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Conserved domains on  [gi|2281921883|ref|WP_256683486|]
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MULTISPECIES: HslU--HslV peptidase ATPase subunit [Bacillus]

Protein Classification

ATP-dependent protease ATPase subunit HslU( domain architecture ID 18510702)

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 COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 9-470 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: 863.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:COG1220     4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQSGVKNPFEmffggsqpngEDE 168
Cdd:COG1220    84 TKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPFE----------EEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 AESQEEANIEEKRKRMAHQLALGELEDYYVTVEVEEQQPSMFDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:COG1220   154 EEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEAR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:COG1220   234 KILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGG-GSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:COG1220   313 ILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAF 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:COG1220   393 EVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
 
Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 9-470 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: 863.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:COG1220     4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQSGVKNPFEmffggsqpngEDE 168
Cdd:COG1220    84 TKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPFE----------EEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 AESQEEANIEEKRKRMAHQLALGELEDYYVTVEVEEQQPSMFDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:COG1220   154 EEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEAR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:COG1220   234 KILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGG-GSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:COG1220   313 ILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAF 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:COG1220   393 EVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
9-470 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 821.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:PRK05201    4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQSGvknpfemffggsqpngede 168
Cdd:PRK05201   84 TKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWG------------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 aESQEEANIEEKRKRMAHQLALGELEDYYVTVEVEEQQPSMfDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:PRK05201  145 -EEEEKEEISATRQKFRKKLREGELDDKEIEIEVAEAAPMM-EIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEAR 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:PRK05201  223 KILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGG-SSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDH 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:PRK05201  302 ILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAY 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:PRK05201  382 QVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 9-470 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: 706.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQsgvknpfemfFGGSQpnGEDE 168
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQ----------WGQTE--QQQE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 AESQEEANIEEKRKrmahqlalGELEDYYVTVEVEEQQPSMFDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:TIGR00390 149 PESAREAFRKKLRE--------GELDDKEIEIDVSAKMPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAK 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGgASSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:TIGR00390 221 KALIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKG-ESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:TIGR00390 300 ILFIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAY 379

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:TIGR00390 380 NVNEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 10-359 4.74e-101

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: 300.07  E-value: 4.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  10 TPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEAT 89
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  90 KFTEVGYVGRDVESMVRDLVEtsvrlikeekmnevkeqaeenankrivrllvpgkkkqsgvknpfemffggsqpngedea 169
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 170 esqeeanieekrkrmahqlalgeledyyvtveveeqqpsmfdmlqgsgmeqmgmnmqdalsglmpkkkkrrkmtvreark 249
Cdd:cd19498       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 250 vltneeasklidmdevgqeavqraeesGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDHV 329
Cdd:cd19498   102 ---------------------------GIVFIDEIDKIAKRGG-SSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHI 153

                         330       340       350
                  ....*....|....*....|....*....|
gi 2281921883 330 LFIAAGAFHMAKPSDLIPELQGRFPIRVEL 359
Cdd:cd19498   154 LFIAAGAFHVAKPSDLIPELQGRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 209-356 1.65e-25

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: 102.27  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 209 MFDMLQGSG---MEQMGMNMQDALsglmpkkkkRRKMTVREARKVLtnEEasKLIDMDEVGQEAVQRAEESG-------- 277
Cdd:pfam07724   7 LFLGPTGVGkteLAKALAELLFGD---------ERALIRIDMSEYM--EE--HSVSRLIGAPPGYVGYEEGGqlteavrr 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 278 ----IIFIDEIDKIAKnggasssadvsreGVQRDILPIVEGSTVVTKYGS-VKTDHVLFIAAGAFHMAKPSD-------- 344
Cdd:pfam07724  74 kpysIVLIDEIEKAHP-------------GVQNDLLQILEGGTLTDKQGRtVDFKNTLFIMTGNFGSEKISDasrlgdsp 140

                         170       180
                  ....*....|....*....|....*...
gi 2281921883 345 ----------------LIPELQGRFPIR 356
Cdd:pfam07724 141 dyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 362-438 1.55e-15

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: 71.71  E-value: 1.55e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2281921883  362 LTVDDFVRILVEPDNALLKQYQallqTEGISLEFSDEAIHKIAEVAYHVnqdtdNIGARRLHTILERLLEDLSFEAP 438
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDP-----KYGARPLRRIIQRELEDPLAELI 68
 
Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 9-470 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: 863.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:COG1220     4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQSGVKNPFEmffggsqpngEDE 168
Cdd:COG1220    84 TKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPFE----------EEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 AESQEEANIEEKRKRMAHQLALGELEDYYVTVEVEEQQPSMFDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:COG1220   154 EEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEAR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:COG1220   234 KILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGG-GSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:COG1220   313 ILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAF 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:COG1220   393 EVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
9-470 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 821.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:PRK05201    4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQSGvknpfemffggsqpngede 168
Cdd:PRK05201   84 TKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWG------------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 aESQEEANIEEKRKRMAHQLALGELEDYYVTVEVEEQQPSMfDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:PRK05201  145 -EEEEKEEISATRQKFRKKLREGELDDKEIEIEVAEAAPMM-EIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEAR 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:PRK05201  223 KILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGG-SSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDH 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:PRK05201  302 ILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAY 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:PRK05201  382 QVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 9-470 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: 706.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEA 88
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  89 TKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQsgvknpfemfFGGSQpnGEDE 168
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQ----------WGQTE--QQQE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 169 AESQEEANIEEKRKrmahqlalGELEDYYVTVEVEEQQPSMFDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREAR 248
Cdd:TIGR00390 149 PESAREAFRKKLRE--------GELDDKEIEIDVSAKMPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAK 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 249 KVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGgASSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDH 328
Cdd:TIGR00390 221 KALIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKG-ESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 329 VLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAY 408
Cdd:TIGR00390 300 ILFIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAY 379

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883 409 HVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL 470
Cdd:TIGR00390 380 NVNEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 10-359 4.74e-101

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: 300.07  E-value: 4.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  10 TPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEAT 89
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  90 KFTEVGYVGRDVESMVRDLVEtsvrlikeekmnevkeqaeenankrivrllvpgkkkqsgvknpfemffggsqpngedea 169
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 170 esqeeanieekrkrmahqlalgeledyyvtveveeqqpsmfdmlqgsgmeqmgmnmqdalsglmpkkkkrrkmtvreark 249
Cdd:cd19498       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 250 vltneeasklidmdevgqeavqraeesGIIFIDEIDKIAKNGGaSSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDHV 329
Cdd:cd19498   102 ---------------------------GIVFIDEIDKIAKRGG-SSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHI 153

                         330       340       350
                  ....*....|....*....|....*....|
gi 2281921883 330 LFIAAGAFHMAKPSDLIPELQGRFPIRVEL 359
Cdd:cd19498   154 LFIAAGAFHVAKPSDLIPELQGRFPIRVEL 183
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-455 2.19e-69

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 226.47  E-value: 2.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   5 EKKPLTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEV-VPK-NILMMGPTGVGKTEIARRIAKLSGAP 82
Cdd:COG1219    57 LKKLPKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVeLEKsNILLIGPTGSGKTLLAQTLARILDVP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  83 FIKIEATKFTEVGYVGRDVESMvrdlvetsvrlikeekmnevkeqaeenankrIVRLLvpgkkkqsgvknpfemffggsq 162
Cdd:COG1219   137 FAIADATTLTEAGYVGEDVENI-------------------------------LLKLL---------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 163 pngedeaesqeeanieekrkrmahqlalgeledyyvtveveeqqpsmfdmlqgsgmeqmgmnmQDAlsglmpkkkkrrkm 242
Cdd:COG1219   164 ---------------------------------------------------------------QAA-------------- 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 243 tvrearkvltneeaskliDMDevgqeaVQRAEEsGIIFIDEIDKIA-KNGGASSSADVSREGVQRDILPIVEGSTV-VTK 320
Cdd:COG1219   167 ------------------DYD------VEKAER-GIIYIDEIDKIArKSENPSITRDVSGEGVQQALLKILEGTVAnVPP 221

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 321 YGSVK----------TDHVLFIAAGAF----------------------------------HMAKPSDL-----IPELQG 351
Cdd:COG1219   222 QGGRKhpqqefiqidTTNILFICGGAFdglekiierrlgkksigfgaevkskkekdegellKQVEPEDLikfglIPEFIG 301

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 352 RFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAyhVNQDTdniGARRLHTILERLLE 431
Cdd:COG1219   302 RLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKA--IERKT---GARGLRSILEEILL 376

                         490       500
                  ....*....|....*....|....*
gi 2281921883 432 DLSFEAPDVT-MEKITITPQYVEEK 455
Cdd:COG1219   377 DVMYELPSRKdVKKVVITKEVVEGK 401
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
9-455 5.27e-67

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 220.42  E-value: 5.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEV-VPK-NILMMGPTGVGKTEIARRIAKLSGAPFIKI 86
Cdd:PRK05342   60 PTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVeLQKsNILLIGPTGSGKTLLAQTLARILDVPFAIA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  87 EATKFTEVGYVGRDVESMvrdlvetsvrlikeekmnevkeqaeenankrIVRLLvpgkkkqsgvknpfemffggsqpnge 166
Cdd:PRK05342  140 DATTLTEAGYVGEDVENI-------------------------------LLKLL-------------------------- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 167 deaesqeeanieekrkrmahqlalgeledyyvtveveeqqpsmfdmlqgsgmeqmgmnmQDAlsglmpkkkkrrkmtvre 246
Cdd:PRK05342  163 -----------------------------------------------------------QAA------------------ 165

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 247 arkvltneeaskliDMDevgqeaVQRAEEsGIIFIDEIDKIA-KNGGASSSADVSREGVQRDILPIVEGSTV-VTKYGSV 324
Cdd:PRK05342  166 --------------DYD------VEKAQR-GIVYIDEIDKIArKSENPSITRDVSGEGVQQALLKILEGTVAsVPPQGGR 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 325 K----------TDHVLFIAAGAF-----------------------------------HMAKPSDL-----IPELQGRFP 354
Cdd:PRK05342  225 KhpqqefiqvdTTNILFICGGAFdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLP 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 355 IRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAyhVNQDTdniGARRLHTILERLLEDLS 434
Cdd:PRK05342  305 VVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKA--IERKT---GARGLRSILEEILLDVM 379

                         490       500
                  ....*....|....*....|....
gi 2281921883 435 FEAP---DVtmEKITITPQYVEEK 455
Cdd:PRK05342  380 FELPsreDV--EKVVITKEVVEGK 401
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 2-453 2.43e-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: 154.93  E-value: 2.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   2 RRMEKKPLTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRsLLDEKLKD-----EVVPKNILMMGPTGVGKTEIARRIA 76
Cdd:TIGR00382  59 EFELSYLPTPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKR-LNFEKNKKsdngvELSKSNILLIGPTGSGKTLLAQTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  77 KLSGAPFIKIEATKFTEVGYVGRDVESMVRDLVETSvrlikeekmnevkeqaeenankrivrllvpgkkkqsgvknpfem 156
Cdd:TIGR00382 138 RILNVPFAIADATTLTEAGYVGEDVENILLKLLQAA-------------------------------------------- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 157 ffggsqpngedeaesqeeanieekrkrmahqlalgeledyyvtveveeqqpsmfdmlqgsgmeqmgmnmqdalsglmpkk 236
Cdd:TIGR00382     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 237 kkrrkmtvrearkvltneeaskliDMDevgqeaVQRAEEsGIIFIDEIDKIA-KNGGASSSADVSREGVQRDILPIVEGS 315
Cdd:TIGR00382 174 ------------------------DYD------VEKAQK-GIIYIDEIDKISrKSENPSITRDVSGEGVQQALLKIIEGT 222

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 316 TV-VTKYGSVK----------TDHVLFIAAGAF---------------------------------HMAKPSD-----LI 346
Cdd:TIGR00382 223 VAnVPPQGGRKhpyqefiqidTSNILFICGGAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLI 302

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 347 PELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAYHvnqdtDNIGARRLHTIL 426
Cdd:TIGR00382 303 PEFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIV 377

                         490       500
                  ....*....|....*....|....*...
gi 2281921883 427 ERLLEDLSFEAPDVT-MEKITITPQYVE 453
Cdd:TIGR00382 378 EGLLLDVMFDLPSLEdLEKVVITKETVL 405
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 9-359 1.61e-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: 124.25  E-value: 1.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   9 LTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVV--PK-NILMMGPTGVGKTEIARRIAKLSGAPFIK 85
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDDDVelEKsNILLIGPTGSGKTLLAQTLAKILDVPFAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  86 IEATKFTEVGYVGRDVESMvrdlvetsvrlikeekmnevkeqaeenankrIVRLLvpgkkkqsgvknpfemffggsqpng 165
Cdd:cd19497    81 ADATTLTEAGYVGEDVENI-------------------------------LLKLL------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 166 edeaesqeeanieekrkrmahqlalgeledyyvtveveeqQPSMFDmlqgsgmeqmgmnmqdalsglmpkkkkrrkmtvr 245
Cdd:cd19497   105 ----------------------------------------QAADYD---------------------------------- 110

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 246 earkvltneeasklidmdevgqeaVQRAEEsGIIFIDEIDKIA-KNGGASSSADVSREGVQRDILPIVEGSTV-VTKYGS 323
Cdd:cd19497   111 ------------------------VERAQR-GIVYIDEIDKIArKSENPSITRDVSGEGVQQALLKILEGTVAnVPPQGG 165

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 324 VK----------TDHVLFIAAGAF-----------------------------------HMAKPSDL-----IPELQGRF 353
Cdd:cd19497   166 RKhpqqefiqvdTTNILFICGGAFvglekiiarrlgkkslgfgaetssekdekerdellSKVEPEDLikfglIPEFVGRL 245


                  ....*.
gi 2281921883 354 PIRVEL 359
Cdd:cd19497   246 PVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 209-356 1.65e-25

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: 102.27  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 209 MFDMLQGSG---MEQMGMNMQDALsglmpkkkkRRKMTVREARKVLtnEEasKLIDMDEVGQEAVQRAEESG-------- 277
Cdd:pfam07724   7 LFLGPTGVGkteLAKALAELLFGD---------ERALIRIDMSEYM--EE--HSVSRLIGAPPGYVGYEEGGqlteavrr 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 278 ----IIFIDEIDKIAKnggasssadvsreGVQRDILPIVEGSTVVTKYGS-VKTDHVLFIAAGAFHMAKPSD-------- 344
Cdd:pfam07724  74 kpysIVLIDEIEKAHP-------------GVQNDLLQILEGGTLTDKQGRtVDFKNTLFIMTGNFGSEKISDasrlgdsp 140

                         170       180
                  ....*....|....*....|....*...
gi 2281921883 345 ----------------LIPELQGRFPIR 356
Cdd:pfam07724 141 dyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 362-438 1.55e-15

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: 71.71  E-value: 1.55e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2281921883  362 LTVDDFVRILVEPDNALLKQYQallqTEGISLEFSDEAIHKIAEVAYHVnqdtdNIGARRLHTILERLLEDLSFEAP 438
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDP-----KYGARPLRRIIQRELEDPLAELI 68
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 28-112 1.83e-12

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: 65.00  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  28 AKKAVAVALRNRYRRSLLDEKlkDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTE--VGYVGRDVESMV 105
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRY--GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78


                  ....*..
gi 2281921883 106 RDLVETS 112
Cdd:cd19481    79 ERARRLA 85
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 12-103 5.02e-09

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 55.65  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  12 RQIVDRLDQYIVGQQNAKKAVAVALRnRYRRSLLDEKLKDEVvpknILMMGPTGVGKTEIARRIAKL---SGAPFIKIEA 88
Cdd:cd19499     3 LNLEERLHERVVGQDEAVKAVSDAIR-RARAGLSDPNRPIGS----FLFLGPTGVGKTELAKALAELlfgDEDNLIRIDM 77

                          90
                  ....*....|....*
gi 2281921883  89 TKFTEVGYVGRDVES 103
Cdd:cd19499    78 SEYMEKHSVSRLIGA 92
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 23-103 7.44e-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: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  23 VGQQNAKKAVAVALRNRYrrslldeklkdevvPKNILMMGPTGVGKTEIARRIAKLS---GAPFIKIEATKFTEVGYVGR 99
Cdd:cd00009     1 VGQEEAIEALREALELPP--------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66


                  ....
gi 2281921883 100 DVES 103
Cdd:cd00009    67 LFGH 70
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 267-359 7.89e-09

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: 54.60  E-value: 7.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 267 QEAVQRAEES--GIIFIDEIDKIAKNGGASSSADVSREGVQRDILPIVEGSTvvtkygsvkTDHVLFIAAGAFhmakPSD 344
Cdd:cd19481    75 RKIFERARRLapCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNS---------RSKVLVIAATNR----PDL 141

                          90
                  ....*....|....*..
gi 2281921883 345 LIPELQ--GRFPIRVEL 359
Cdd:cd19481   142 LDPALLrpGRFDEVIEF 158
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 54-111 1.07e-07

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 51.46  E-value: 1.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2281921883  54 VPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEVgYVGRDVeSMVRDLVET 111
Cdd:cd19501    36 IPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFEQ 91
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 267-359 1.12e-07

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 50.67  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 267 QEAVQRAEESG--IIFIDEIDKIAKNGGASSSADVSRegVQRDILPIVEGSTvvtkygsVKTDHVLFIAAGafhmAKPSD 344
Cdd:pfam00004  47 RELFEAAKKLApcVIFIDEIDALAGSRGSGGDSESRR--VVNQLLTELDGFT-------SSNSKVIVIAAT----NRPDK 113

                          90
                  ....*....|....*
gi 2281921883 345 LIPELQGRFPIRVEL 359
Cdd:pfam00004 114 LDPALLGRFDRIIEF 128
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 22-133 1.70e-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: 49.91  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  22 IVGQQNAKKAV--AVALRNRYRRSLLDEKLKdevVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGr 99
Cdd:COG0464   159 LGGLEEVKEELreLVALPLKRPELREEYGLP---PPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG- 233

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2281921883 100 dvesmvrdlvETsvrlikEEKMNEVKEQAEENAN 133
Cdd:COG0464   234 ----------ET------EKNLREVFDKARGLAP 251
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 55-136 3.13e-06

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: 47.68  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGRDvESMVRDLVET------SVRLIKE-EKMNEVKEQ 127
Cdd:cd19525    55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVGEG-EKMVRALFSVarckqpAVIFIDEiDSLLSQRGE 132


                  ....*....
gi 2281921883 128 AEENANKRI 136
Cdd:cd19525   133 GEHESSRRI 141
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 55-137 3.27e-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: 47.01  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFteVGYVGRDVESMVRDLVETSVRL------IKE-EKMNEVKEQ 127
Cdd:cd19518    34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAISNapcivfIDEiDAITPKRES 111

                          90
                  ....*....|
gi 2281921883 128 AEENANKRIV 137
Cdd:cd19518   112 AQREMERRIV 121
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 10-89 3.92e-06

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: 48.63  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  10 TPRQIVDRLDQYIVGQQNAKKAVAVALRNRyrrslldeklkdevvpKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEAT 89
Cdd:COG0714     2 TEARLRAEIGKVYVGQEELIELVLIALLAG----------------GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT 65
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 58-110 5.98e-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: 45.66  E-value: 5.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2281921883  58 ILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGrDVESMVRDLVE 110
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFE 51
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 22-111 8.37e-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: 45.81  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  22 IVGQQNAKKAvavalrnryrrslldekLKDEVV---------------PKNILMMGPTGVGKTEIARRIAKLSGAPFIKI 86
Cdd:cd19509     1 IAGLDDAKEA-----------------LKEAVIlpslrpdlfpglrgpPRGILLYGPPGTGKTLLARAVASESGSTFFSI 63

                          90       100
                  ....*....|....*....|....*
gi 2281921883  87 EATKFTeVGYVGrDVESMVRDLVET 111
Cdd:cd19509    64 SASSLV-SKWVG-ESEKIVRALFAL 86
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
54-112 9.00e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 48.11  E-value: 9.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2281921883  54 VPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEVgYVGRDVeSMVRDLVETS 112
Cdd:PRK10733  184 IPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGA-SRVRDMFEQA 240
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 362-432 1.38e-05

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, pfam00004) 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 oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.


Pssm-ID: 463090 [Multi-domain]  Cd Length: 81  Bit Score: 43.16  E-value: 1.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2281921883 362 LTVDDFVRILvepDNALLKQYQALLQtEGISLEFSDEAIHKIAEVAYHVnqdtdNIGARRLHTILERLLED 432
Cdd:pfam10431   1 LSKEELRKIV---DLQLKELQKRLAE-RGITLELTDAAKDWLAEKGYDP-----EYGARPLRRAIQREIED 62
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 55-110 1.77e-05

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 46.54  E-value: 1.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGrDVESMVRDLVE 110
Cdd:COG1222   112 PKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS-KYIG-EGARNVREVFE 165
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 16-76 1.98e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 47.00  E-value: 1.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2281921883  16 DRLDQYIVGQQNAKKAVAVALRnRYRRSLLDEKlkdevvpKNI---LMMGPTGVGKTEIARRIA 76
Cdd:COG0542   545 EELHERVIGQDEAVEAVADAIR-RSRAGLKDPN-------RPIgsfLFLGPTGVGKTELAKALA 600
ftsH CHL00176
cell division protein; Validated
 54-111 2.88e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 46.58  E-value: 2.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  54 VPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTE--VGyVGrdvESMVRDLVET 111
Cdd:CHL00176  215 IPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG-VG---AARVRDLFKK 270
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 55-96 5.92e-05

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: 43.57  E-value: 5.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEVGY 96
Cdd:cd19520    35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY 76
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 55-110 8.03e-05

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: 43.05  E-value: 8.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGrDVESMVRDLVE 110
Cdd:cd19503    34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVS-KYLG-ESEKNLREIFE 87
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 55-110 8.61e-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: 8.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGrDVESMVRDLVE 110
Cdd:cd19502    37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVRELFE 90
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 55-134 8.66e-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: 8.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883   55 PKNILMMGPTGVGKTEIARRIAKL---SGAPFIKIEATKFTEVGYVGRDVESMVRDLVETSvrliKEEKMNEVKEQAEEN 131
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----GELRLRLALALARKL 77


                   ...
gi 2281921883  132 ANK 134
Cdd:smart00382  78 KPD 80
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 55-108 9.65e-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: 42.66  E-value: 9.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIkieATKFTEV--GYVGrDVESMVRDL 108
Cdd:cd19511    27 PKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREI 78
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 22-167 1.51e-04

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 42.14  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  22 IVGQQNAKKAVAVALRNRYRRSLLDEKLKDEvvPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGrDV 101
Cdd:cd19524     2 IAGQDLAKQALQEMVILPSLRPELFTGLRAP--ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2281921883 102 ESMVRDL------VETSVRLIKE-EKMNEVKEQAEENANKRIvrllvpgkkkqsgvKNPFEMFFGGSQPNGED 167
Cdd:cd19524    78 EKLVRALfavareLQPSIIFIDEvDSLLSERSEGEHEASRRL--------------KTEFLIEFDGVQSNGDD 136
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
54-111 1.54e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 44.26  E-value: 1.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  54 VPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTE--VGyVGrdvESMVRDLVET 111
Cdd:COG0465   174 IPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVG-VG---ASRVRDLFEQ 229
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 55-132 2.44e-04

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: 41.65  E-value: 2.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATkftevgyvgrdvESMVRDLVETsvrlikEEKMNEVKEQAEENA 132
Cdd:cd19519    34 PRGILLYGPPGTGKTLIARAVANETGAFFFLINGP------------EIMSKLAGES------ESNLRKAFEEAEKNA 93
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 267-460 3.24e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.76  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 267 QEAVQRAEESG------IIFIDEIDKIAKNggasssadvsregvQRDI-LPIVEgstvvtkygsvkTDHVLFIAAGAfhm 339
Cdd:PRK13342   78 REVIEEARQRRsagrrtILFIDEIHRFNKA--------------QQDAlLPHVE------------DGTITLIGATT--- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 340 AKPS-DLIPELQGRfpIRV-ELNKLTVDDFVRILVepdnallkqyQALLQTEGISLEFSDEAIHKIAEVAyhvnqDTDni 417
Cdd:PRK13342  129 ENPSfEVNPALLSR--AQVfELKPLSEEDIEQLLK----------RALEDKERGLVELDDEALDALARLA-----NGD-- 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2281921883 418 gARRLHTILErLLEDLsfeapdvtmeKITITPQYVEEKLGTIA 460
Cdd:PRK13342  190 -ARRALNLLE-LAALG----------VDSITLELLEEALQKRA 220
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 268-371 6.51e-04

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 41.82  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 268 EAVQRAEES--GIIFIDEIDKIAKNGGASSSaDVSREGVQRdILPIVEGstvvtkygsvKTDHVLFIAAGAFhmakPSDL 345
Cdd:COG0464   241 EVFDKARGLapCVLFIDEADALAGKRGEVGD-GVGRRVVNT-LLTEMEE----------LRSDVVVIAATNR----PDLL 304

                          90       100
                  ....*....|....*....|....*.
gi 2281921883 346 IPELQGRFPIRVELNKLTVDDFVRIL 371
Cdd:COG0464   305 DPALLRRFDEIIFFPLPDAEERLEIF 330
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 22-75 6.74e-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: 40.98  E-value: 6.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2281921883  22 IVGQQNAKKAVAVALRNRYrrslldeklkdevvpkNILMMGPTGVGKTEIARRI 75
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGGH----------------NLLMIGPPGSGKTMLAKRL 42
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 58-84 7.31e-04

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 39.93  E-value: 7.31e-04
                          10        20
                  ....*....|....*....|....*..
gi 2281921883  58 ILMMGPTGVGKTEIARRIAKLSGAPFI 84
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFI 28
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 57-93 7.63e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.58  E-value: 7.63e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2281921883  57 NILMMGPTGVGKTEIARRIAK-LSGAPFIKIEATKFTE 93
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 56-110 9.98e-04

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 39.97  E-value: 9.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2281921883  56 KNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGrDVESMVRDLVE 110
Cdd:cd19522    34 KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTS-KYRG-ESEKLVRLLFE 86
Sigma54_activat pfam00158
Sigma-54 interaction domain;
55-86 1.08e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.69  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLS---GAPFIKI 86
Cdd:pfam00158  22 DAPVLITGESGTGKELFARAIHQLSpraDGPFVAV 56
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 55-132 1.32e-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: 41.43  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGRdvesmvrdlvetsvrliKEEKMNEVKEQAEENA 132
Cdd:TIGR01243 212 PKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMS-KYYGE-----------------SEERLREIFKEAEENA 271
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 55-86 1.32e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 39.40  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKI 86
Cdd:cd19529    27 PKGILLYGPPGTGKTLLAKAVATESNANFISV 58
clpC CHL00095
Clp protease ATP binding subunit
 13-98 1.74e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 40.81  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  13 QIVDRLDQYIVGQQNAKKAVAVALRnRYRRSLldeklkdevvpKNI-------LMMGPTGVGKTEIARRIAKL---SGAP 82
Cdd:CHL00095  502 HMEETLHKRIIGQDEAVVAVSKAIR-RARVGL-----------KNPnrpiasfLFSGPTGVGKTELTKALASYffgSEDA 569

                          90       100
                  ....*....|....*....|....*..
gi 2281921883  83 FIKIEATKFTE-----------VGYVG 98
Cdd:CHL00095  570 MIRLDMSEYMEkhtvskligspPGYVG 596
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 48-86 1.88e-03

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon 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: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 39.08  E-value: 1.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2281921883  48 KLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKI 86
Cdd:cd19500    30 KLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRI 68
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 54-110 2.11e-03

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 38.95  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2281921883  54 VPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGRDvESMVRDLVE 110
Cdd:cd19526    26 LRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLN-KYIGAS-EQNVRDLFS 80
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 62-89 2.15e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 40.45  E-value: 2.15e-03
                          10        20
                  ....*....|....*....|....*...
gi 2281921883  62 GPTGVGKTEIARRIAKLSGAPFIKIEAT 89
Cdd:PRK13342   43 GPPGTGKTTLARIIAGATDAPFEALSAV 70
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
16-101 2.49e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 40.60  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  16 DRLDQYIVGQQNAKKAVAVALRnRYRRSLLDEKLKdevvPKNILMMGPTGVGKTEIARRIAKL---SGAPFIKIEATKFT 92
Cdd:PRK10865  564 QELHHRVIGQNEAVEAVSNAIR-RSRAGLSDPNRP----IGSFLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEFM 638


                  ....*....
gi 2281921883  93 EVGYVGRDV 101
Cdd:PRK10865  639 EKHSVSRLV 647
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 22-75 2.92e-03

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: 40.02  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2281921883  22 IVGQQNAKKA--VAVALRNryrrslldeklkdevvpkNILMMGPTGVGKTEIARRI 75
Cdd:COG0606   194 VKGQEQAKRAleIAAAGGH------------------NLLMIGPPGSGKTMLARRL 231
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 378-432 3.18e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2281921883 378 LLKQYQALLQTEGISLEFSDEAIHKIAEVAYhvnqDTDNiGARRLHTILERLLED 432
Cdd:COG0542   760 QLKRLRKRLAERGITLELTDAAKDFLAEKGY----DPEY-GARPLKRAIQRELED 809
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 53-108 3.53e-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: 3.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2281921883  53 VVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEVgYVGrDVESMVRDL 108
Cdd:cd19530    28 DLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNK-YVG-ESERAVRQV 81
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 12-109 3.69e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.82  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883  12 RQIVDRLDQYIVGQQNAKKAVAVALRnryrrsLLDEKLKDEVVP-KNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATK 90
Cdd:PRK11034  450 KNLGDRLKMLVFGQDKAIEALTEAIK------MSRAGLGHEHKPvGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSE 523

                          90       100       110
                  ....*....|....*....|....*....|
gi 2281921883  91 FTE-----------VGYVGRDVESMVRDLV 109
Cdd:PRK11034  524 YMErhtvsrligapPGYVGFDQGGLLTDAV 553
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 254-361 3.92e-03

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: 37.90  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281921883 254 EEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIaknggasssadvsREGVQRDILPIVEgstvVTKYGSVKTDHVLFIA 333
Cdd:cd00009    63 VVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL-------------SRGAQNALLRVLE----TLNDLRIDRENVRVIG 125

                          90       100
                  ....*....|....*....|....*...
gi 2281921883 334 AGAFHMakPSDLIPELQGRFPIRVELNK 361
Cdd:cd00009   126 ATNRPL--LGDLDRALYDRLDIRIVIPL 151
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 57-116 4.14e-03

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


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 37.92  E-value: 4.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2281921883  57 NILMMGPTGVGKTEIARRIAKLSGAPFI----KIEAT-------KFTEVGYVG-RDVESMVRDLVETSVRLI 116
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFVdldeLIEQRagmsipeIFAEEGEEGfRELEREVLLLLLTKENAV 72
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
58-84 4.20e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 4.20e-03
                          10        20
                  ....*....|....*....|....*..
gi 2281921883  58 ILMMGPTGVGKTEIARRIAKLSGAPFI 84
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRL 28
aroK PRK00131
shikimate kinase; Reviewed
 55-108 6.78e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.48  E-value: 6.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFI----KIEATK-------FTEVGYVG-RDVES-MVRDL 108
Cdd:PRK00131    4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFIdtdhLIEARAgksipeiFEEEGEAAfRELEEeVLAEL 70
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 55-118 7.58e-03

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 38.59  E-value: 7.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2281921883  55 PKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEvGYVGRDvESMVRDLvetsVRLIKE 118
Cdd:PTZ00454  179 PRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ-KYLGEG-PRMVRDV----FRLARE 236
 
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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