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Conserved domains on  [gi|500108331|ref|WP_011784336|]
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MULTISPECIES: HslU--HslV peptidase ATPase subunit [Marinobacter]

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: 896.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   1 MSAMTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  81 VEATKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFNEDSQRTNADSSTRQLFR 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 161 KKLREGELDDKEIEIDLRSSGAGVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEEAAKLVNEEEIK 240
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 241 QKAIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIP 320
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 321 ELQGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTENIGARRLHTVLE 400
Cdd:PRK05201 321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 500108331 401 RLLESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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: 896.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   1 MSAMTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  81 VEATKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFNEDSQRTNADSSTRQLFR 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 161 KKLREGELDDKEIEIDLRSSGAGVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEEAAKLVNEEEIK 240
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 241 QKAIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIP 320
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 321 ELQGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTENIGARRLHTVLE 400
Cdd:PRK05201 321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 500108331 401 RLLESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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: 888.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   1 MSAMTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  81 VEATKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFN----------EDSQRTN 150
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAgsnnpfeeeeEEEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 151 ADSSTRQLFRKKLREGELDDKEIEIDLR-SSGAGVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEE 229
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEeSSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 230 AAKLVNEEEIKQKAIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGA 309
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 310 FHLSKPSDLIPELQGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTEN 389
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500108331 390 IGARRLHTVLERLLESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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: 666.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331    4 MTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   84 TKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFNEDSQRTNADSSTRQLFRKKL 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEPESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  164 REGELDDKEIEIDLRSSGA-GVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEEAAKLVNEEEIKQK 242
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKMPsGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  243 AIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIPEL 322
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  323 QGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTENIGARRLHTVLERL 402
Cdd:TIGR00390 321 QGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERL 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 500108331  403 LESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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 7.88e-106

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: 311.24  E-value: 7.88e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   5 TPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  85 KFTEVGYVGRDVESIIRDLADmavkmlreqemkrhehraldaaedrildallppprdfnedsqrtnadsstrqlfrkklr 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 165 egelddkeieidlrssgagveimappgmeemtsqlqsmfsnlssdkrktrkmkvadamkrvkdeeaaklvneeeikqkai 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 245 qaveqnGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIPELQG 324
Cdd:cd19498  102 ------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQG 175


                 ....*...
gi 500108331 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 ...
 184-329 1.51e-26

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: 104.97  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  184 VEIMAPPG-----MEEMTSQLQSMFsnlssdkrkTRKMKVADaMKRVKDEeaaKLVNEEEIKQKAIQAVEQNG------- 251
Cdd:pfam07724   6 FLFLGPTGvgkteLAKALAELLFGD---------ERALIRID-MSEYMEE---HSVSRLIGAPPGYVGYEEGGqlteavr 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  252 -----IVFIDEIDKVAKrsentssdvsreGVQRDLLPLIEGSTVSTKYGS-IRTDHILFIASGAFHLSKPSD-------- 317
Cdd:pfam07724  73 rkpysIVLIDEIEKAHP------------GVQNDLLQILEGGTLTDKQGRtVDFKNTLFIMTGNFGSEKISDasrlgdsp 140

                         170       180
                  ....*....|....*....|....*...
gi 500108331  318 ----------------LIPELQGRLPIR 329
Cdd:pfam07724 141 dyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 335-429 6.42e-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: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   335 LTPDDFKRILTEPDASLVQQYEalmgTEGVKLTFADDAIARIAEVAYKvnettENIGARRLHTVLERLLESLSYDA--GD 412
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilSG 71

                           90
                   ....*....|....*..
gi 500108331   413 QVTDTFEVTADYVDEKL 429
Cdd:smart01086  72 ELKDGDTVVVDVDDGEL 88
 
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: 896.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   1 MSAMTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  81 VEATKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFNEDSQRTNADSSTRQLFR 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 161 KKLREGELDDKEIEIDLRSSGAGVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEEAAKLVNEEEIK 240
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 241 QKAIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIP 320
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 321 ELQGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTENIGARRLHTVLE 400
Cdd:PRK05201 321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 500108331 401 RLLESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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: 888.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   1 MSAMTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  81 VEATKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFN----------EDSQRTN 150
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAgsnnpfeeeeEEEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 151 ADSSTRQLFRKKLREGELDDKEIEIDLR-SSGAGVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEE 229
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEeSSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 230 AAKLVNEEEIKQKAIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGA 309
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 310 FHLSKPSDLIPELQGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTEN 389
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500108331 390 IGARRLHTVLERLLESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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: 666.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331    4 MTPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   84 TKFTEVGYVGRDVESIIRDLADMAVKMLREQEMKRHEHRALDAAEDRILDALLPPPRDFNEDSQRTNADSSTRQLFRKKL 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEPESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  164 REGELDDKEIEIDLRSSGA-GVEIMAPPGMEEMTSQLQSMFSNLSSDKRKTRKMKVADAMKRVKDEEAAKLVNEEEIKQK 242
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKMPsGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  243 AIQAVEQNGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIPEL 322
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  323 QGRLPIRVELQALTPDDFKRILTEPDASLVQQYEALMGTEGVKLTFADDAIARIAEVAYKVNETTENIGARRLHTVLERL 402
Cdd:TIGR00390 321 QGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERL 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 500108331  403 LESLSYDAGDQVTDTFEVTADYVDEKLGELSEDEDLSRYIL 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 7.88e-106

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: 311.24  E-value: 7.88e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   5 TPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  85 KFTEVGYVGRDVESIIRDLADmavkmlreqemkrhehraldaaedrildallppprdfnedsqrtnadsstrqlfrkklr 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 165 egelddkeieidlrssgagveimappgmeemtsqlqsmfsnlssdkrktrkmkvadamkrvkdeeaaklvneeeikqkai 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 245 qaveqnGIVFIDEIDKVAKRSENTSSDVSREGVQRDLLPLIEGSTVSTKYGSIRTDHILFIASGAFHLSKPSDLIPELQG 324
Cdd:cd19498  102 ------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQG 175


                 ....*...
gi 500108331 325 RLPIRVEL 332
Cdd:cd19498  176 RFPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
5-432 1.95e-67

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 220.80  E-value: 1.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   5 TPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRD--EITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVE 82
Cdd:PRK05342  61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDdvELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  83 ATKFTEVGYVGRDVESIIRDLadmavkmlreqemkrhehraLDAAedrildallppprDFNedsqrtnadsstrqlfrkk 162
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILLKL--------------------LQAA-------------DYD------------------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 163 lregelddkeieidlrssgagveimappgmeemtsqlqsmfsnlssdkrktrkmkVADAmkrvkdeeaaklvneeeikqk 242
Cdd:PRK05342 169 -------------------------------------------------------VEKA--------------------- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 243 aiqaveQNGIVFIDEIDKVAKRSENTSS--DVSREGVQRDLLPLIEGSTVS-----------TKYGSIRTDHILFIASGA 309
Cdd:PRK05342 173 ------QRGIVYIDEIDKIARKSENPSItrDVSGEGVQQALLKILEGTVASvppqggrkhpqQEFIQVDTTNILFICGGA 246

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 310 F-----------------------------------HLSKPSDL-----IPELQGRLPIRVELQALTPDDFKRILTEPDA 349
Cdd:PRK05342 247 FdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLPVVATLEELDEEALVRILTEPKN 326

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 350 SLVQQYEALMGTEGVKLTFADDAIARIAEVAYKvnettENIGARRLHTVLERLLESLSYDAGDQVTDT-FEVTADYVDEK 428
Cdd:PRK05342 327 ALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMFELPSREDVEkVVITKEVVEGK 401


                 ....
gi 500108331 429 LGEL 432
Cdd:PRK05342 402 AKPL 405
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-428 6.47e-67

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 219.15  E-value: 6.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   5 TPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRD--EITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVE 82
Cdd:COG1219   62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDdvELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  83 ATKFTEVGYVGRDVESIIRDLadmavkmlreqemkrhehraLDAAedrildallppprDFNedsqrtnadsstrqlfrkk 162
Cdd:COG1219  142 ATTLTEAGYVGEDVENILLKL--------------------LQAA-------------DYD------------------- 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 163 lregelddkeieidlrssgagVEimappgmeemtsqlqsmfsnlssdkrktrkmkvadamkrvkdeeaaklvneeeikqK 242
Cdd:COG1219  170 ---------------------VE--------------------------------------------------------K 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 243 AiqaveQNGIVFIDEIDKVAKRSENTSS--DVSREGVQRDLLPLIEGSTVS-----------TKYGSIRTDHILFIASGA 309
Cdd:COG1219  173 A-----ERGIIYIDEIDKIARKSENPSItrDVSGEGVQQALLKILEGTVANvppqggrkhpqQEFIQIDTTNILFICGGA 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 310 F-HLSK---------------------------------PSDL-----IPELQGRLPIRVELQALTPDDFKRILTEPDAS 350
Cdd:COG1219  248 FdGLEKiierrlgkksigfgaevkskkekdegellkqvePEDLikfglIPEFIGRLPVIATLEELDEEALVRILTEPKNA 327

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500108331 351 LVQQYEALMGTEGVKLTFADDAIARIAEVAYKvnettENIGARRLHTVLERLLESLSYDA-GDQVTDTFEVTADYVDEK 428
Cdd:COG1219  328 LVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMYELpSRKDVKKVVITKEVVEGK 401
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 5-409 1.06e-41

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: 152.61  E-value: 1.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331    5 TPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRD----EITPKNILMIGPTGVGKTEIARRLAKLADAPFLK 80
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   81 VEATKFTEVGYVGRDVESIIRDLadmavkmlreqemkrhehraLDAAEDRIldallppprdfnedsqrtnadsstrqlfr 160
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENILLKL--------------------LQAADYDV----------------------------- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  161 kklregelddkeieidlrssgagveimappgmeemtsqlqsmfsnlssdkrktrkmkvadamkrvkdeeaaklvneeeik 240
Cdd:TIGR00382     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  241 QKAiqaveQNGIVFIDEIDKVAKRSENTS--SDVSREGVQRDLLPLIEGSTVST-----------KYGSIRTDHILFIAS 307
Cdd:TIGR00382 178 EKA-----QKGIIYIDEIDKISRKSENPSitRDVSGEGVQQALLKIIEGTVANVppqggrkhpyqEFIQIDTSNILFICG 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  308 GAF---------------------------------HLSKPSD-----LIPELQGRLPIRVELQALTPDDFKRILTEPDA 349
Cdd:TIGR00382 253 GAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLIPEFIGRLPVIATLEKLDEEALIAILTKPKN 332

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  350 SLVQQYEALMGTEGVKLTFADDAIARIAEVAYKvnettENIGARRLHTVLERLLESLSYD 409
Cdd:TIGR00382 333 ALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFD 387
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 5-332 1.32e-39

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: 142.74  E-value: 1.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   5 TPREIVHELNKHIVGQEEAKRAVAIALRNRWRRMQLDSSLRD---EITPKNILMIGPTGVGKTEIARRLAKLADAPFLKV 81
Cdd:cd19497    2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  82 EATKFTEVGYVGRDVESIIRDLadmavkmlreqemkrhehraLDAAedrildallppprDFNedsqrtnadsstrqlfrk 161
Cdd:cd19497   82 DATTLTEAGYVGEDVENILLKL--------------------LQAA-------------DYD------------------ 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 162 klregelddkeieidlrssgagveimappgmeemtsqlqsmfsnlssdkrktrkmkVADAmkrvkdeeaaklvneeeikq 241
Cdd:cd19497  111 --------------------------------------------------------VERA-------------------- 114

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 242 kaiqaveQNGIVFIDEIDKVAKRSENTS--SDVSREGVQRDLLPLIEGSTVST-----------KYGSIRTDHILFIASG 308
Cdd:cd19497  115 -------QRGIVYIDEIDKIARKSENPSitRDVSGEGVQQALLKILEGTVANVppqggrkhpqqEFIQVDTTNILFICGG 187

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500108331 309 AF---------------------------------HLSK--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 ...
 184-329 1.51e-26

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: 104.97  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  184 VEIMAPPG-----MEEMTSQLQSMFsnlssdkrkTRKMKVADaMKRVKDEeaaKLVNEEEIKQKAIQAVEQNG------- 251
Cdd:pfam07724   6 FLFLGPTGvgkteLAKALAELLFGD---------ERALIRID-MSEYMEE---HSVSRLIGAPPGYVGYEEGGqlteavr 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  252 -----IVFIDEIDKVAKrsentssdvsreGVQRDLLPLIEGSTVSTKYGS-IRTDHILFIASGAFHLSKPSD-------- 317
Cdd:pfam07724  73 rkpysIVLIDEIEKAHP------------GVQNDLLQILEGGTLTDKQGRtVDFKNTLFIMTGNFGSEKISDasrlgdsp 140

                         170       180
                  ....*....|....*....|....*...
gi 500108331  318 ----------------LIPELQGRLPIR 329
Cdd:pfam07724 141 dyellkeevmdllkkgFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 23-136 4.53e-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: 69.62  E-value: 4.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  23 AKRAVAIALRNRWRRMQLdsSLRDEITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTE--VGYVGRDVESII 100
Cdd:cd19481    1 LKASLREAVEAPRRGSRL--RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 500108331 101 RDLADMAVKMLREQEM----KRHEHRALDAAEDRILDALL 136
Cdd:cd19481   79 ERARRLAPCILFIDEIdaigRKRDSSGESGELRRVLNQLL 118
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 335-429 6.42e-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: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   335 LTPDDFKRILTEPDASLVQQYEalmgTEGVKLTFADDAIARIAEVAYKvnettENIGARRLHTVLERLLESLSYDA--GD 412
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilSG 71

                           90
                   ....*....|....*..
gi 500108331   413 QVTDTFEVTADYVDEKL 429
Cdd:smart01086  72 ELKDGDTVVVDVDDGEL 88
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 12-73 1.32e-09

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: 57.19  E-value: 1.32e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500108331  12 ELNKHIVGQEEAKRAVAIALRnRWRrmqldSSLRDEITPK-NILMIGPTGVGKTEIARRLAKL 73
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIR-RAR-----AGLSDPNRPIgSFLFLGPTGVGKTELAKALAEL 64
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 18-110 2.06e-09

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: 56.00  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  18 VGQEEAKRAVAIALRNRwrrmqldsslrdeiTPKNILMIGPTGVGKTEIARRLAKLA---DAPFLKVEATKFTEVGYVGR 94
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                         90
                 ....*....|....*.
gi 500108331  95 DVESIIRDLADMAVKM 110
Cdd:cd00009   67 LFGHFLVRLLFELAEK 82
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 4-84 5.43e-09

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: 57.10  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   4 MTPREIVHELNKHIVGQEEAKRAVAIALRNRwrrmqldsslrdeitpKNILMIGPTGVGKTEIARRLAKLADAPFLKVEA 83
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAG----------------GHLLLEGVPGVGKTTLAKALARALGLPFIRIQF 64


                 .
gi 500108331  84 T 84
Cdd:COG0714   65 T 65
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 15-109 3.25e-08

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: 53.01  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  15 KHIVGQEEAKRAVAIA---LRNRWRRMQLDSSLrdeitPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEVgY 91
Cdd:cd19501    4 KDVAGCEEAKEELKEVvefLKNPEKFTKLGAKI-----PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-F 77

                         90
                 ....*....|....*...
gi 500108331  92 VGRDVeSIIRDLADMAVK 109
Cdd:cd19501   78 VGVGA-SRVRDLFEQAKK 94
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 229-332 7.08e-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: 47.97  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  229 EAAKLVNE--EEIKQKAIqaveqnGIVFIDEIDKVAKRSENTSSDVSREgVQRDLLPLIEGSTvstkygsIRTDHILFIA 306
Cdd:pfam00004  41 ESEKRLRElfEAAKKLAP------CVIFIDEIDALAGSRGSGGDSESRR-VVNQLLTELDGFT-------SSNSKVIVIA 106

                          90       100
                  ....*....|....*....|....*.
gi 500108331  307 SGafhlSKPSDLIPELQGRLPIRVEL 332
Cdd:pfam00004 107 AT----NRPDKLDPALLGRFDRIIEF 128
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 12-71 1.73e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 50.47  E-value: 1.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500108331  12 ELNKHIVGQEEAKRAVAIA-LRNRwrrmqldSSLRDEITPknI---LMIGPTGVGKTEIARRLA 71
Cdd:COG0542  546 ELHERVIGQDEAVEAVADAiRRSR-------AGLKDPNRP--IgsfLFLGPTGVGKTELAKALA 600
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 53-110 3.41e-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: 46.05  E-value: 3.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 500108331   53 ILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEvGYVGrDVESIIRDLADMAVKM 110
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFEAAKKL 56
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 15-107 4.48e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 48.46  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  15 KHIVGQEEAKR----AVAIALRN--RWRRMQLDsslrdeiTPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTE 88
Cdd:COG1222   78 DDIGGLDEQIEeireAVELPLKNpeLFRKYGIE-------PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150

                         90
                 ....*....|....*....
gi 500108331  89 vGYVGrDVESIIRDLADMA 107
Cdd:COG1222  151 -KYIG-EGARNVREVFELA 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 17-132 4.97e-06

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: 46.58  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  17 IVGQEEAKRAVAIALRNRWRRMQLDSSLRDeiTPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTeVGYVGrDV 96
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRG--PPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG-ES 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500108331  97 ESIIRDLADMAVKM-------------LREQEMKRHEHRA-------------LDAAEDRIL 132
Cdd:cd19509   77 EKIVRALFALARELqpsiifideidslLSERGSGEHEASRrvkteflvqmdgvLNKPEDRVL 138
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
17-109 7.41e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 48.49  E-value: 7.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  17 IVGQEEAKRAVAIA---LRNRWRRMQLDSSLrdeitPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEVgYVG 93
Cdd:PRK10733 154 VAGCDEAKEEVAELveyLREPSRFQKLGGKI-----PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVG 227

                         90
                 ....*....|....*.
gi 500108331  94 RDVeSIIRDLADMAVK 109
Cdd:PRK10733 228 VGA-SRVRDMFEQAKK 242
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 17-70 7.97e-06

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: 46.37  E-value: 7.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 500108331   17 IVGQEEAKRAVAIALRNRwrrmqldsslrdeitpKNILMIGPTGVGKTEIARRL 70
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGG----------------HNLLMIGPPGSGKTMLAKRL 42
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 17-70 1.04e-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: 47.73  E-value: 1.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500108331  17 IVGQEEAKRAVAIAlrnrwrrmqldsslrdeitpkNILMIGPTGVGKTEIARRL 70
Cdd:COG0606  194 VKGQEQAKRALEIAaag----------------ghNLLMIGPPGSGKTMLARRL 231
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 17-93 3.05e-05

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: 46.06  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  17 IVGQEEAKRAvaiaLRNRWRRMQLDSSLRDEI---TPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEvGYVG 93
Cdd:COG0464  159 LGGLEEVKEE----LRELVALPLKRPELREEYglpPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 50-108 3.66e-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: 43.93  E-value: 3.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500108331  50 PKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFteVGYVGRDVESIIRDLADMAV 108
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAI 90
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
11-96 5.82e-05

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 45.61  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  11 HELNKHIVGQEEAKRAVAIALRnRWRrmqldSSLRDEITP-KNILMIGPTGVGKTEIARRLAKL---ADAPFLKVEATKF 86
Cdd:PRK10865 564 QELHHRVIGQNEAVEAVSNAIR-RSR-----AGLSDPNRPiGSFLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEF 637

                         90
                 ....*....|
gi 500108331  87 TEVGYVGRDV 96
Cdd:PRK10865 638 MEKHSVSRLV 647
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 50-107 9.64e-05

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: 42.71  E-value: 9.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500108331  50 PKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEvGYVGrDVESIIRDLADMA 107
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVRELFEMA 92
clpC CHL00095
Clp protease ATP binding subunit
 12-73 1.17e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 44.66  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500108331  12 ELNKHIVGQEEAKRAVAIALRnRWRrmqldSSLRDEITP-KNILMIGPTGVGKTEIARRLAKL 73
Cdd:CHL00095 506 TLHKRIIGQDEAVVAVSKAIR-RAR-----VGLKNPNRPiASFLFSGPTGVGKTELTKALASY 562
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 52-88 1.30e-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: 41.89  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 500108331   52 NILMIGPTGVGKTEIARRLAK-LADAPFLKVEATKFTE 88
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
ftsH CHL00176
cell division protein; Validated
 17-103 1.63e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 43.89  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  17 IVGQEEAKR---AVAIALRNRWRRMQLDSSLrdeitPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTE--VGy 91
Cdd:CHL00176 185 IAGIEEAKEefeEVVSFLKKPERFTAVGAKI-----PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG- 258

                         90
                 ....*....|..
gi 500108331  92 VGrdvESIIRDL 103
Cdd:CHL00176 259 VG---AARVRDL 267
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 17-110 1.65e-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: 42.14  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  17 IVGQEEAKRAVAIALRNRWRRMQLDSSLRdeITPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEvGYVGrDV 96
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLR--APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77

                         90
                 ....*....|....
gi 500108331  97 ESIIRDLADMAVKM 110
Cdd:cd19524   78 EKLVRALFAVAREL 91
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 224-333 2.02e-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: 41.36  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331 224 RVKDEEAAKLVNEEEIKQKAIQAVEQNGIVFIDEIDKVakrsentssdvsREGVQRDLLPLIEGSTVSTkygsIRTDHIL 303
Cdd:cd00009   59 LEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLETLNDLR----IDRENVR 122

                         90       100       110
                 ....*....|....*....|....*....|
gi 500108331 304 FIASGAFHLskPSDLIPELQGRLPIRVELQ 333
Cdd:cd00009  123 VIGATNRPL--LGDLDRALYDRLDIRIVIP 150
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 17-107 3.99e-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: 41.13  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  17 IVGQEEAKRAVAIALRNRWRRMQLDSSLRDeiTPKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEvGYVGRDv 96
Cdd:cd19525   24 IAGLEFAKKTIKEIVVWPMLRPDIFTGLRG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVGEG- 99

                         90
                 ....*....|.
gi 500108331  97 ESIIRDLADMA 107
Cdd:cd19525  100 EKMVRALFSVA 110
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 4.12e-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: 40.73  E-value: 4.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500108331  49 TPKNILMIGPTGVGKTEIARRLAKLADAPFLkveATKFTEV--GYVGrDVESIIRDLADMA 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 5.07e-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: 5.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 500108331  50 PKNILMIGPTGVGKTEIARRLAKLADAPFLKVEA 83
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISG 67
AAA_22 pfam13401
AAA domain;
49-127 1.34e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331   49 TPKNILMIGPTGVGKTEIARRLAKL---ADAPFLKVEATKFTEVGYVgrdVESIIRDLADMAVKMLREQEMKRHEHRALD 125
Cdd:pfam13401   4 GAGILVLTGESGTGKTTLLRRLLEQlpeVRDSVVFVDLPSGTSPKDL---LRALLRALGLPLSGRLSKEELLAALQQLLL 80


                  ..
gi 500108331  126 AA 127
Cdd:pfam13401  81 AL 82
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
7-74 1.36e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 40.62  E-value: 1.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500108331   7 REIVHELNKHIvGQEEAKRAVAIALRNRWRRMQLDSSLRdeitPKNILMIGPTGVGKTEIarrLAKLA 74
Cdd:COG1419  126 RELLEKLPEDL-SAEEAWRALLEALARRLPVAEDPLLDE----GGVIALVGPTGVGKTTT---IAKLA 185
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 50-128 1.41e-03

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: 39.33  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  50 PKNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEVGYvgRDVESIIRDLADMAVK-------------MLREQEM 116
Cdd:cd19520   35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY--GESQKLVAAVFSLASKlqpsiifideidsFLRQRSS 112

                         90
                 ....*....|..
gi 500108331 117 KRHEHRALDAAE 128
Cdd:cd19520  113 TDHEATAMMKAE 124
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 49-81 1.73e-03

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: 38.89  E-value: 1.73e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 500108331    49 TPKNILMIGPTGVGKTEIARRLAKLADAPFLKV 81
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
flhF PRK05703
flagellar biosynthesis protein FlhF;
1-74 3.20e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 39.49  E-value: 3.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500108331   1 MSAMTPREIVHELNKHI-VGQEEAKRAVAIALRNrwrrmQLDSSLRDEITPKNILM-IGPTGVGKTEIarrLAKLA 74
Cdd:PRK05703 175 LSPEIAEKLLKLLLEHMpPRERTAWRYLLELLAN-----MIPVRVEDILKQGGVVAlVGPTGVGKTTT---LAKLA 242
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 51-107 4.52e-03

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: 38.04  E-value: 4.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500108331  51 KNILMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTEvGYVGrDVESIIRDLADMA 107
Cdd:cd19522   34 KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTS-KYRG-ESEKLVRLLFEMA 88
aroK PRK00131
shikimate kinase; Reviewed
 48-79 5.63e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.48  E-value: 5.63e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 500108331  48 ITPKNILMIGPTGVGKTEIARRLAKLADAPFL 79
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
Sigma54_activat pfam00158
Sigma-54 interaction domain;
49-81 6.01e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.38  E-value: 6.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 500108331   49 TPKNILMIGPTGVGKTEIAR---RLAKLADAPFLKV 81
Cdd:pfam00158  21 TDAPVLITGESGTGKELFARaihQLSPRADGPFVAV 56
PRK13947 PRK13947
shikimate kinase; Provisional
 51-115 6.73e-03

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 37.38  E-value: 6.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  51 KNILMIGPTGVGKTEIARRLAKLADAPFLKVEA-----TKFTEVGYVGRDVESIIRDLADMAVKMLREQE 115
Cdd:PRK13947   2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKeiekmTGMTVAEIFEKDGEVRFRSEEKLLVKKLARLK 71
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 52-79 7.46e-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: 37.15  E-value: 7.46e-03
                         10        20
                 ....*....|....*....|....*...
gi 500108331  52 NILMIGPTGVGKTEIARRLAKLADAPFL 79
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 54-102 9.13e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 38.66  E-value: 9.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500108331  54 LMIGPTGVGKTEIARRLAKLADAPFLKVEATKFTE-----------VGYVGRDVESIIRD 102
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGLLTD 551
 
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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