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Conserved domains on  [gi|498361875|ref|WP_010676031|]
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MULTISPECIES: HslU--HslV peptidase ATPase subunit [Aeromonas]

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;
1-442 0e+00

ATP-dependent protease ATPase subunit HslU;


:

Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 903.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   1 MSEMTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  81 VEATKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWG-EEEKADNSNTRQIFR 159
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGeEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 160 KKLREGQLDDKEIELDLAASPMGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEEAARLVNPEELK 239
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 240 QKAIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIP 319
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 320 ELQGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTENIGARRLHTVME 399
Cdd:PRK05201 321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 498361875 400 RLMEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:PRK05201 401 KLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-442 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 903.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   1 MSEMTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  81 VEATKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWG-EEEKADNSNTRQIFR 159
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGeEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 160 KKLREGQLDDKEIELDLAASPMGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEEAARLVNPEELK 239
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 240 QKAIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIP 319
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 320 ELQGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTENIGARRLHTVME 399
Cdd:PRK05201 321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 498361875 400 RLMEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:PRK05201 401 KLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-442 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: 880.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   1 MSEMTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  81 VEATKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWG-----------EEEKA 149
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGsnnpfeeeeeeEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 150 DNSNTRQIFRKKLREGQLDDKEIELDLAASP-MGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEE 228
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEESSsPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 229 AARLVNPEELKQKAIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGA 308
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 309 FQIAKPSDLIPELQGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTEN 388
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498361875 389 IGARRLHTVMERLMEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:COG1220  401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-442 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: 703.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875    4 MTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   84 TKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWGEEEKADN-SNTRQIFRKKL 162
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEpESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  163 REGQLDDKEIELDLAAS-PMGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEEAARLVNPEELKQK 241
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKmPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  242 AIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIPEL 321
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  322 QGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTENIGARRLHTVMERL 401
Cdd:TIGR00390 321 QGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERL 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 498361875  402 MEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:TIGR00390 401 LEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-331 2.76e-109

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: 320.10  E-value: 2.76e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   5 TPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  85 KFTEVGYVGKEVDSIIRDLTDvaiklvretemekmkyraeeaaeerildallpnprnswgeeekadnsntrqifrkklre 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 165 gqlddkeieldlaaspmgveimtppgmeemanqlqglfqnlgqnqkkkrkikvkeamkalieeeaarlvnpeelkqkaia 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 245 svennGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIPELQGR 324
Cdd:cd19498  102 -----GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQGR 176


                 ....*..
gi 498361875 325 LPIRVEL 331
Cdd:cd19498  177 FPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 221-328 4.98e-23

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: 94.95  E-value: 4.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  221 MKALIEEeaaRLVNPEELKQKAIASVENNG------------IVFLDEIDKICKrgessgpdvsreGVQRDLLPLVEGCT 288
Cdd:pfam07724  39 MSEYMEE---HSVSRLIGAPPGYVGYEEGGqlteavrrkpysIVLIDEIEKAHP------------GVQNDLLQILEGGT 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498361875  289 VNTKHG-MVKTDHILFVASGAFQIAKPSD------------------------LIPELQGRLPIR 328
Cdd:pfam07724 104 LTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 334-422 1.47e-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: 63.23  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   334 LTTEDFERILTEPNASLTDQYkalmATEGVNIEFTQDGIRRLAEAAWQvnertENIGARRLHTVMERLMEDISYDA---- 409
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|...
gi 498361875   410 SEKSGETFVINTD 422
Cdd:smart01086  72 ELKDGDTVVVDVD 84
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-442 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 903.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   1 MSEMTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  81 VEATKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWG-EEEKADNSNTRQIFR 159
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGeEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 160 KKLREGQLDDKEIELDLAASPMGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEEAARLVNPEELK 239
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 240 QKAIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIP 319
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLIP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 320 ELQGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTENIGARRLHTVME 399
Cdd:PRK05201 321 ELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVME 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 498361875 400 RLMEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:PRK05201 401 KLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-442 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: 880.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   1 MSEMTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  81 VEATKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWG-----------EEEKA 149
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGsnnpfeeeeeeEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 150 DNSNTRQIFRKKLREGQLDDKEIELDLAASP-MGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEE 228
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEESSsPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 229 AARLVNPEELKQKAIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGA 308
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 309 FQIAKPSDLIPELQGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTEN 388
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498361875 389 IGARRLHTVMERLMEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:COG1220  401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-442 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: 703.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875    4 MTPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   84 TKFTEVGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYRAEEAAEERILDALLPNPRNSWGEEEKADN-SNTRQIFRKKL 162
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEpESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  163 REGQLDDKEIELDLAAS-PMGVEIMTPPGMEEMANQLQGLFQNLGQNQKKKRKIKVKEAMKALIEEEAARLVNPEELKQK 241
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKmPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  242 AIASVENNGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIPEL 321
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPEL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  322 QGRLPIRVELTALTTEDFERILTEPNASLTDQYKALMATEGVNIEFTQDGIRRLAEAAWQVNERTENIGARRLHTVMERL 401
Cdd:TIGR00390 321 QGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLERL 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 498361875  402 MEDISYDASEKSGETFVINTDYVNAHLGKLIEDEDLSRFIL 442
Cdd:TIGR00390 401 LEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-331 2.76e-109

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: 320.10  E-value: 2.76e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   5 TPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  85 KFTEVGYVGKEVDSIIRDLTDvaiklvretemekmkyraeeaaeerildallpnprnswgeeekadnsntrqifrkklre 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 165 gqlddkeieldlaaspmgveimtppgmeemanqlqglfqnlgqnqkkkrkikvkeamkalieeeaarlvnpeelkqkaia 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 245 svennGIVFLDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVNTKHGMVKTDHILFVASGAFQIAKPSDLIPELQGR 324
Cdd:cd19498  102 -----GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQGR 176


                 ....*..
gi 498361875 325 LPIRVEL 331
Cdd:cd19498  177 FPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
5-436 6.73e-63

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 208.86  E-value: 6.73e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   5 TPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEV--TPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:PRK05342  61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVelQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  83 ATKFTEVGYVGKEVDSIIRdltdvaiklvretemekmkyraeeaaeeRILDAllpnprnswgeeekADNsntrqifrkkl 162
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILL----------------------------KLLQA--------------ADY----------- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 163 regqlddkeielDLaaspmgveimtppgmeemanqlqglfqnlgqnqkkkrkikvkeamkalieEEAARlvnpeelkqka 242
Cdd:PRK05342 168 ------------DV--------------------------------------------------EKAQR----------- 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 243 iasvennGIVFLDEIDKICKRGE--SSGPDVSREGVQRDLLPLVEGCTVNT------KHGM-----VKTDHILFVASGAF 309
Cdd:PRK05342 175 -------GIVYIDEIDKIARKSEnpSITRDVSGEGVQQALLKILEGTVASVppqggrKHPQqefiqVDTTNILFICGGAF 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 310 Q-----IAK------------------------------PSDL-----IPELQGRLPIRVELTALTTEDFERILTEPNAS 349
Cdd:PRK05342 248 DglekiIKQrlgkkgigfgaevkskkekrtegellkqvePEDLikfglIPEFIGRLPVVATLEELDEEALVRILTEPKNA 327

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 350 LTDQYKALMATEGVNIEFTQDGIRRLAEAAWqvnERteNIGARRLHTVMERLMEDISYDA-SEKSGETFVINTDYVNAHL 428
Cdd:PRK05342 328 LVKQYQKLFEMDGVELEFTDEALEAIAKKAI---ER--KTGARGLRSILEEILLDVMFELpSREDVEKVVITKEVVEGKA 402


                 ....*...
gi 498361875 429 GKLIEDED 436
Cdd:PRK05342 403 KPLLIYRE 410
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-432 1.67e-59

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 199.89  E-value: 1.67e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   5 TPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRHEVT-PK-NILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:COG1219   62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVElEKsNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  83 ATKFTEVGYVGKEVDSIIRdltdvaiklvretemekmkyraeeaaeeRILDAllpnprnswgeeekADNsntrqifrkkl 162
Cdd:COG1219  142 ATTLTEAGYVGEDVENILL----------------------------KLLQA--------------ADY----------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 163 regqlddkeielDLaaspmgveimtppgmeemanqlqglfqnlgqnqkkkrkikvkeamkalieEEAARlvnpeelkqka 242
Cdd:COG1219  169 ------------DV--------------------------------------------------EKAER----------- 175

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 243 iasvennGIVFLDEIDKICKRGE--SSGPDVSREGVQRDLLPLVEGCTVNT------KHGM-----VKTDHILFVASGAF 309
Cdd:COG1219  176 -------GIIYIDEIDKIARKSEnpSITRDVSGEGVQQALLKILEGTVANVppqggrKHPQqefiqIDTTNILFICGGAF 248

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 310 Q-----IAK-----------------------------PSDL-----IPELQGRLPIRVELTALTTEDFERILTEPNASL 350
Cdd:COG1219  249 DglekiIERrlgkksigfgaevkskkekdegellkqvePEDLikfglIPEFIGRLPVIATLEELDEEALVRILTEPKNAL 328

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 351 TDQYKALMATEGVNIEFTQDGIRRLAEAAwqvNERteNIGARRLHTVMERLMEDISYDA-SEKSGETFVINTDYVNAHLG 429
Cdd:COG1219  329 VKQYQKLFEMDGVELEFTDEALEAIAKKA---IER--KTGARGLRSILEEILLDVMYELpSRKDVKKVVITKEVVEGKAK 403


                 ...
gi 498361875 430 KLI 432
Cdd:COG1219  404 PIL 406
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 5-424 7.21e-37

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: 139.52  E-value: 7.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875    5 TPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRH----EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   81 VEATKFTEVGYVGKEVDSIIRDLTDVAiklvretemekmKYRAEEAaeerildallpnprnswgeeekadnsntrqifrk 160
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENILLKLLQAA------------DYDVEKA---------------------------------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  161 klregqlddkeieldlaaspmgveimtppgmeemanqlqglfqnlgqnqkkkrkikvkeamkalieeeaarlvnpeelkQ 240
Cdd:TIGR00382 181 -------------------------------------------------------------------------------Q 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  241 KaiasvennGIVFLDEIDKICKRGE--SSGPDVSREGVQRDLLPLVEGCTVNT------KHG-----MVKTDHILFVASG 307
Cdd:TIGR00382 182 K--------GIIYIDEIDKISRKSEnpSITRDVSGEGVQQALLKIIEGTVANVppqggrKHPyqefiQIDTSNILFICGG 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  308 AF----QIAK-----------------------------PSD-----LIPELQGRLPIRVELTALTTEDFERILTEPNAS 349
Cdd:TIGR00382 254 AFvgleKIIKkrtgkssigfgaevkkkskekadllrqvePEDlvkfgLIPEFIGRLPVIATLEKLDEEALIAILTKPKNA 333

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498361875  350 LTDQYKALMATEGVNIEFTQDGIRRLAEAAWQvnertENIGARRLHTVMERLMEDISYD-ASEKSGETFVINTDYV 424
Cdd:TIGR00382 334 LVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFDlPSLEDLEKVVITKETV 404
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 5-331 1.47e-31

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: 121.17  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   5 TPREIVHELDRHIIGQADAKRAVAVALRNRWRRMQLSEEMRH---EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:cd19497    2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  82 EATKFTEVGYVGKEVDSIIrdltdvaIKLVretemekmkyraeEAAEerildallpnprnswGEEEKAdnsntrqifrkk 161
Cdd:cd19497   82 DATTLTEAGYVGEDVENIL-------LKLL-------------QAAD---------------YDVERA------------ 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 162 lregqlddkeieldlaaspmgveimtppgmeemanqlqglfqnlgqnqkkkrkikvkeamkalieeeaarlvnpeelkQK 241
Cdd:cd19497  115 ------------------------------------------------------------------------------QR 116

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875 242 aiasvennGIVFLDEIDKICKRGESSG--PDVSREGVQRDLLPLVEGCTVNT------KHG-----MVKTDHILFVASGA 308
Cdd:cd19497  117 --------GIVYIDEIDKIARKSENPSitRDVSGEGVQQALLKILEGTVANVppqggrKHPqqefiQVDTTNILFICGGA 188

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498361875 309 FQ-----IAK------------------------------PSDL-----IPELQGRLPIRVEL 331
Cdd:cd19497  189 FVglekiIARrlgkkslgfgaetssekdekerdellskvePEDLikfglIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 221-328 4.98e-23

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: 94.95  E-value: 4.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  221 MKALIEEeaaRLVNPEELKQKAIASVENNG------------IVFLDEIDKICKrgessgpdvsreGVQRDLLPLVEGCT 288
Cdd:pfam07724  39 MSEYMEE---HSVSRLIGAPPGYVGYEEGGqlteavrrkpysIVLIDEIEKAHP------------GVQNDLLQILEGGT 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498361875  289 VNTKHG-MVKTDHILFVASGAFQIAKPSD------------------------LIPELQGRLPIR 328
Cdd:pfam07724 104 LTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 23-136 1.79e-15

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: 73.47  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  23 AKRAVAVALRNRWRRMQLSEemRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVDSII 100
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRR--YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 498361875 101 RDLTDVAIKLVRETEMEKMKYRAEEAAE----ERILDALL 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, ...
 334-422 1.47e-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: 63.23  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   334 LTTEDFERILTEPNASLTDQYkalmATEGVNIEFTQDGIRRLAEAAWQvnertENIGARRLHTVMERLMEDISYDA---- 409
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|...
gi 498361875   410 SEKSGETFVINTD 422
Cdd:smart01086  72 ELKDGDTVVVDVD 84
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 18-139 1.53e-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: 53.30  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  18 IGQADAKRAVAVALRNRwrrmqlseemrhevTPKNILMIGPTGVGKTEIARRLAKLA---NAPFIKVEATKFTEVGYVGK 94
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 498361875  95 EVDSIIRDLTDVAIKLVRET-----EMEKMkYRAEEAAEERILDALLPNP 139
Cdd:cd00009   67 LFGHFLVRLLFELAEKAKPGvlfidEIDSL-SRGAQNALLRVLETLNDLR 115
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 4-84 7.69e-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: 7.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   4 MTPREIVHELDRHIIGQADAKRAVAVALRNRwrrmqlseemRHevtpknILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAG----------GH------LLLEGVPGVGKTTLAKALARALGLPFIRIQF 64


                 .
gi 498361875  84 T 84
Cdd:COG0714   65 T 65
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 12-73 1.17e-07

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: 51.41  E-value: 1.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498361875  12 ELDRHIIGQADAKRAVAVALRNRwrRMQLSEEMRHevtPKNILMIGPTGVGKTEIARRLAKL 73
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIRRA--RAGLSDPNRP---IGSFLFLGPTGVGKTELAKALAEL 64
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 3-70 9.45e-07

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 50.81  E-value: 9.45e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361875   3 EMTPREIVHELD-RHIIGQADAKRA--VAVAlrnrwrrmqlseeMRHevtpkNILMIGPTGVGKTEIARRL 70
Cdd:COG0606  179 DAPPAEPPYEPDlADVKGQEQAKRAleIAAA-------------GGH-----NLLMIGPPGSGKTMLARRL 231
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 50-107 1.88e-06

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 48.00  E-value: 1.88e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVGKEVdSIIRDLTDVA 107
Cdd:cd19501   37 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFEQA 92
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 53-137 7.43e-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: 7.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   53 ILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLtdvaIKLVRET--------EMEKM---KY 121
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLREL----FEAAKKLapcvifidEIDALagsRG 74

                          90
                  ....*....|....*.
gi 498361875  122 RAEEAAEERILDALLP 137
Cdd:pfam00004  75 SGGDSESRRVVNQLLT 90
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 50-107 9.95e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 47.31  E-value: 9.95e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDVA 107
Cdd:COG1222  112 PKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS-KYIG-EGARNVREVFELA 167
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 244-331 1.35e-05

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: 44.51  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  244 ASVENNGIVFLDEIDKICKRGESSGPDVSREgVQRDLLPLVEGCTVNtkhgmvkTDHILFVASGafqiAKPSDLIPELQG 323
Cdd:pfam00004  53 AKKLAPCVIFIDEIDALAGSRGSGGDSESRR-VVNQLLTELDGFTSS-------NSKVIVIAAT----NRPDKLDPALLG 120


                  ....*...
gi 498361875  324 RLPIRVEL 331
Cdd:pfam00004 121 RFDRIIEF 128
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 50-110 3.10e-05

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 44.32  E-value: 3.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFteVGYVGKEVDSIIRDLTDVAIKL 110
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAISN 92
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 17-93 3.43e-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: 45.67  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  17 IIGQADAKRAvavaLRNRWRRMQLSEEMRHE---VTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG 93
Cdd:COG0464  159 LGGLEEVKEE----LRELVALPLKRPELREEyglPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
50-109 4.01e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 45.80  E-value: 4.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVGKEVdSIIRDLTDVAIK 109
Cdd:PRK10733 185 PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGA-SRVRDMFEQAKK 242
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 17-70 7.43e-05

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 43.68  E-value: 7.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 498361875   17 IIGQADAKRAVAVALRNRwrrmqlseemrHevtpkNILMIGPTGVGKTEIARRL 70
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGG-----------H-----NLLMIGPPGSGKTMLAKRL 42
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 50-107 7.96e-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: 43.09  E-value: 7.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDVA 107
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVRELFEMA 92
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 50-110 9.38e-05

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: 42.72  E-value: 9.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTeVGYVGkEVDSIIRDLTDVAIKL 110
Cdd:cd19509   32 PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG-ESEKIVRALFALAREL 90
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 52-88 9.84e-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: 42.28  E-value: 9.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 498361875   52 NILMIGPTGVGKTEIARRLAK-LANAPFIKVEATKFTE 88
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
ftsH CHL00176
cell division protein; Validated
 50-103 1.55e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 43.89  E-value: 1.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGyVGKevdSIIRDL 103
Cdd:CHL00176 216 PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG-VGA---ARVRDL 267
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 50-136 3.29e-04

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 40.94  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVDSIIRDLTDVAIKLVRETEMEKMKYR----A 123
Cdd:cd19529   27 PKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVGESEKAIREIFRKARQVAPCVIFFDEIDSIAPRrgttG 106

                         90
                 ....*....|...
gi 498361875 124 EEAAEERILDALL 136
Cdd:cd19529  107 DSGVTERVVNQLL 119
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 3.78e-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: 41.12  E-value: 3.78e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISG 67
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
11-95 3.88e-04

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 42.91  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  11 HELDRHIIGQADAKRAVAVALRNRwrRMQLSEEMRhevTPKNILMIGPTGVGKTEIARRLAKL---ANAPFIKVEATKFT 87
Cdd:PRK10865 564 QELHHRVIGQNEAVEAVSNAIRRS--RAGLSDPNR---PIGSFLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEFM 638

                         90
                 ....*....|....*....
gi 498361875  88 EV-----------GYVGKE 95
Cdd:PRK10865 639 EKhsvsrlvgappGYVGYE 657
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 50-107 4.13e-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: 4.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDVA 107
Cdd:cd19525   55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVG-EGEKMVRALFSVA 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 4.74e-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: 4.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361875  49 TPKNILMIGPTGVGKTEIARRLAKLANAPFIkveATKFTEV--GYVGkEVDSIIRDLTDVA 107
Cdd:cd19511   26 PPKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREIFQKA 82
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 50-110 4.99e-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: 40.49  E-value: 4.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYvgKEVDSIIRDLTDVAIKL 110
Cdd:cd19520   35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY--GESQKLVAAVFSLASKL 93
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 17-110 5.26e-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: 40.60  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  17 IIGQADAKRAVAVALRNRWRRMQLSEEMRheVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEV 96
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLR--APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77

                         90
                 ....*....|....
gi 498361875  97 DSIIRDLTDVAIKL 110
Cdd:cd19524   78 EKLVRALFAVAREL 91
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 12-71 5.40e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 5.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498361875  12 ELDRHIIGQADAKRAVAVALRnrwR-RMQLSEEMRhevtPknI---LMIGPTGVGKTEIARRLA 71
Cdd:COG0542  546 ELHERVIGQDEAVEAVADAIR---RsRAGLKDPNR----P--IgsfLFLGPTGVGKTELAKALA 600
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 49-81 7.90e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 7.90e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 498361875    49 TPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 52-79 1.02e-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: 39.46  E-value: 1.02e-03
                         10        20
                 ....*....|....*....|....*...
gi 498361875  52 NILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 50-107 1.19e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 40.97  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDVA 107
Cdd:PRK03992 165 PKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQ-KFIG-EGARLVRELFELA 220
Sigma54_activat pfam00158
Sigma-54 interaction domain;
49-81 1.19e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.69  E-value: 1.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 498361875   49 TPKNILMIGPTGVGKTEIAR---RLAKLANAPFIKV 81
Cdd:pfam00158  21 TDAPVLITGESGTGKELFARaihQLSPRADGPFVAV 56
aroK PRK00131
shikimate kinase; Reviewed
 50-79 1.68e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.02  E-value: 1.68e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:PRK00131   4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
AAA_22 pfam13401
AAA domain;
46-136 3.17e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   46 HEVTPKNILMIGPTGVGKTEIARRLAKL---ANAPFIKVEATKFTevgyvgkevdsiirDLTDVAIKLVRETEMEKMKYR 122
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQlpeVRDSVVFVDLPSGT--------------SPKDLLRALLRALGLPLSGRL 66

                          90
                  ....*....|....
gi 498361875  123 AEEAAEERILDALL 136
Cdd:pfam13401  67 SKEELLAALQQLLL 80
clpC CHL00095
Clp protease ATP binding subunit
 7-93 3.59e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 39.65  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   7 REIVHEldrHIIGQADAKRAVAVALRnrwrrmqlseemRHEVTPKNI-------LMIGPTGVGKTEIARRLAKL---ANA 76
Cdd:CHL00095 504 EETLHK---RIIGQDEAVVAVSKAIR------------RARVGLKNPnrpiasfLFSGPTGVGKTELTKALASYffgSED 568

                         90       100
                 ....*....|....*....|....*...
gi 498361875  77 PFIKVEATKFTE-----------VGYVG 93
Cdd:CHL00095 569 AMIRLDMSEYMEkhtvskligspPGYVG 596
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 50-148 5.75e-03

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 37.42  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEatkftevgyvGKEVDSiirdltdvaiKLVRETE--MEKMKYRAEEAA 127
Cdd:cd19519   34 PRGILLYGPPGTGKTLIARAVANETGAFFFLIN----------GPEIMS----------KLAGESEsnLRKAFEEAEKNA 93

                         90       100
                 ....*....|....*....|....*
gi 498361875 128 EERI----LDALLPNPRNSWGEEEK 148
Cdd:cd19519   94 PAIIfideIDAIAPKREKTHGEVER 118
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 53-79 5.99e-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: 5.99e-03
                         10        20
                 ....*....|....*....|....*..
gi 498361875  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 55-84 6.58e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.53  E-value: 6.58e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 498361875  55 MI--GPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:PRK13342  39 MIlwGPPGTGKTTLARIIAGATDAPFEALSAV 70
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
50-103 7.52e-03

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 38.48  E-value: 7.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498361875  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGyVGKevdSIIRDL 103
Cdd:COG0465  175 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVG-VGA---SRVRDL 226
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 50-148 9.46e-03

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 38.35  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498361875   50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEatkftevgyvGKEVDSiirdltdvaiKLVRETE--MEKMKYRAEEAA 127
Cdd:TIGR01243 212 PKGVLLYGPPGTGKTLLAKAVANEAGAYFISIN----------GPEIMS----------KYYGESEerLREIFKEAEENA 271

                          90       100
                  ....*....|....*....|....*
gi 498361875  128 EERI----LDALLPNPRNSWGEEEK 148
Cdd:TIGR01243 272 PSIIfideIDAIAPKREEVTGEVEK 296
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
53-79 9.59e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.81  E-value: 9.59e-03
                         10        20
                 ....*....|....*....|....*..
gi 498361875  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRL 28
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
1-74 9.73e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 37.92  E-value: 9.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498361875   1 MSEMTPREIVHELDRHIiGQADAKRAVAVALRnrwRRMQLSEEMRHEvTPKNILMIGPTGVGKTEIarrLAKLA 74
Cdd:COG1419  120 VSPELARELLEKLPEDL-SAEEAWRALLEALA---RRLPVAEDPLLD-EGGVIALVGPTGVGKTTT---IAKLA 185
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 54-109 9.75e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 38.28  E-value: 9.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498361875  54 LMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE-----------VGYVGKEVDSIirdLTDVAIK 109
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGL---LTDAVIK 555
 
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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