQHG------------IVFI 265
Cdd:pfam07724  12 TGVGKTELAKALAELLFGD------ERALIRIDMSEYMEE----HSVSRLIGAPPGYVGYEEGGqlteavrrkpysIVLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  266 DEIDKVAKrgeagssggdvsreGVQRDLLPLVEGSNVSTKYG-TVKTDHILFIASGAFHLAKPSD--------------- 329
Cdd:pfam07724  82 DEIEKAHP--------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellke 147

                         170       180
                  ....*....|....*....|.
gi 499665579  330 ---------LIPELQGRFPIR 341
Cdd:pfam07724 148 evmdllkkgFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 28-112 1.78e-14

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: 70.77  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  28 AKRAVAIALRNRWRRMQLpeELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTE--VGYVGKDVEQII 105
Cdd:cd19481    1 LKASLREAVEAPRRGSRL--RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78


                 ....*..
gi 499665579 106 RDLADTS 112
Cdd:cd19481   79 ERARRLA 85
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 347-434 5.51e-14

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: 67.08  E-value: 5.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   347 LTKADFVRILTEPKAALIKQYEallqTEGVALTFAPDAVDRLAEIAAqvnerQENIGARRLHTVLERLLDVLSYEAP--- 423
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGY-----DPKYGARPLRRIIQRELEDPLAELIlsg 71

                           90
                   ....*....|..
gi 499665579   424 -DRDGQSVTVDA 434
Cdd:smart01086  72 eLKDGDTVVVDV 83
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 14-76 4.75e-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: 52.56  E-value: 4.75e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499665579  14 IVQELDRHIVGQHDAKRAVAIALRnrwrrmQLPEELRNEVMPK-NILMIGPTGVGKTEIARRLA 76
Cdd:cd19499    5 LEERLHERVVGQDEAVKAVSDAIR------RARAGLSDPNRPIgSFLFLGPTGVGKTELAKALA 62
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 23-108 2.63e-07

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: 49.84  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  23 VGQHDAKRAVAIALRNRwrrmqlpeelrnevMPKNILMIGPTGVGKTEIARRLATLA---NAPFVKVEATRFTEVGYVGK 99
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66


                 ....*....
gi 499665579 100 DVEQIIRDL 108
Cdd:cd00009   67 LFGHFLVRL 75
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 9-89 6.00e-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: 50.94  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   9 MTPREIVQELDRHIVGQHDAKRAVAIALRNRwrrmqlpeelrnevmpKNILMIGPTGVGKTEIARRLATLANAPFVKVEA 88
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAG----------------GHLLLEGVPGVGKTTLAKALARALGLPFIRIQF 64


                 .
gi 499665579  89 T 89
Cdd:COG0714   65 T 65
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 217-344 7.10e-07

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: 48.36  E-value: 7.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  217 GSGKSqkrkLTIKA-ARPL---LIEEEAGKLVN------EDDVRTAAIEACEQ-HGIVFIDEIDKVAKRgeaGSSGGDVS 285
Cdd:pfam00004   8 GTGKT----TLAKAvAKELgapFIEISGSELVSkyvgesEKRLRELFEAAKKLaPCVIFIDEIDALAGS---RGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499665579  286 REGVQRDLLPLVEGsnvstkyGTVKTDHILFIASGafhlAKPSDLIPELQGRFPIRVEL 344
Cdd:pfam00004  81 SRRVVNQLLTELDG-------FTSSNSKVIVIAAT----NRPDKLDPALLGRFDRIIEF 128
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 4-78 1.49e-06

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 50.42  E-value: 1.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499665579   4 PDTATMTPREIVQELD-RHIVGQHDAKRAVAIAlrnrwrrmqlpeelrnevmpkNILMIGPTGVGKTEIARRLATL 78
Cdd:COG0606  175 PAEPDAPPAEPPYEPDlADVKGQEQAKRALEIAaag----------------ghNLLMIGPPGSGKTMLARRLPGI 234
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 22-108 2.97e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 48.85  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  22 IVGQHDAKR----AVAIALRNrwrrmqlPEELRNE--VMPKNILMIGPTGVGKTEIARRLATLANAPFVKVeatRFTEV- 94
Cdd:COG1222   80 IGGLDEQIEeireAVELPLKN-------PELFRKYgiEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRV---RGSELv 149

                         90
                 ....*....|....*
gi 499665579  95 -GYVGKDvEQIIRDL 108
Cdd:COG1222  150 sKYIGEG-ARNVREV 163
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 54-149 3.04e-06

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: 47.23  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  54 MPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVgYVGKDVEQiIRDLAdtsvklyreqakvrvrNQAEERAE 133
Cdd:cd19501   36 IPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGASR-VRDLF----------------EQAKKNAP 97

                         90       100
                 ....*....|....*....|.
gi 499665579 134 -----DRIlDALLPRRAAGIG 149
Cdd:cd19501   98 civfiDEI-DAVGRKRGAGLG 117
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 58-142 3.32e-06

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: 46.43  E-value: 3.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   58 ILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVGkDVEQIIRDLADTSvklyREQAK-----------VRVRN 126
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFEAA----KKLAPcvifideidalAGSRG 74

                          90
                  ....*....|....*.
gi 499665579  127 QAEERAEDRILDALLP 142
Cdd:pfam00004  75 SGGDSESRRVVNQLLT 90
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 22-78 3.03e-05

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: 44.83  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499665579   22 IVGQHDAKRAVAIALRNRwrrmqlpeelrnevmpKNILMIGPTGVGKTEIARRLATL 78
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGG----------------HNLLMIGPPGSGKTMLAKRLPGI 45
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
54-114 8.34e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 45.03  E-value: 8.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499665579  54 MPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVgYVGKDVEQiIRDLADTSVK 114
Cdd:PRK10733 184 IPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASR-VRDMFEQAKK 242
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 55-115 9.10e-05

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: 42.78  E-value: 9.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFteVGYVGKDVEQIIRDLADTSVKL 115
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAISN 92
ftsH CHL00176
cell division protein; Validated
 55-162 1.22e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 44.66  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVgYVGkdveqiirdladtsvklyreQAKVRVRN---QAEER 131
Cdd:CHL00176 216 PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVG--------------------VGAARVRDlfkKAKEN 274

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499665579 132 AE-----DRIlDALLPRRAAGIGfdpeaARNEPSSQ 162
Cdd:CHL00176 275 SPcivfiDEI-DAVGRQRGAGIG-----GGNDEREQ 304
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 22-106 1.56e-04

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: 43.75  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  22 IVGQHDAKRAvaiaLRNRWRRMQLPEELRNE---VMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVG 98
Cdd:COG0464  159 LGGLEEVKEE----LRELVALPLKRPELREEyglPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233

                         90
                 ....*....|.
gi 499665579  99 ---KDVEQIIR 106
Cdd:COG0464  234 eteKNLREVFD 244
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 22-115 1.65e-04

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: 41.95  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  22 IVGQHDAKRAVAIALRNRWRRMQLPEELRNevMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTeVGYVGkDV 101
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRG--PPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG-ES 76

                         90
                 ....*....|....
gi 499665579 102 EQIIRDLADTSVKL 115
Cdd:cd19509   77 EKIVRALFALAREL 90
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 57-93 1.68e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 41.51  E-value: 1.68e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 499665579   57 NILMIGPTGVGKTEIARRLAT-LANAPFVKVEATRFTE 93
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 22-110 2.30e-04

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: 41.89  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  22 IVGQHDAKRAV--AIALRnrwrrMQLPEELRNEVMP-KNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVG 98
Cdd:cd19522    2 IADLEEAKKLLeeAVVLP-----MWMPEFFKGIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTS-KYRG 75

                         90
                 ....*....|..
gi 499665579  99 KDvEQIIRDLAD 110
Cdd:cd19522   76 ES-EKLVRLLFE 86
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 55-174 3.83e-04

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: 41.51  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVGKDvEQIIRDLadTSVKLYREQAKVRV---------R 125
Cdd:cd19525   55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVGEG-EKMVRAL--FSVARCKQPAVIFIdeidsllsqR 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499665579 126 NQAEERAEDRILDALLPrRAAGIGFDPE------AARNEPSSQDNETRIKFRRML 174
Cdd:cd19525  131 GEGEHESSRRIKTEFLV-QLDGATTSSEdrilvvGATNRPQEIDEAARRRLVKRL 184
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 55-127 4.33e-04

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: 40.43  E-value: 4.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499665579    55 PKNILMIGPTGVGKTEIARRLATLANAP---FVKVEATRFTEVGYVGKDVEQIIRDLADTSVKLYREQAKVRVRNQ 127
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 226-344 4.96e-04

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: 40.59  E-value: 4.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579 226 LTIKAARPLLIEEEAGKLVNEDDVRTAAIEACEQHGIVFIDEIDKVakrgeagssggdvsREGVQRDLLPLVEGSNvstk 305
Cdd:cd00009   51 LYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL--------------SRGAQNALLRVLETLN---- 112

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499665579 306 YGTVKTDHILFIASGAFHLakPSDLIPELQGRFPIRVEL 344
Cdd:cd00009  113 DLRIDRENVRVIGATNRPL--LGDLDRALYDRLDIRIVI 149
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 55-186 6.76e-04

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: 40.35  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEAtrftevgyvgkdvEQIIRDLADTSVKLYREqakvrVRNQAEERAED 134
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISG-------------PSIVSKYLGESEKNLRE-----IFEEARSHAPS 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499665579 135 RI----LDALLPRRAA------------------GIGFDPE----AARNEPSSQDNETRikfrrmlRNGELDeREIEL 186
Cdd:cd19503   96 IIfideIDALAPKREEdqreverrvvaqlltlmdGMSSRGKvvviAATNRPDAIDPALR-------RPGRFD-REVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 55-108 7.73e-04

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: 39.96  E-value: 7.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVgYVGkDVEQIIRDL 108
Cdd:cd19511   27 PKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK-YVG-ESERAVREI 78
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 22-108 8.99e-04

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: 39.83  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  22 IVGQHDAKRAVAIALRNRWRRMQLPEELRNEvmPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVGkDV 101
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLRAP--ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77


                 ....*..
gi 499665579 102 EQIIRDL 108
Cdd:cd19524   78 EKLVRAL 84
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 55-106 9.29e-04

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: 39.79  E-value: 9.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTE--VGYVGKDVEQIIR 106
Cdd:cd19529   27 PKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVGESEKAIREIFR 80
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 55-108 1.05e-03

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: 39.63  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499665579  55 PKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVGkDVEQIIRDL 108
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVREL 88
clpC CHL00095
Clp protease ATP binding subunit
 17-98 1.14e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 41.58  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  17 ELDRHIVGQHDAKRAVAIALRnRWRrmqlpEELRNEVMP-KNILMIGPTGVGKTEIARRLATL---ANAPFVKVEATRFT 92
Cdd:CHL00095 506 TLHKRIIGQDEAVVAVSKAIR-RAR-----VGLKNPNRPiASFLFSGPTGVGKTELTKALASYffgSEDAMIRLDMSEYM 579

                         90
                 ....*....|....*..
gi 499665579  93 E-----------VGYVG 98
Cdd:CHL00095 580 EkhtvskligspPGYVG 596
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 41-72 1.18e-03

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 39.94  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499665579  41 RRMQLpeELRNEVMPKNILMIGPTGVGKTEIA 72
Cdd:cd18034    4 RSYQL--ELFEAALKRNTIVVLPTGSGKTLIA 33
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
16-93 1.43e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 40.98  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  16 QELDRHIVGQHDAKRAVAIALRNRwrRMQLPEELRnevmP-KNILMIGPTGVGKTEIARRLATL---ANAPFVKVEATRF 91
Cdd:PRK10865 564 QELHHRVIGQNEAVEAVSNAIRRS--RAGLSDPNR----PiGSFLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEF 637


                 ..
gi 499665579  92 TE 93
Cdd:PRK10865 638 ME 639
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 16-76 1.87e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499665579  16 QELDRHIVGQHDAKRAVAIALRnRWR-RMQLPEelrnevmpKNI---LMIGPTGVGKTEIARRLA 76
Cdd:COG0542  545 EELHERVIGQDEAVEAVADAIR-RSRaGLKDPN--------RPIgsfLFLGPTGVGKTELAKALA 600
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 30-143 4.69e-03

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: 37.51  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  30 RAVAIALRNrwrrmqlpeELRNEVMPKNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEVGYVGKDVEQIIRDLA 109
Cdd:cd19512    6 RDIAIATRN---------TKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499665579 110 DTSVK---LYREQAKVRVRNQAEER-AEDR--ILDALLPR 143
Cdd:cd19512   77 NTSRRgllLFVDEADAFLRKRSTEKiSEDLraALNAFLYR 116
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 262-296 5.05e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.05  E-value: 5.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 499665579 262 IVFIDEIDKV-AKRGEAGSSGgdvSREgVQRDLLPL 296
Cdd:PRK03992 227 IIFIDEIDAIaAKRTDSGTSG---DRE-VQRTLMQL 258
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 56-172 5.08e-03

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: 37.92  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579  56 KNILMIGPTGVGKTEIARRLATLANAPFVKVEATRFTEvGYVGkDVEQIIRDLadtsVKLYREQAKVRV----------- 124
Cdd:cd19521   41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS-KWMG-ESEKLVKQL----FAMARENKPSIIfidevdslcgt 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499665579 125 RNQAEERAEDRILDALLPrRAAGIGFDPE-----AARNEPSSQDNETRIKFRR 172
Cdd:cd19521  115 RGEGESEASRRIKTELLV-QMNGVGNDSQgvlvlGATNIPWQLDSAIRRRFEK 166
AAA_22 pfam13401
AAA domain;
58-141 7.27e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.55  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499665579   58 ILMIGPTGVGKTEIARRLATL---ANAPFVKVEATRFTevgyvgkDVEQIIRDLA-DTSVKLYREQAKVRVRNQAEERAE 133
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpeVRDSVVFVDLPSGT-------SPKDLLRALLrALGLPLSGRLSKEELLAALQQLLL 80


                  ....*...
gi 499665579  134 DRILDALL 141
Cdd:pfam13401  81 ALAVAVVL 88
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 57-84 9.31e-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: 36.76  E-value: 9.31e-03
                         10        20
                 ....*....|....*....|....*...
gi 499665579  57 NILMIGPTGVGKTEIARRLATLANAPFV 84
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 60-105 9.40e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.14  E-value: 9.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 499665579  60 MI--GPTGVGKTEIARRLATLANAPFVKVEATrFTEVgyvgKDVEQII 105
Cdd:PRK13342  39 MIlwGPPGTGKTTLARIIAGATDAPFEALSAV-TSGV----KDLREVI 81
 
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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