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Conserved domains on  [gi|515628550|ref|WP_017061150|]
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MULTISPECIES: HslU--HslV peptidase ATPase subunit [Vibrio]

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;
1-446 0e+00

ATP-dependent protease ATPase subunit HslU;


:

Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 890.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   1 MSEMTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  81 VEATKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQNEQSTEDttsSNTRQ 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEI---SATRQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 161 IFRKKLREGKLDDKEIEVDVAAPQMGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEEAAKLVNQE 240
Cdd:PRK05201 158 KFRKKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 241 ELKENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSD 320
Cdd:PRK05201 238 EIKQEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 321 LIPELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTENIGARRLHT 400
Cdd:PRK05201 318 LIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHT 397

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 515628550 401 VMERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:PRK05201 398 VMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-446 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 890.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   1 MSEMTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  81 VEATKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQNEQSTEDttsSNTRQ 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEI---SATRQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 161 IFRKKLREGKLDDKEIEVDVAAPQMGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEEAAKLVNQE 240
Cdd:PRK05201 158 KFRKKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 241 ELKENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSD 320
Cdd:PRK05201 238 EIKQEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 321 LIPELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTENIGARRLHT 400
Cdd:PRK05201 318 LIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHT 397

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 515628550 401 VMERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:PRK05201 398 VMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-446 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: 867.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   1 MSEMTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  81 VEATKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQN-------EQSTEDT 153
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNnpfeeeeEEEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 154 TSSNTRQIFRKKLREGKLDDKEIEVDVAA-PQMGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEE 232
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEEsSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 233 AAKLVNQEELKENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGA 312
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 313 FQVAKPSDLIPELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTEN 392
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515628550 393 IGARRLHTVMERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:COG1220  401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-446 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: 674.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550    4 MTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   84 TKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQNEQSTEdttSSNTRQIFR 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQE---PESAREAFR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  164 KKLREGKLDDKEIEVDVAAPQ-MGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEEAAKLVNQEEL 242
Cdd:TIGR00390 158 KKLREGELDDKEIEIDVSAKMpSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  243 KENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSDLI 322
Cdd:TIGR00390 238 KQEAIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  323 PELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTENIGARRLHTVM 402
Cdd:TIGR00390 318 PELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVL 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 515628550  403 ERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:TIGR00390 398 ERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-335 2.36e-105

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 310.08  E-value: 2.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   5 TPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  85 KFTEVGYVGKEVETIIRDLTDvaikmthqqamekvqyraeeqaeerildallppardawgqneqstedttssntrqifrk 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 165 klregklddkeievdvaapqmgveimsppgmeemtnqlqgmfqnlagdtkkkrkmkikdafkalteeeaaklvnqeelke 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 245 naifnaennGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSDLIPE 324
Cdd:cd19498  102 ---------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPE 172

                        330
                 ....*....|.
gi 515628550 325 LQGRLPIRVEL 335
Cdd:cd19498  173 LQGRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 173-332 5.94e-24

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: 97.65  E-value: 5.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  173 DKEIEVDVAAPQmGVeimSPPGMEEMTNQLQGMFQNlagdtkkkrKMKIKDAFKaLTEEeaaKLVNQEELKENAIFNAEN 252
Cdd:pfam07724   1 RPIGSFLFLGPT-GV---GKTELAKALAELLFGDER---------ALIRIDMSE-YMEE---HSVSRLIGAPPGYVGYEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  253 NG------------IVFIDEIDKICKrgdssgpdvsreGVQRDLLPLIEGSTVSTKHG-MVKTDHILFITSGAFQVAKPS 319
Cdd:pfam07724  64 GGqlteavrrkpysIVLIDEIEKAHP------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKIS 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 515628550  320 D------------------------LIPELQGRLPIR 332
Cdd:pfam07724 132 DasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 338-425 1.25e-11

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: 60.54  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   338 LSAHDFKRILTEPKASLTEQYialmKTEDVNIEFTEDGINQIADAAWRvnettENIGARRLHTVMERLMDEISFEA---- 413
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|..
gi 515628550   414 TDKAGSKLVIDE 425
Cdd:smart01086  72 ELKDGDTVVVDV 83
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-446 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 890.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   1 MSEMTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  81 VEATKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQNEQSTEDttsSNTRQ 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEI---SATRQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 161 IFRKKLREGKLDDKEIEVDVAAPQMGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEEAAKLVNQE 240
Cdd:PRK05201 158 KFRKKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 241 ELKENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSD 320
Cdd:PRK05201 238 EIKQEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 321 LIPELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTENIGARRLHT 400
Cdd:PRK05201 318 LIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHT 397

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 515628550 401 VMERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:PRK05201 398 VMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-446 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: 867.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   1 MSEMTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  81 VEATKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQN-------EQSTEDT 153
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNnpfeeeeEEEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 154 TSSNTRQIFRKKLREGKLDDKEIEVDVAA-PQMGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEE 232
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEEsSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 233 AAKLVNQEELKENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGA 312
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 313 FQVAKPSDLIPELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTEN 392
Cdd:COG1220  321 FHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTEN 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515628550 393 IGARRLHTVMERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:COG1220  401 IGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-446 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: 674.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550    4 MTPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   84 TKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYRAEEQAEERILDALLPPARDAWGQNEQSTEdttSSNTRQIFR 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQE---PESAREAFR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  164 KKLREGKLDDKEIEVDVAAPQ-MGVEIMSPPGMEEMTNQLQGMFQNLAGDTKKKRKMKIKDAFKALTEEEAAKLVNQEEL 242
Cdd:TIGR00390 158 KKLREGELDDKEIEIDVSAKMpSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  243 KENAIFNAENNGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSDLI 322
Cdd:TIGR00390 238 KQEAIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  323 PELQGRLPIRVELEALSAHDFKRILTEPKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRVNETTENIGARRLHTVM 402
Cdd:TIGR00390 318 PELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVL 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 515628550  403 ERLMDEISFEATDKAGSKLVIDEAYVTSKLGEFVEDEDLSRFIL 446
Cdd:TIGR00390 398 ERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-335 2.36e-105

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 310.08  E-value: 2.36e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   5 TPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  85 KFTEVGYVGKEVETIIRDLTDvaikmthqqamekvqyraeeqaeerildallppardawgqneqstedttssntrqifrk 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 165 klregklddkeievdvaapqmgveimsppgmeemtnqlqgmfqnlagdtkkkrkmkikdafkalteeeaaklvnqeelke 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 245 naifnaennGIVFIDEIDKICKRGDSSGPDVSREGVQRDLLPLIEGSTVSTKHGMVKTDHILFITSGAFQVAKPSDLIPE 324
Cdd:cd19498  102 ---------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPE 172

                        330
                 ....*....|.
gi 515628550 325 LQGRLPIRVEL 335
Cdd:cd19498  173 LQGRFPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
5-431 7.85e-66

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 216.56  E-value: 7.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   5 TPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLR--VEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:PRK05342  61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDddVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  83 ATKFTEVGYVGKEVETIIRDLTDVAikmthqqamekvqyraeeqaeerildallppardawgqneqstedttssntrqif 162
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 163 rkklregklddkeiEVDVAAPQMgveimsppgmeemtnqlqgmfqnlagdtkkkrkmkikdafkalteeeaaklvnqeel 242
Cdd:PRK05342 166 --------------DYDVEKAQR--------------------------------------------------------- 174

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 243 kenaifnaennGIVFIDEIDKICKRGD--SSGPDVSREGVQRDLLPLIEGSTVST------KHGM-----VKTDHILFIT 309
Cdd:PRK05342 175 -----------GIVYIDEIDKIARKSEnpSITRDVSGEGVQQALLKILEGTVASVppqggrKHPQqefiqVDTTNILFIC 243

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 310 SGAF-----------------------------------QVAKPSDL-----IPELQGRLPIRVELEALSAHDFKRILTE 349
Cdd:PRK05342 244 GGAFdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLPVVATLEELDEEALVRILTE 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 350 PKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRvnettENIGARRLHTVMERLMDEISFEA-TDKAGSKLVIDEAYV 428
Cdd:PRK05342 324 PKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMFELpSREDVEKVVITKEVV 398


                 ...
gi 515628550 429 TSK 431
Cdd:PRK05342 399 EGK 401
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-431 2.88e-61

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 204.51  E-value: 2.88e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   5 TPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLR--VEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:COG1219   62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDddVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  83 ATKFTEVGYVGKEVETIIRDLTDVAikmthqqamekvqyraeeqaeerildallppardawgqneqstedttssntrqif 162
Cdd:COG1219  142 ATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 163 rkklregklddkeiEVDVAAPQMgveimsppgmeemtnqlqgmfqnlagdtkkkrkmkikdafkalteeeaaklvnqeel 242
Cdd:COG1219  167 --------------DYDVEKAER--------------------------------------------------------- 175

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 243 kenaifnaennGIVFIDEIDKICKRGD--SSGPDVSREGVQRDLLPLIEGSTVST------KHGM-----VKTDHILFIT 309
Cdd:COG1219  176 -----------GIIYIDEIDKIARKSEnpSITRDVSGEGVQQALLKILEGTVANVppqggrKHPQqefiqIDTTNILFIC 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 310 SGAF-----------------------------------QVAkPSDL-----IPELQGRLPIRVELEALSAHDFKRILTE 349
Cdd:COG1219  245 GGAFdglekiierrlgkksigfgaevkskkekdegellkQVE-PEDLikfglIPEFIGRLPVIATLEELDEEALVRILTE 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 350 PKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRvnettENIGARRLHTVMERLMDEISFEA-TDKAGSKLVIDEAYV 428
Cdd:COG1219  324 PKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMYELpSRKDVKKVVITKEVV 398


                 ...
gi 515628550 429 TSK 431
Cdd:COG1219  399 EGK 401
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 5-429 1.04e-42

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: 155.31  E-value: 1.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550    5 TPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLR----VEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKsdngVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   81 VEATKFTEVGYVGKEVETIirdltdvaikmthqqamekvqyraeeqaeerildallppardawgqneqstedttssntrq 160
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENI------------------------------------------------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  161 ifrkklregklddkeievdvaapqmgveimsppgmeemtnqLQGMFQNLAGDTkkkrkmkikdafkalteEEAAKlvnqe 240
Cdd:TIGR00382 166 -----------------------------------------LLKLLQAADYDV-----------------EKAQK----- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  241 elkenaifnaennGIVFIDEIDKICKRGD--SSGPDVSREGVQRDLLPLIEGSTVST------KHG-----MVKTDHILF 307
Cdd:TIGR00382 183 -------------GIIYIDEIDKISRKSEnpSITRDVSGEGVQQALLKIIEGTVANVppqggrKHPyqefiQIDTSNILF 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  308 ITSGAF---------------------------------QVAKPSD-----LIPELQGRLPIRVELEALSAHDFKRILTE 349
Cdd:TIGR00382 250 ICGGAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLIPEFIGRLPVIATLEKLDEEALIAILTK 329

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  350 PKASLTEQYIALMKTEDVNIEFTEDGINQIADAAWRvnettENIGARRLHTVMERLMDEISFE-ATDKAGSKLVIDEAYV 428
Cdd:TIGR00382 330 PKNALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFDlPSLEDLEKVVITKETV 404


                  .
gi 515628550  429 T 429
Cdd:TIGR00382 405 L 405
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 5-335 1.94e-32

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 123.48  E-value: 1.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   5 TPREIVHELNRHIIGQDNAKRSVAIALRNRWRRMQLEESLR---VEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:cd19497    2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKdddVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  82 EATKFTEVGYVGKEVETIIRDLTDVAikmthqqamekvqyraeeqaeerildallppardawgqneqstedttssntrqi 161
Cdd:cd19497   82 DATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------ 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 162 frkklregklddkeiEVDVAAPQMgveimsppgmeemtnqlqgmfqnlagdtkkkrkmkikdafkalteeeaaklvnqee 241
Cdd:cd19497  108 ---------------DYDVERAQR-------------------------------------------------------- 116

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 242 lkenaifnaennGIVFIDEIDKICKRGDSSG--PDVSREGVQRDLLPLIEGSTVST------KHG-----MVKTDHILFI 308
Cdd:cd19497  117 ------------GIVYIDEIDKIARKSENPSitRDVSGEGVQQALLKILEGTVANVppqggrKHPqqefiQVDTTNILFI 184

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515628550 309 TSGAFQ-----VAK------------------------------PSDL-----IPELQGRLPIRVEL 335
Cdd:cd19497  185 CGGAFVglekiIARrlgkkslgfgaetssekdekerdellskvePEDLikfglIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 173-332 5.94e-24

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: 97.65  E-value: 5.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  173 DKEIEVDVAAPQmGVeimSPPGMEEMTNQLQGMFQNlagdtkkkrKMKIKDAFKaLTEEeaaKLVNQEELKENAIFNAEN 252
Cdd:pfam07724   1 RPIGSFLFLGPT-GV---GKTELAKALAELLFGDER---------ALIRIDMSE-YMEE---HSVSRLIGAPPGYVGYEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  253 NG------------IVFIDEIDKICKrgdssgpdvsreGVQRDLLPLIEGSTVSTKHG-MVKTDHILFITSGAFQVAKPS 319
Cdd:pfam07724  64 GGqlteavrrkpysIVLIDEIEKAHP------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKIS 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 515628550  320 D------------------------LIPELQGRLPIR 332
Cdd:pfam07724 132 DasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 23-107 2.03e-14

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 70.39  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  23 AKRSVAIALRNRWRRMQLEEslRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVETII 100
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRR--YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78


                 ....*..
gi 515628550 101 RDLTDVA 107
Cdd:cd19481   79 ERARRLA 85
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 338-425 1.25e-11

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: 60.54  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   338 LSAHDFKRILTEPKASLTEQYialmKTEDVNIEFTEDGINQIADAAWRvnettENIGARRLHTVMERLMDEISFEA---- 413
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|..
gi 515628550   414 TDKAGSKLVIDE 425
Cdd:smart01086  72 ELKDGDTVVVDV 83
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 18-112 6.34e-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: 54.46  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  18 IGQDNAKRSVAIALRNRwrrmqleeslrvevSPKNILMIGPTGVGKTEIARRLAKLA---NAPFIKVEATKFTEVGYVGK 94
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                         90
                 ....*....|....*...
gi 515628550  95 EVETIIRDLTDVAIKMTH 112
Cdd:cd00009   67 LFGHFLVRLLFELAEKAK 84
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 4-84 2.80e-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: 54.79  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   4 MTPREIVHELNRHIIGQDNAKRSVAIALRNRwrrmqleeslrvevspKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAG----------------GHLLLEGVPGVGKTTLAKALARALGLPFIRIQF 64


                 .
gi 515628550  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 9.26e-08

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 51.79  E-value: 9.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515628550  12 ELNRHIIGQDNAKRSVAIALRnrwrRMQLEESLRVEvSPKNILMIGPTGVGKTEIARRLAKL 73
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIR----RARAGLSDPNR-PIGSFLFLGPTGVGKTELAKALAEL 64
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 232-336 3.14e-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: 49.13  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  232 EAAKLVNQ--EELKENAIfnaennGIVFIDEIDKICKRGDSSGPDVSREgVQRDLLPLIEGSTvstkhgmVKTDHILFIT 309
Cdd:pfam00004  41 ESEKRLRElfEAAKKLAP------CVIFIDEIDALAGSRGSGGDSESRR-VVNQLLTELDGFT-------SSNSKVIVIA 106

                          90       100
                  ....*....|....*....|....*..
gi 515628550  310 SGafqvAKPSDLIPELQGRLPIRVELE 336
Cdd:pfam00004 107 AT----NRPDKLDPALLGRFDRIIEFP 129
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 50-107 1.04e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 50.39  E-value: 1.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVETIIRDLTDVA 107
Cdd:COG1222  112 PKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS-KYIG-EGARNVREVFELA 167
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 53-137 2.14e-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: 46.82  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   53 ILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVETIIRDLTDVAIKMT---------HqqAMEKVQYRA 123
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFEAAKKLApcvifideiD--ALAGSRGSG 76

                          90
                  ....*....|....
gi 515628550  124 EEQAEERILDALLP 137
Cdd:pfam00004  77 GDSESRRVVNQLLT 90
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 50-93 2.21e-06

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 47.61  E-value: 2.21e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVG 93
Cdd:cd19501   37 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVG 79
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 17-111 6.93e-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: 46.19  E-value: 6.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  17 IIGQDNAKRSVaialrnrwRRMQLEESLRVEV------SPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTeVG 90
Cdd:cd19509    1 IAGLDDAKEAL--------KEAVILPSLRPDLfpglrgPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SK 71

                         90       100
                 ....*....|....*....|.
gi 515628550  91 YVGkEVETIIRDLTDVAIKMT 111
Cdd:cd19509   72 WVG-ESEKIVRALFALARELQ 91
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 50-108 7.52e-06

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: 46.24  E-value: 7.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFteVGYVGKEVETIIRDLTDVAI 108
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAI 90
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 17-107 8.38e-06

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 47.98  E-value: 8.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  17 IIGQDNAKRsvaiALRNRWRRMQLEESLRVEVS---PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG 93
Cdd:COG0464  159 LGGLEEVKE----ELRELVALPLKRPELREEYGlppPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233

                         90
                 ....*....|....
gi 515628550  94 kEVETIIRDLTDVA 107
Cdd:COG0464  234 -ETEKNLREVFDKA 246
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 17-110 8.85e-06

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: 45.61  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  17 IIGQDNAKRSVAIALRNRWRRMQLEESLRVevSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEV 96
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLRA--PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77

                         90
                 ....*....|....
gi 515628550  97 ETIIRDLTDVAIKM 110
Cdd:cd19524   78 EKLVRALFAVAREL 91
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 52-88 6.21e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.66  E-value: 6.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 515628550   52 NILMIGPTGVGKTEIARRLAK-LANAPFIKVEATKFTE 88
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 50-107 6.43e-05

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: 43.04  E-value: 6.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIkveATKFTEV--GYVGkEVETIIRDLTDVA 107
Cdd:cd19511   27 PKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREIFQKA 82
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 49-122 7.68e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 7.68e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515628550    49 SPKNILMIGPTGVGKTEIARRLAKLANAP---FIKVEATKFTEVGYVGKEVETIIRDLTDVAIKMTHQQAMEKVQYR 122
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
50-109 8.58e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 45.03  E-value: 8.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVGKEVETiIRDLTDVAIK 109
Cdd:PRK10733 185 PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASR-VRDMFEQAKK 242
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 50-107 9.02e-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: 9.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVETIIRDLTDVA 107
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVRELFEMA 92
clpC CHL00095
Clp protease ATP binding subunit
 12-93 1.23e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 44.66  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  12 ELNRHIIGQDNAKRSVAIALRnrwrrmqleeslRVEVSPKNI-------LMIGPTGVGKTEIARRLAKL---ANAPFIKV 81
Cdd:CHL00095 506 TLHKRIIGQDEAVVAVSKAIR------------RARVGLKNPnrpiasfLFSGPTGVGKTELTKALASYffgSEDAMIRL 573

                         90       100
                 ....*....|....*....|...
gi 515628550  82 EATKFTE-----------VGYVG 93
Cdd:CHL00095 574 DMSEYMEkhtvskligspPGYVG 596
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 1.42e-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: 42.67  E-value: 1.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVETIIRDLTDVA 107
Cdd:cd19525   55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVG-EGEKMVRALFSVA 110
Sigma54_activat pfam00158
Sigma-54 interaction domain;
17-81 2.10e-04

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 41.62  E-value: 2.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515628550   17 IIGQDNAKRSVaialrnrwrrmqLEESLRVEVSPKNILMIGPTGVGKTEIAR---RLAKLANAPFIKV 81
Cdd:pfam00158   1 IIGESPAMQEV------------LEQAKRVAPTDAPVLITGESGTGKELFARaihQLSPRADGPFVAV 56
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 2.90e-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: 41.51  E-value: 2.90e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISG 67
ftsH CHL00176
cell division protein; Validated
 50-88 3.50e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 43.11  E-value: 3.50e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE 88
Cdd:CHL00176 216 PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVE 254
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 12-71 3.78e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 3.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515628550  12 ELNRHIIGQDNAKRSVAIALRnrwrrmqleESlRVEVSPKN--I---LMIGPTGVGKTEIARRLA 71
Cdd:COG0542  546 ELHERVIGQDEAVEAVADAIR---------RS-RAGLKDPNrpIgsfLFLGPTGVGKTELAKALA 600
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 17-70 4.12e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 41.37  E-value: 4.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515628550   17 IIGQDNAKRSVAIALRNRwrrmqleeslrvevspKNILMIGPTGVGKTEIARRL 70
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGG----------------HNLLMIGPPGSGKTMLAKRL 42
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 15-70 4.55e-04

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: 42.33  E-value: 4.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628550  15 RHIIGQDNAKRSVAIAlrnrwrrmqleeslrvevspkNILMIGPTGVGKTEIARRL 70
Cdd:COG0606  192 ADVKGQEQAKRALEIAaag----------------ghNLLMIGPPGSGKTMLARRL 231
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 36-91 5.14e-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: 5.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628550  36 RRMQLEESLRVEVSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGY 91
Cdd:cd19520   21 QRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY 76
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 243-336 5.63e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.21  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550 243 KENAIFNAENNGIVFIDEIDKIckrgdssgpdvsREGVQRDLLPLIEgsTVSTKHGMVKTDHILFITSGAFqvakPSDLI 322
Cdd:cd00009   75 LLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLE--TLNDLRIDRENVRVIGATNRPL----LGDLD 136

                         90
                 ....*....|....
gi 515628550 323 PELQGRLPIRVELE 336
Cdd:cd00009  137 RALYDRLDIRIVIP 150
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 50-107 5.65e-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: 40.56  E-value: 5.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVETIIRDLTDVA 107
Cdd:cd19529   27 PKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVGESEKAIREIFRKARQVA 86
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
11-95 8.26e-04

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 41.75  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  11 HELNRHIIGQDNAKRSVAIALRNRwrRMQLEESLRVEVSpknILMIGPTGVGKTEIARRLAKL---ANAPFIKVEATKFT 87
Cdd:PRK10865 564 QELHHRVIGQNEAVEAVSNAIRRS--RAGLSDPNRPIGS---FLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEFM 638

                         90
                 ....*....|....*....
gi 515628550  88 EV-----------GYVGKE 95
Cdd:PRK10865 639 EKhsvsrlvgappGYVGYE 657
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 52-79 8.30e-04

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


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 39.85  E-value: 8.30e-04
                         10        20
                 ....*....|....*....|....*...
gi 515628550  52 NILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 50-107 1.30e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 40.97  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVETIIRDLTDVA 107
Cdd:PRK03992 165 PKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQ-KFIG-EGARLVRELFELA 220
aroK PRK00131
shikimate kinase; Reviewed
 50-79 1.36e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.40  E-value: 1.36e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 515628550  50 PKNILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:PRK00131   4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 41-107 2.05e-03

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 38.65  E-value: 2.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515628550  41 EESLRVEVSP-KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYvgKEVETIIRDLTDVA 107
Cdd:cd19528   17 DKFLKFGMTPsKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWF--GESEANVRDIFDKA 82
ycf2 CHL00206
Ycf2; Provisional
 43-105 3.10e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 40.28  E-value: 3.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515628550   43 SLRVEVSP-KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVETIIRDLTD 105
Cdd:CHL00206 1622 SLRLALSPsRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDNKPKGFLIDDIDIDDSD 1685
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 48-136 3.37e-03

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 38.24  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  48 VSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVGkEVETIIRDLTDVA-------IKMTHQQAMEKVQ 120
Cdd:cd19530   28 DLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNK-YVG-ESERAVRQVFQRArasapcvIFFDEVDALVPKR 105

                         90
                 ....*....|....*.
gi 515628550 121 YRAEEQAEERILDALL 136
Cdd:cd19530  106 GDGGSWASERVVNQLL 121
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
1-74 3.59e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.46  E-value: 3.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515628550   1 MSEMTPREIVHELNRHIiGQDNAKRSVaialrnrwrRMQLEESLRVEVSP-----KNILMIGPTGVGKTEIarrLAKLA 74
Cdd:COG1419  120 VSPELARELLEKLPEDL-SAEEAWRAL---------LEALARRLPVAEDPlldegGVIALVGPTGVGKTTT---IAKLA 185
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 54-112 4.54e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.43  E-value: 4.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550  54 LMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE-----------VGYVGKEVETIirdLTDVAIKMTH 112
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGL---LTDAVIKHPH 558
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 53-79 4.70e-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: 37.80  E-value: 4.70e-03
                         10        20
                 ....*....|....*....|....*..
gi 515628550  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 36-81 4.91e-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: 37.80  E-value: 4.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515628550  36 RRMQLEESLRVEvSPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:cd19519   21 RHPELFKAIGIK-PPRGILLYGPPGTGKTLIARAVANETGAFFFLI 65
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 55-84 5.31e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.91  E-value: 5.31e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 515628550  55 MI--GPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:PRK13342  39 MIlwGPPGTGKTTLARIIAGATDAPFEALSAV 70
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
53-79 7.18e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 7.18e-03
                         10        20
                 ....*....|....*....|....*..
gi 515628550  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRL 28
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 51-103 7.51e-03

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 37.47  E-value: 7.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515628550  51 KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGkEVETIIRDL 103
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVG-ESEANIRKL 87
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 43-86 7.73e-03

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. 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: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 36.97  E-value: 7.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 515628550  43 SLRVEVSP-KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKF 86
Cdd:cd19505    4 SLRLGLSPsKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKL 48
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 36-148 9.34e-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: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628550   36 RRMQLEESLRVEvSPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGKEvetiirdltdvaikmthQQA 115
Cdd:TIGR01243 199 KHPELFEHLGIE-PPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMS-KYYGES-----------------EER 259

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 515628550  116 MEKVQYRAEEQAEERI----LDALLPPARDAWGQNEQ 148
Cdd:TIGR01243 260 LREIFKEAEENAPSIIfideIDAIAPKREEVTGEVEK 296
 
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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