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Conserved domains on  [gi|1017579656|emb|SAC86785|]
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ATP-dependent hsl protease ATP-binding subunit HslU [Enterobacter ludwigii]

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;
1-443 0e+00

ATP-dependent protease ATPase subunit HslU;


:

Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 936.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   1 MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201    1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  81 VEATKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQAEQQAEPSAARQAFR 160
Cdd:PRK05201   81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 161 KKLREGELDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELK 240
Cdd:PRK05201  161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 241 QDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIP 320
Cdd:PRK05201  241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 321 ELQGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLE 400
Cdd:PRK05201  321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1017579656 401 RLMEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:PRK05201  401 KLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-443 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 936.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   1 MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201    1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  81 VEATKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQAEQQAEPSAARQAFR 160
Cdd:PRK05201   81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 161 KKLREGELDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELK 240
Cdd:PRK05201  161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 241 QDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIP 320
Cdd:PRK05201  241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 321 ELQGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLE 400
Cdd:PRK05201  321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1017579656 401 RLMEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:PRK05201  401 KLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-443 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: 909.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   1 MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220     1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  81 VEATKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQ----------AEQQA 150
Cdd:COG1220    81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSnnpfeeeeeeEEEEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 151 EPSAARQAFRKKLREGELDDKEIEIDLAAAP-MGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEE 229
Cdd:COG1220   161 EISRTREKFRKKLREGELDDREIEIEVEESSsPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 230 AAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGA 309
Cdd:COG1220   241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 310 FQVAKPSDLIPELQGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTEN 389
Cdd:COG1220   321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1017579656 390 IGARRLHTVLERLMEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:COG1220   401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-443 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: 766.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   4 MTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  84 TKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQAEQQAEPSAARQAFRKKL 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEPESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 164 REGELDDKEIEIDLAAA-PMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQD 242
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKmPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 243 AIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIPEL 322
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 323 QGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLERL 402
Cdd:TIGR00390 321 QGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERL 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1017579656 403 MEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:TIGR00390 401 LEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-332 5.27e-110

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: 322.02  E-value: 5.27e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   5 TPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  85 KFTEVGYVGKEVDSIIRDLTDsaikmvrvqaieknryraeemaeerildvlippaknnwgqaeqqaepsaarqafrkklr 164
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 165 egelddkeieidlaaapmgveimappgmeemtsqlqsmfqnlggqkqkarklkikdamkllieeeaaklvnpeelkqdai 244
Cdd:cd19498       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 245 daveqhGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIPELQG 324
Cdd:cd19498   102 ------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQG 175


                  ....*...
gi 1017579656 325 RLPIRVEL 332
Cdd:cd19498   176 RFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 170-329 2.76e-29

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: 112.29  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 170 DKEIEIDLAAaPMGVeimAPPGMEEMTSQLQSMFQnlggqkqkaRKLKIKDAMKLLIEeeaaKLVNPEELKQDAIDAVEQ 249
Cdd:pfam07724   1 RPIGSFLFLG-PTGV---GKTELAKALAELLFGDE---------RALIRIDMSEYMEE----HSVSRLIGAPPGYVGYEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 250 HG------------IVFIDEIDKICKrgessgpdvsreGVQRDLLPLVEGCTVSTKHG-MVKTDHILFIASGAFQVAKPS 316
Cdd:pfam07724  64 GGqlteavrrkpysIVLIDEIEKAHP------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKIS 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1017579656 317 D------------------------LIPELQGRLPIR 329
Cdd:pfam07724 132 DasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 335-423 1.13e-12

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: 63.62  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  335 LTTEDFERILTEPNASVTVQYkalmATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLMEDISYDA---- 410
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|...
gi 1017579656  411 SDLNGQSITIDAE 423
Cdd:smart01086  72 ELKDGDTVVVDVD 84
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-443 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 936.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   1 MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201    1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  81 VEATKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQAEQQAEPSAARQAFR 160
Cdd:PRK05201   81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 161 KKLREGELDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELK 240
Cdd:PRK05201  161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 241 QDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIP 320
Cdd:PRK05201  241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 321 ELQGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLE 400
Cdd:PRK05201  321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1017579656 401 RLMEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:PRK05201  401 KLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-443 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: 909.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   1 MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220     1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  81 VEATKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQ----------AEQQA 150
Cdd:COG1220    81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSnnpfeeeeeeEEEEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 151 EPSAARQAFRKKLREGELDDKEIEIDLAAAP-MGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEE 229
Cdd:COG1220   161 EISRTREKFRKKLREGELDDREIEIEVEESSsPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 230 AAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGA 309
Cdd:COG1220   241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 310 FQVAKPSDLIPELQGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTEN 389
Cdd:COG1220   321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1017579656 390 IGARRLHTVLERLMEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:COG1220   401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-443 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: 766.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   4 MTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  84 TKFTEVGYVGKEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERILDVLIPPAKNNWGQAEQQAEPSAARQAFRKKL 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEPESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 164 REGELDDKEIEIDLAAA-PMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQD 242
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKmPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 243 AIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIPEL 322
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 323 QGRLPIRVELQALTTEDFERILTEPNASVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLERL 402
Cdd:TIGR00390 321 QGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERL 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1017579656 403 MEDISYDASDLNGQSITIDAEYVGKHLDALVADEDLSRFIL 443
Cdd:TIGR00390 401 LEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-332 5.27e-110

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: 322.02  E-value: 5.27e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   5 TPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  85 KFTEVGYVGKEVDSIIRDLTDsaikmvrvqaieknryraeemaeerildvlippaknnwgqaeqqaepsaarqafrkklr 164
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 165 egelddkeieidlaaapmgveimappgmeemtsqlqsmfqnlggqkqkarklkikdamkllieeeaaklvnpeelkqdai 244
Cdd:cd19498       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 245 daveqhGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVAKPSDLIPELQG 324
Cdd:cd19498   102 ------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQG 175


                  ....*...
gi 1017579656 325 RLPIRVEL 332
Cdd:cd19498   176 RFPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
5-437 1.60e-65

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 215.79  E-value: 1.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   5 TPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEV--TPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:PRK05342   61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVelQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  83 ATKFTEVGYVGKEVDSIIRDLtdsaikmvrvqaieknryraeemaeerildvlippaknnwgqaeqqaepsaarqafrkk 162
Cdd:PRK05342  141 ATTLTEAGYVGEDVENILLKL----------------------------------------------------------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 163 lregelddkeieidLAAAPMGVEimappgmeemtsqlqsmfqnlggqkqKArklkikdamkllieeeaaklvnpeelkqd 242
Cdd:PRK05342  162 --------------LQAADYDVE--------------------------KA----------------------------- 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 243 aidaveQHGIVFIDEIDKICKRGE--SSGPDVSREGVQRDLLPLVEGCTVST------KHGM-----VKTDHILFIASGA 309
Cdd:PRK05342  173 ------QRGIVYIDEIDKIARKSEnpSITRDVSGEGVQQALLKILEGTVASVppqggrKHPQqefiqVDTTNILFICGGA 246

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 310 F-----------------------------------QVAKPSDL-----IPELQGRLPIRVELQALTTEDFERILTEPNA 349
Cdd:PRK05342  247 FdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLPVVATLEELDEEALVRILTEPKN 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 350 SVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLMEDISYDA-SDLNGQSITIDAEYVGKH 428
Cdd:PRK05342  327 ALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMFELpSREDVEKVVITKEVVEGK 401


                  ....*....
gi 1017579656 429 LDALVADED 437
Cdd:PRK05342  402 AKPLLIYRE 410
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-433 8.53e-61

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 203.36  E-value: 8.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   5 TPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRHEVT-PK-NILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:COG1219    62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVElEKsNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  83 ATKFTEVGYVGKEVDSIIRDLTDSAikmvrvqaieknryraeemaeerildvlippaknnwgqaeqqaepsaarqafrkk 162
Cdd:COG1219   142 ATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 163 lregeldDKEIEidlaaapmgveimappgmeemtsqlqsmfqnlggqkqKArklkikdamkllieeeaaklvnpeelkqd 242
Cdd:COG1219   167 -------DYDVE-------------------------------------KA----------------------------- 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 243 aidaveQHGIVFIDEIDKICKRGE--SSGPDVSREGVQRDLLPLVEGCTVST------KHGM-----VKTDHILFIASGA 309
Cdd:COG1219   174 ------ERGIIYIDEIDKIARKSEnpSITRDVSGEGVQQALLKILEGTVANVppqggrKHPQqefiqIDTTNILFICGGA 247

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 310 F-----------------------------------QVAkPSDL-----IPELQGRLPIRVELQALTTEDFERILTEPNA 349
Cdd:COG1219   248 FdglekiierrlgkksigfgaevkskkekdegellkQVE-PEDLikfglIPEFIGRLPVIATLEELDEEALVRILTEPKN 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 350 SVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLMEDISYDA-SDLNGQSITIDAEYVGKH 428
Cdd:COG1219   327 ALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMYELpSRKDVKKVVITKEVVEGK 401


                  ....*
gi 1017579656 429 LDALV 433
Cdd:COG1219   402 AKPIL 406
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 5-433 1.44e-40

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: 149.53  E-value: 1.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   5 TPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRH----EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  81 VEATKFTEVGYVGKEVDSIirdltdsaikmvrvqaieknryraeemaeerildvlippaknnwgqaeqqaepsaarqafr 160
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENI------------------------------------------------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 161 kklregelddkeieidlaaapmgveimappgmeemtsqLQSMFQNLGGQKQKARKlkikdamkllieeeaaklvnpeelk 240
Cdd:TIGR00382 166 --------------------------------------LLKLLQAADYDVEKAQK------------------------- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 241 qdaidaveqhGIVFIDEIDKICKRGE--SSGPDVSREGVQRDLLPLVEGCTVST------KHG-----MVKTDHILFIAS 307
Cdd:TIGR00382 183 ----------GIIYIDEIDKISRKSEnpSITRDVSGEGVQQALLKIIEGTVANVppqggrKHPyqefiQIDTSNILFICG 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 308 GAF---------------------------------QVAKPSD-----LIPELQGRLPIRVELQALTTEDFERILTEPNA 349
Cdd:TIGR00382 253 GAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLIPEFIGRLPVIATLEKLDEEALIAILTKPKN 332

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 350 SVTVQYKALMATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLMEDISYDASDL-NGQSITIDAEYVGKH 428
Cdd:TIGR00382 333 ALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFDLPSLeDLEKVVITKETVLKQ 407


                  ....*
gi 1017579656 429 LDALV 433
Cdd:TIGR00382 408 SEPLL 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 5-332 4.70e-32

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: 122.32  E-value: 4.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   5 TPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLEEELRH---EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:cd19497     2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  82 EATKFTEVGYVGKEVDSIIRDLtdsaikmvrvqaieknryraeemaeerildvlippaknnwgqaeqqaepsaarqafrk 161
Cdd:cd19497    82 DATTLTEAGYVGEDVENILLKL---------------------------------------------------------- 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 162 klregelddkeieidLAAAPMGVEimappgmeemtsqlqsmfqnlggqkqKArklkikdamkllieeeaaklvnpeelkq 241
Cdd:cd19497   104 ---------------LQAADYDVE--------------------------RA---------------------------- 114

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 242 daidaveQHGIVFIDEIDKICKRGESSG--PDVSREGVQRDLLPLVEGCTVST------KHG-----MVKTDHILFIASG 308
Cdd:cd19497   115 -------QRGIVYIDEIDKIARKSENPSitRDVSGEGVQQALLKILEGTVANVppqggrKHPqqefiQVDTTNILFICGG 187

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017579656 309 AFQ-----VAK------------------------------PSDL-----IPELQGRLPIRVEL 332
Cdd:cd19497   188 AFVglekiIARrlgkkslgfgaetssekdekerdellskvePEDLikfglIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 170-329 2.76e-29

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: 112.29  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 170 DKEIEIDLAAaPMGVeimAPPGMEEMTSQLQSMFQnlggqkqkaRKLKIKDAMKLLIEeeaaKLVNPEELKQDAIDAVEQ 249
Cdd:pfam07724   1 RPIGSFLFLG-PTGV---GKTELAKALAELLFGDE---------RALIRIDMSEYMEE----HSVSRLIGAPPGYVGYEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 250 HG------------IVFIDEIDKICKrgessgpdvsreGVQRDLLPLVEGCTVSTKHG-MVKTDHILFIASGAFQVAKPS 316
Cdd:pfam07724  64 GGqlteavrrkpysIVLIDEIEKAHP------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKIS 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1017579656 317 D------------------------LIPELQGRLPIR 329
Cdd:pfam07724 132 DasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 23-118 8.11e-16

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: 74.63  E-value: 8.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  23 AKRSVAIALRNRWRRMQLEEelRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVDSII 100
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRR--YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78

                          90
                  ....*....|....*...
gi 1017579656 101 RDLTDSAIKMVRVQAIEK 118
Cdd:cd19481    79 ERARRLAPCILFIDEIDA 96
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 335-423 1.13e-12

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: 63.62  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  335 LTTEDFERILTEPNASVTVQYkalmATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLMEDISYDA---- 410
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|...
gi 1017579656  411 SDLNGQSITIDAE 423
Cdd:smart01086  72 ELKDGDTVVVDVD 84
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 18-110 2.19e-08

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: 52.92  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  18 IGQDNAKRSVAIALRNRwrrmqleeelrhevTPKNILMIGPTGVGKTEIARRLAKLA---NAPFIKVEATKFTEVGYVGK 94
Cdd:cd00009     1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                          90
                  ....*....|....*.
gi 1017579656  95 EVDSIIRDLTDSAIKM 110
Cdd:cd00009    67 LFGHFLVRLLFELAEK 82
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 12-73 5.93e-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: 52.18  E-value: 5.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017579656  12 ELDKHIIGQDNAKRSVAIALRnrwrrmqleeELRHEVTPKN-----ILMIGPTGVGKTEIARRLAKL 73
Cdd:cd19499     8 RLHERVVGQDEAVKAVSDAIR----------RARAGLSDPNrpigsFLFLGPTGVGKTELAKALAEL 64
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 4-84 7.78e-08

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: 53.63  E-value: 7.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   4 MTPREIVSELDKHIIGQDNAKRSVAIALRNRwrrmqleeelRHevtpknILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:COG0714     1 MTEARLRAEIGKVYVGQEELIELVLIALLAG----------GH------LLLEGVPGVGKTTLAKALARALGLPFIRIQF 64


                  .
gi 1017579656  84 T 84
Cdd:COG0714    65 T 65
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 53-137 1.33e-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: 50.28  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  53 ILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDSAIKMVR-------VQAIEKNRYRAEE 125
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFEAAKKLAPcvifideIDALAGSRGSGGD 78

                          90
                  ....*....|..
gi 1017579656 126 MAEERILDVLIP 137
Cdd:pfam00004  79 SESRRVVNQLLT 90
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 3-107 6.57e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 50.78  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   3 EMTPREIVSELDKHIIGQDNAKRSVaialrnrwrRMQLEEELRH--------EVTPKNILMIGPTGVGKTEIARRLAKLA 74
Cdd:COG1222    66 TAVPAESPDVTFDDIGGLDEQIEEI---------REAVELPLKNpelfrkygIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1017579656  75 NAPFIKVEATKFTEvGYVGkEVDSIIRDLTDSA 107
Cdd:COG1222   137 GAPFIRVRGSELVS-KYIG-EGARNVREVFELA 167
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 15-107 7.02e-07

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: 49.15  E-value: 7.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  15 KHIIGQDNAKRSVAIA---LRNRWRRMQLEEELrhevtPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgY 91
Cdd:cd19501     4 KDVAGCEEAKEELKEVvefLKNPEKFTKLGAKI-----PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-F 77

                          90
                  ....*....|....*.
gi 1017579656  92 VGKEVdSIIRDLTDSA 107
Cdd:cd19501    78 VGVGA-SRVRDLFEQA 92
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 50-136 9.35e-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: 48.55  E-value: 9.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFteVGYVGKEVDSIIRDLTDSAIKMV-------RVQAIEKNRYR 122
Cdd:cd19518    34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAISNApcivfidEIDAITPKRES 111

                          90
                  ....*....|....
gi 1017579656 123 AEEMAEERILDVLI 136
Cdd:cd19518   112 AQREMERRIVSQLL 125
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 17-93 6.09e-06

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: 48.37  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  17 IIGQDNAKRsvaiALRNRWRRMQLEEELRHE---VTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG 93
Cdd:COG0464   159 LGGLEEVKE----ELRELVALPLKRPELREEyglPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 252-332 7.17e-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: 45.28  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656 252 IVFIDEIDKICKRGESSGPDVSREgVQRDLLPLVEGCTvstkhgmVKTDHILFIASGafqvAKPSDLIPELQGRLPIRVE 331
Cdd:pfam00004  60 VIFIDEIDALAGSRGSGGDSESRR-VVNQLLTELDGFT-------SSNSKVIVIAAT----NRPDKLDPALLGRFDRIIE 127


                  .
gi 1017579656 332 L 332
Cdd:pfam00004 128 F 128
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
17-109 1.77e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 46.95  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  17 IIGQDNAKRSVAIA---LRNRWRRMQLEEELrhevtPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVG 93
Cdd:PRK10733  154 VAGCDEAKEEVAELveyLREPSRFQKLGGKI-----PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVG 227

                          90
                  ....*....|....*.
gi 1017579656  94 KEVdSIIRDLTDSAIK 109
Cdd:PRK10733  228 VGA-SRVRDMFEQAKK 242
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 49-136 2.29e-05

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: 44.29  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656   49 TPKNILMIGPTGVGKTEIARRLAKLANAP---FIKVEATKFTEVGYVGKEVDSIIRDLTDSaikmVRVQAIEKnryrAEE 125
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASG----SGELRLRL----ALA 72

                           90
                   ....*....|.
gi 1017579656  126 MAEERILDVLI 136
Cdd:smart00382  73 LARKLKPDVLI 83
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 52-88 5.99e-05

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: 42.66  E-value: 5.99e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1017579656  52 NILMIGPTGVGKTEIARRLAK-LANAPFIKVEATKFTE 88
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 3-70 8.53e-05

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: 44.65  E-value: 8.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017579656   3 EMTPREIVSELD-KHIIGQDNAKRSVAIAlrnrwrrmqleeelRHevtpkNILMIGPTGVGKTEIARRL 70
Cdd:COG0606   179 DAPPAEPPYEPDlADVKGQEQAKRALEIAaa-----------gGH-----NLLMIGPPGSGKTMLARRL 231
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 17-131 1.13e-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: 42.53  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  17 IIGQDNAKRSVAIALRNRWRRMQLEEELRheVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG--- 93
Cdd:cd19524     2 IAGQDLAKQALQEMVILPSLRPELFTGLR--APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVGege 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1017579656  94 ---KEVDSIIRDLTDSAIKMVRVQAIEKNRYRAEEMAEERI 131
Cdd:cd19524    79 klvRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRL 119
ftsH CHL00176
cell division protein; Validated
 50-103 1.62e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 43.89  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGyVGKevdSIIRDL 103
Cdd:CHL00176  216 PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG-VGA---ARVRDL 267
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 50-103 1.75e-04

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: 41.94  E-value: 1.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDL 103
Cdd:cd19502    37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVREL 88
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 17-70 2.43e-04

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: 42.14  E-value: 2.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1017579656  17 IIGQDNAKRSVAIALRNRwrrmqleeelrHevtpkNILMIGPTGVGKTEIARRL 70
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGG-----------H-----NLLMIGPPGSGKTMLAKRL 42
clpC CHL00095
Clp protease ATP binding subunit
 12-93 2.78e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 43.51  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  12 ELDKHIIGQDNAKRSVAIALRnrwrrmqleeelRHEVTPKNI-------LMIGPTGVGKTEIARRLAKL---ANAPFIKV 81
Cdd:CHL00095  506 TLHKRIIGQDEAVVAVSKAIR------------RARVGLKNPnrpiasfLFSGPTGVGKTELTKALASYffgSEDAMIRL 573

                          90       100
                  ....*....|....*....|...
gi 1017579656  82 EATKFTE-----------VGYVG 93
Cdd:CHL00095  574 DMSEYMEkhtvskligspPGYVG 596
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 49-107 3.16e-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: 41.11  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017579656  49 TPKNILMIGPTGVGKTEIARRLAKLANAPFIkveATKFTEV--GYVGkEVDSIIRDLTDSA 107
Cdd:cd19511    26 PPKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREIFQKA 82
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 50-83 4.08e-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: 40.74  E-value: 4.08e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:cd19503    34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISG 67
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 50-91 6.64e-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: 40.10  E-value: 6.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGY 91
Cdd:cd19520    35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY 76
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 50-110 6.84e-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: 40.03  E-value: 6.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTeVGYVGkEVDSIIRDLTDSAIKM 110
Cdd:cd19509    32 PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG-ESEKIVRALFALAREL 90
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 52-79 9.13e-04

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: 39.46  E-value: 9.13e-04
                          10        20
                  ....*....|....*....|....*...
gi 1017579656  52 NILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
Sigma54_activat pfam00158
Sigma-54 interaction domain;
49-81 1.14e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.69  E-value: 1.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1017579656  49 TPKNILMIGPTGVGKTEIAR---RLAKLANAPFIKV 81
Cdd:pfam00158  21 TDAPVLITGESGTGKELFARaihQLSPRADGPFVAV 56
aroK PRK00131
shikimate kinase; Reviewed
 50-79 1.66e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.40  E-value: 1.66e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:PRK00131    4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 50-81 1.84e-03

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: 39.02  E-value: 1.84e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:cd19529    27 PKGILLYGPPGTGKTLLAKAVATESNANFISV 58
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 11-71 1.88e-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: 1.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017579656  11 SELDKHIIGQDNAKRSVAIALR---------NRwrrmqleeelrhevtPknI---LMIGPTGVGKTEIARRLA 71
Cdd:COG0542   545 EELHERVIGQDEAVEAVADAIRrsraglkdpNR---------------P--IgsfLFLGPTGVGKTELAKALA 600
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 50-103 2.38e-03

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: 38.82  E-value: 2.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDL 103
Cdd:cd19525    55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVG-EGEKMVRAL 106
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 41-107 2.39e-03

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: 38.65  E-value: 2.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017579656  41 EEELRHEVTP-KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYvgKEVDSIIRDLTDSA 107
Cdd:cd19528    17 DKFLKFGMTPsKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWF--GESEANVRDIFDKA 82
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 50-81 2.98e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.82  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:PRK03992  165 PKGVLLYGPPGTGKTLLAKAVAHETNATFIRV 196
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 50-136 3.01e-03

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 39.75  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG------KEVDSIIRDLTDSAIKMVRVQAIEKNRYRA 123
Cdd:PTZ00454  179 PRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ-KYLGegprmvRDVFRLARENAPSIIFIDEVDSIATKRFDA 257

                          90
                  ....*....|...
gi 1017579656 124 EEMAEERILDVLI 136
Cdd:PTZ00454  258 QTGADREVQRILL 270
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
12-95 4.36e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 39.44  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  12 ELDKHIIGQDNAKRSVAIALRNRwrRMQLEEELRhevTPKNILMIGPTGVGKTEIARRLAKL---ANAPFIKVEATKFTE 88
Cdd:PRK10865  565 ELHHRVIGQNEAVEAVSNAIRRS--RAGLSDPNR---PIGSFLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEFME 639

                          90
                  ....*....|....*...
gi 1017579656  89 V-----------GYVGKE 95
Cdd:PRK10865  640 KhsvsrlvgappGYVGYE 657
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 54-118 4.38e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.43  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017579656  54 LMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE-----------VGYVGKEVDSIirdLTDSAIK----MVRVQAIEK 118
Cdd:PRK11034  492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGL---LTDAVIKhphaVLLLDEIEK 568
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 53-79 5.57e-03

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 37.42  E-value: 5.57e-03
                          10        20
                  ....*....|....*....|....*..
gi 1017579656  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0703     1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 55-84 7.40e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.53  E-value: 7.40e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1017579656  55 MI--GPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:PRK13342   39 MIlwGPPGTGKTTLARIIAGATDAPFEALSAV 70
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
50-103 7.68e-03

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 38.48  E-value: 7.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1017579656  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGyVGKevdSIIRDL 103
Cdd:COG0465   175 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVG-VGA---SRVRDL 226
PRK13946 PRK13946
shikimate kinase; Provisional
 41-79 9.70e-03

shikimate kinase; Provisional


Pssm-ID: 184411 [Multi-domain]  Cd Length: 184  Bit Score: 37.21  E-value: 9.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1017579656  41 EEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:PRK13946    1 EERARAALGKRTVVLVGLMGAGKSTVGRRLATMLGLPFL 39
 
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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