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Conserved domains on  [gi|1493997673|gb|RLQ12627|]
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HslU--HslV peptidase ATPase subunit [Geobacillus stearothermophilus]

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

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, ...
 3-464 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: 857.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   3 ESLTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:COG1220     2 SELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQTIKNPLEllfggqgnPSDN 162
Cdd:COG1220    82 EATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPF--------EEEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 SYGHEDEQIEQKRRQVAWQLANGQLENEMVTIEIEEQTPMLFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEAR 242
Cdd:COG1220   154 EEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEAR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 KVLINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDH 322
Cdd:COG1220   234 KILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSG-PDVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 323 ILFIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAF 402
Cdd:COG1220   313 ILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAF 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 403 EVNQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:COG1220   393 EVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
 
Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 3-464 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: 857.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   3 ESLTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:COG1220     2 SELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQTIKNPLEllfggqgnPSDN 162
Cdd:COG1220    82 EATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPF--------EEEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 SYGHEDEQIEQKRRQVAWQLANGQLENEMVTIEIEEQTPMLFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEAR 242
Cdd:COG1220   154 EEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEAR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 KVLINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDH 322
Cdd:COG1220   234 KILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSG-PDVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 323 ILFIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAF 402
Cdd:COG1220   313 ILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAF 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 403 EVNQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:COG1220   393 EVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
3-464 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 827.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   3 ESLTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:PRK05201    2 SELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQtiknplellfggqgnpsdN 162
Cdd:PRK05201   82 EATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNN------------------W 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 SYGHEDEQIEQKRRQVAWQLANGQLENEMVTIEIEEQTPMlFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEAR 242
Cdd:PRK05201  144 GEEEEKEEISATRQKFRKKLREGELDDKEIEIEVAEAAPM-MEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEAR 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 KVLINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDH 322
Cdd:PRK05201  223 KILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGGSSG-PDVSREGVQRDLLPLVEGSTVSTKYGMVKTDH 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 323 ILFIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAF 402
Cdd:PRK05201  302 ILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAY 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 403 EVNQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:PRK05201  382 QVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 5-464 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: 637.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   5 LTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEA 84
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  85 TKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQtiknplellFGGQGNPSdnsy 164
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQ---------WGQTEQQQ---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 165 ghEDEQIEQKRRQvawQLANGQLENEMVTIEIEEQTPMLFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEARKV 244
Cdd:TIGR00390 148 --EPESAREAFRK---KLREGELDDKEIEIDVSAKMPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 245 LINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDHIL 324
Cdd:TIGR00390 223 LIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKGESSG-ADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHIL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 325 FIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAFEV 404
Cdd:TIGR00390 302 FIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNV 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 405 NQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:TIGR00390 382 NEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 6-353 8.95e-104

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: 306.61  E-value: 8.95e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   6 TPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEAT 85
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  86 KFTEVGYVGRDVESMVRDLVEtsvrivkerkmnevkdraeqqankrlvellvpgkqkqtiknplellfggqgnpsdnsyg 165
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 166 hedeqieqkrrqvawqlangqlenemvtieieeqtpmlfdflqgtgieqmgvnmqdalsslmprrrkkrrlkvsearkvl 245
Cdd:cd19498       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 246 ineeaqklidmdevtqeavrlaeqsGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDHILF 325
Cdd:cd19498   102 -------------------------GIVFIDEIDKIAKRGGSSG-PDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILF 155

                         330       340
                  ....*....|....*....|....*...
gi 1493997673 326 IAAGAFHMAKPSDLIPELQGRFPIRVEL 353
Cdd:cd19498   156 IAAGAFHVAKPSDLIPELQGRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 236-350 9.06e-26

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 103.04  E-value: 9.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 236 LKVSEARKVLIneeaQKLIDMDEVTQEAVRLAEQSG------------IIFIDEIDKIARsgavsgsadvsreGVQRDIL 303
Cdd:pfam07724  34 LIRIDMSEYME----EHSVSRLIGAPPGYVGYEEGGqlteavrrkpysIVLIDEIEKAHP-------------GVQNDLL 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 304 PIVEGSTVMTKYG-PVKTDHILFIAAGAFHMAKPSD------------------------LIPELQGRFPIR 350
Cdd:pfam07724  97 QILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 356-442 2.09e-16

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: 74.02  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  356 LSVDDFVSILVEPNNALIKQYqallATEGISLEFSDDAIRKIAEVAFEVnqttdNIGARRLHTILEKLLEDLLFEAPDIG 435
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDP-----KYGARPLRRIIQRELEDPLAELILSG 71

                           90
                   ....*....|.
gi 1493997673  436 L----DKVVIT 442
Cdd:smart01086  72 ElkdgDTVVVD 82
 
Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 3-464 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: 857.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   3 ESLTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:COG1220     2 SELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQTIKNPLEllfggqgnPSDN 162
Cdd:COG1220    82 EATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPF--------EEEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 SYGHEDEQIEQKRRQVAWQLANGQLENEMVTIEIEEQTPMLFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEAR 242
Cdd:COG1220   154 EEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEAR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 KVLINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDH 322
Cdd:COG1220   234 KILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSG-PDVSREGVQRDLLPIVEGSTVNTKYGMVKTDH 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 323 ILFIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAF 402
Cdd:COG1220   313 ILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAF 392

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 403 EVNQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:COG1220   393 EVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
3-464 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 827.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   3 ESLTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:PRK05201    2 SELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQtiknplellfggqgnpsdN 162
Cdd:PRK05201   82 EATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNN------------------W 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 SYGHEDEQIEQKRRQVAWQLANGQLENEMVTIEIEEQTPMlFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEAR 242
Cdd:PRK05201  144 GEEEEKEEISATRQKFRKKLREGELDDKEIEIEVAEAAPM-MEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEAR 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 KVLINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDH 322
Cdd:PRK05201  223 KILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGGSSG-PDVSREGVQRDLLPLVEGSTVSTKYGMVKTDH 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 323 ILFIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAF 402
Cdd:PRK05201  302 ILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAY 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 403 EVNQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:PRK05201  382 QVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 5-464 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: 637.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   5 LTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEA 84
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  85 TKFTEVGYVGRDVESMVRDLVETSVRIVKERKMNEVKDRAEQQANKRLVELLVPGKQKQtiknplellFGGQGNPSdnsy 164
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQ---------WGQTEQQQ---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 165 ghEDEQIEQKRRQvawQLANGQLENEMVTIEIEEQTPMLFDFLQGTGIEQMGVNMQDALSSLMPRRRKKRRLKVSEARKV 244
Cdd:TIGR00390 148 --EPESAREAFRK---KLREGELDDKEIEIDVSAKMPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 245 LINEEAQKLIDMDEVTQEAVRLAEQSGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDHIL 324
Cdd:TIGR00390 223 LIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKGESSG-ADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHIL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 325 FIAAGAFHMAKPSDLIPELQGRFPIRVELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAFEV 404
Cdd:TIGR00390 302 FIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNV 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 405 NQTTDNIGARRLHTILEKLLEDLLFEAPDIGLDKVVITPQYVEQKLGSIVKNKDLSEFIL 464
Cdd:TIGR00390 382 NEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 6-353 8.95e-104

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: 306.61  E-value: 8.95e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   6 TPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEAT 85
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  86 KFTEVGYVGRDVESMVRDLVEtsvrivkerkmnevkdraeqqankrlvellvpgkqkqtiknplellfggqgnpsdnsyg 165
Cdd:cd19498    81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 166 hedeqieqkrrqvawqlangqlenemvtieieeqtpmlfdflqgtgieqmgvnmqdalsslmprrrkkrrlkvsearkvl 245
Cdd:cd19498       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 246 ineeaqklidmdevtqeavrlaeqsGIIFIDEIDKIARSGAVSGsADVSREGVQRDILPIVEGSTVMTKYGPVKTDHILF 325
Cdd:cd19498   102 -------------------------GIVFIDEIDKIAKRGGSSG-PDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILF 155

                         330       340
                  ....*....|....*....|....*...
gi 1493997673 326 IAAGAFHMAKPSDLIPELQGRFPIRVEL 353
Cdd:cd19498   156 IAAGAFHVAKPSDLIPELQGRFPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
5-454 8.95e-72

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 232.74  E-value: 8.95e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   5 LTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEV-MPK-NILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:PRK05342   60 PTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVeLQKsNILLIGPTGSGKTLLAQTLARILDVPFAIA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMVrdlvetsvrivkerkmnevkdraeqqankrlvellvpgkqkqtiknpLELLfggqgnpsdn 162
Cdd:PRK05342  140 DATTLTEAGYVGEDVENIL-----------------------------------------------LKLL---------- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 syghedeqieqkrrqvawQLANGQLEnemvtieieeqtpmlfdflqgtgieqmgvnmqdalsslmprrrkkrrlkvsear 242
Cdd:PRK05342  163 ------------------QAADYDVE------------------------------------------------------ 170

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 kvlineEAQKlidmdevtqeavrlaeqsGIIFIDEIDKIAR-SGAVSGSADVSREGVQRDILPIVEGSTV---------- 311
Cdd:PRK05342  171 ------KAQR------------------GIVYIDEIDKIARkSENPSITRDVSGEGVQQALLKILEGTVAsvppqggrkh 226

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 312 -MTKYGPVKTDHILFIAAGAF-----------------------------------HMAKPSDL-----IPELQGRFPIR 350
Cdd:PRK05342  227 pQQEFIQVDTTNILFICGGAFdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLPVV 306

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 351 VELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAFEvnqttDNIGARRLHTILEKLLEDLLFE 430
Cdd:PRK05342  307 ATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMFE 381

                         490       500
                  ....*....|....*....|....*
gi 1493997673 431 APDI-GLDKVVITPQYVEQKLGSIV 454
Cdd:PRK05342  382 LPSReDVEKVVITKEVVEGKAKPLL 406
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-457 1.82e-71

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 231.86  E-value: 1.82e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   5 LTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRDEV-MPK-NILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:COG1219    61 PKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVeLEKsNILLIGPTGSGKTLLAQTLARILDVPFAIA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  83 EATKFTEVGYVGRDVESMvrdlvetsvrivkerkmnevkdraeqqankrLVELLvpgkqkqtiknplellfggqgnpsdn 162
Cdd:COG1219   141 DATTLTEAGYVGEDVENI-------------------------------LLKLL-------------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 163 syghedeqieqkrrQVAwqlangqlenemvtieieeqtpmlfdflqgtgieqmgvnmqdalsslmprrrkkrrlkvsear 242
Cdd:COG1219   164 --------------QAA--------------------------------------------------------------- 166

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 243 kvlineeaqkliDMDevtqeaVRLAEQsGIIFIDEIDKIAR-SGAVSGSADVSREGVQRDILPIVEGSTV---------- 311
Cdd:COG1219   167 ------------DYD------VEKAER-GIIYIDEIDKIARkSENPSITRDVSGEGVQQALLKILEGTVAnvppqggrkh 227

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 312 -MTKYGPVKTDHILFIAAGAF----------------------------------HMAKPSDL-----IPELQGRFPIRV 351
Cdd:COG1219   228 pQQEFIQIDTTNILFICGGAFdglekiierrlgkksigfgaevkskkekdegellKQVEPEDLikfglIPEFIGRLPVIA 307

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 352 ELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAFEvnqttDNIGARRLHTILEKLLEDLLFEA 431
Cdd:COG1219   308 TLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMYEL 382

                         490       500
                  ....*....|....*....|....*..
gi 1493997673 432 PDI-GLDKVVITPQYVEQKLGSIVKNK 457
Cdd:COG1219   383 PSRkDVKKVVITKEVVEGKAKPILVYK 409
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 6-447 4.10e-45

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: 162.24  E-value: 4.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   6 TPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRsLLDEKLRD-----EVMPKNILMIGPTGVGKTEIARRLAKLVGAPFI 80
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKR-LNFEKNKKsdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  81 KVEATKFTEVGYVGRDVESMVRDLVetsvrivkerkmnevkdraeqqankrlvellvpgkqkqtiknplellfggqgnps 160
Cdd:TIGR00382 146 IADATTLTEAGYVGEDVENILLKLL------------------------------------------------------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 161 dnsyghedeqieqkrrqvawQLANGQLEnemvtieieeqtpmlfdflqgtgieqmgvnmqdalsslmprrrkkrrlkvse 240
Cdd:TIGR00382 171 --------------------QAADYDVE---------------------------------------------------- 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 241 arkvlineEAQKlidmdevtqeavrlaeqsGIIFIDEIDKIAR-SGAVSGSADVSREGVQRDILPIVEGS--TVMTKYG- 316
Cdd:TIGR00382 179 --------KAQK------------------GIIYIDEIDKISRkSENPSITRDVSGEGVQQALLKIIEGTvaNVPPQGGr 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 317 --------PVKTDHILFIAAGAF---------------------------------HMAKPSDL-----IPELQGRFPIR 350
Cdd:TIGR00382 233 khpyqefiQIDTSNILFICGGAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDLvkfglIPEFIGRLPVI 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 351 VELAKLSVDDFVSILVEPNNALIKQYQALLATEGISLEFSDDAIRKIAEVAFEvnqttDNIGARRLHTILEKLLEDLLFE 430
Cdd:TIGR00382 313 ATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFD 387

                         490
                  ....*....|....*...
gi 1493997673 431 APDI-GLDKVVITPQYVE 447
Cdd:TIGR00382 388 LPSLeDLEKVVITKETVL 405
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 5-353 3.39e-33

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: 125.79  E-value: 3.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   5 LTPRQIVEKLDQFIVGQKEAKKAVAIALRNRYRRSLLDEKLRD---EVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIK 81
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  82 VEATKFTEVGYVGRDVESMvrdlvetsvrivkerkmnevkdraeqqankrLVELLvpgkqkqtiknplellfggqgnpsd 161
Cdd:cd19497    81 ADATTLTEAGYVGEDVENI-------------------------------LLKLL------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 162 nsyghedeqieqkrrqvawQLANGQLENemvtieieeqtpmlfdflqgtgieqmgvnmqdalsslmprrrkkrrlkvsea 241
Cdd:cd19497   105 -------------------QAADYDVER---------------------------------------------------- 113

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 242 rkvlineeAQKlidmdevtqeavrlaeqsGIIFIDEIDKIAR-SGAVSGSADVSREGVQRDILPIVEGSTV--------M 312
Cdd:cd19497   114 --------AQR------------------GIVYIDEIDKIARkSENPSITRDVSGEGVQQALLKILEGTVAnvppqggrK 167

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 313 TKYG---PVKTDHILFIAAGAF-----------------------------------HMAKPSDL-----IPELQGRFPI 349
Cdd:cd19497   168 HPQQefiQVDTTNILFICGGAFvglekiiarrlgkkslgfgaetssekdekerdellSKVEPEDLikfglIPEFVGRLPV 247


                  ....
gi 1493997673 350 RVEL 353
Cdd:cd19497   248 IVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 236-350 9.06e-26

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 103.04  E-value: 9.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 236 LKVSEARKVLIneeaQKLIDMDEVTQEAVRLAEQSG------------IIFIDEIDKIARsgavsgsadvsreGVQRDIL 303
Cdd:pfam07724  34 LIRIDMSEYME----EHSVSRLIGAPPGYVGYEEGGqlteavrrkpysIVLIDEIEKAHP-------------GVQNDLL 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673 304 PIVEGSTVMTKYG-PVKTDHILFIAAGAFHMAKPSD------------------------LIPELQGRFPIR 350
Cdd:pfam07724  97 QILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 356-442 2.09e-16

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: 74.02  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  356 LSVDDFVSILVEPNNALIKQYqallATEGISLEFSDDAIRKIAEVAFEVnqttdNIGARRLHTILEKLLEDLLFEAPDIG 435
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDP-----KYGARPLRRIIQRELEDPLAELILSG 71

                           90
                   ....*....|.
gi 1493997673  436 L----DKVVIT 442
Cdd:smart01086  72 ElkdgDTVVVD 82
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 24-108 1.15e-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: 65.77  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  24 AKKAVAIALRNRYRRSLLDEklRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTE--VGYVGRDVESMV 101
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRR--YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78


                  ....*..
gi 1493997673 102 RDLVETS 108
Cdd:cd19481    79 ERARRLA 85
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 8-99 4.83e-10

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: 58.34  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   8 RQIVEKLDQFIVGQKEAKKAVAIALRnRYRRSLLDEKLRDEVMpkniLMIGPTGVGKTEIARRLAKLV---GAPFIKVEA 84
Cdd:cd19499     3 LNLEERLHERVVGQDEAVKAVSDAIR-RARAGLSDPNRPIGSF----LFLGPTGVGKTELAKALAELLfgdEDNLIRIDM 77

                          90
                  ....*....|....*
gi 1493997673  85 TKFTEVGYVGRDVES 99
Cdd:cd19499    78 SEYMEKHSVSRLIGA 92
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 19-136 3.67e-08

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 52.53  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  19 VGQKEAKKAVAIALRNRYrrslldeklrdevmPKNILMIGPTGVGKTEIARRLAKLV---GAPFIKVEATKFTEVGYVGR 95
Cdd:cd00009     1 VGQEEAIEALREALELPP--------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1493997673  96 DVESMVRDLVEtsvRIVKERK-----MNEVkDRAEQQANKRLVELL 136
Cdd:cd00009    67 LFGHFLVRLLF---ELAEKAKpgvlfIDEI-DSLSRGAQNALLRVL 108
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 256-353 6.50e-08

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: 51.90  E-value: 6.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 256 MDEVTQEAVRLAeqSGIIFIDEIDKIARSGAVSGSADVSREGVQRDILPIVegstvmtkyGPVKTDHILFIAAGAFhmak 335
Cdd:cd19481    74 LRKIFERARRLA--PCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELD---------GVNSRSKVLVIAATNR---- 138

                          90       100
                  ....*....|....*....|
gi 1493997673 336 PSDLIPELQ--GRFPIRVEL 353
Cdd:cd19481   139 PDLLDPALLrpGRFDEVIEF 158
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 6-85 3.80e-07

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: 51.71  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   6 TPRQIVEKLDQFIVGQKEAKKAVAIALRNRyrrslldeklrdevmpKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEAT 85
Cdd:COG0714     2 TEARLRAEIGKVYVGQEELIELVLIALLAG----------------GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT 65
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 18-129 4.84e-07

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: 51.84  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  18 IVGQKEAKKAvaiaLRNRYRRSLLDEKLRDE---VMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVG 94
Cdd:COG0464   159 LGGLEEVKEE----LRELVALPLKRPELREEyglPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1493997673  95 rdvesmvrdlvETsvrivkERKMNEVKDRAEQQAN 129
Cdd:COG0464   234 -----------ET------EKNLREVFDKARGLAP 251
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 236-353 7.41e-07

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 47.97  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673 236 LKVSEARKVLINEEAQKLIDMDEVTQEavrlaEQSGIIFIDEIDKIARSGAVSGSADVSRegVQRDILPIVEGSTvmtky 315
Cdd:pfam00004  29 ISGSELVSKYVGESEKRLRELFEAAKK-----LAPCVIFIDEIDALAGSRGSGGDSESRR--VVNQLLTELDGFT----- 96

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1493997673 316 gpVKTDHILFIAAGafhmAKPSDLIPELQGRFPIRVEL 353
Cdd:pfam00004  97 --SSNSKVIVIAAT----NRPDKLDPALLGRFDRIIEF 128
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 18-107 7.45e-07

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 49.15  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  18 IVGQKEAKKAVAIA---LRN--RYRRslLDEKLrdevmPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEVgY 92
Cdd:cd19501     6 VAGCEEAKEELKEVvefLKNpeKFTK--LGAKI-----PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-F 77

                          90
                  ....*....|....*
gi 1493997673  93 VGRDVeSMVRDLVET 107
Cdd:cd19501    78 VGVGA-SRVRDLFEQ 91
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 14-106 2.24e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 49.23  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  14 LDQFIvgqKEAKKAVAIALRNRyrrslldEKLR--DEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvG 91
Cdd:COG1222    83 LDEQI---EEIREAVELPLKNP-------ELFRkyGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS-K 151

                          90
                  ....*....|....*
gi 1493997673  92 YVGrDVESMVRDLVE 106
Cdd:COG1222   152 YIG-EGARNVREVFE 165
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
2-135 3.73e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 49.26  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   2 AESLTPRQIVEKLDQfIVGQKEAKKAVAiALRNRYRRSLLDEKLRDEVmPKNILMIGPTGVGKTEIARRLAKLVGAPFIK 81
Cdd:PRK10733  139 ARMLTEDQIKTTFAD-VAGCDEAKEEVA-ELVEYLREPSRFQKLGGKI-PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFT 215

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1493997673  82 VEATKFTEVgYVGRDVeSMVRDLVETSVR----IVKERKMNEV-----------KDRAEQQANKRLVEL 135
Cdd:PRK10733  216 ISGSDFVEM-FVGVGA-SRVRDMFEQAKKaapcIIFIDEIDAVgrqrgaglgggHDEREQTLNQMLVEM 282
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 12-94 5.80e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.92  E-value: 5.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  12 EKLDQFIVGQKEAKKAVAIALRnRYRRSLLDEKlrdevmpKNI---LMIGPTGVGKTEIARRLA---------------- 72
Cdd:COG0542   545 EELHERVIGQDEAVEAVADAIR-RSRAGLKDPN-------RPIgsfLFLGPTGVGKTELAKALAeflfgdedaliridms 616

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1493997673  73 ---------KLVGAPfikveatkfteVGYVG 94
Cdd:COG0542   617 eymekhsvsRLIGAP-----------PGYVG 636
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 356-432 8.41e-06

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: 43.93  E-value: 8.41e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1493997673 356 LSVDDFVSILVEpnnaLIKQYQALLATEGISLEFSDDAIRKIAEVAFEVnqttdNIGARRLHTILEKLLEDLLFEAP 432
Cdd:pfam10431   1 LSKEELRKIVDL----QLKELQKRLAERGITLELTDAAKDWLAEKGYDP-----EYGARPLRRAIQREIEDPLAEEI 68
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 54-106 9.27e-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: 44.89  E-value: 9.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1493997673  54 ILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVGrDVESMVRDLVE 106
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFE 51
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 51-110 4.38e-05

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 43.93  E-value: 4.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFteVGYVGRDVESMVRDLVETSVR 110
Cdd:cd19518    34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAIS 91
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 16-71 4.47e-05

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 44.45  E-value: 4.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493997673  16 QFIVGQKEAKKAVAIALRNRYrrslldeklrdevmpkNILMIGPTGVGKTEIARRL 71
Cdd:pfam01078   3 ADVKGQEQAKRALEIAAAGGH----------------NLLMIGPPGSGKTMLAKRL 42
clpC CHL00095
Clp protease ATP binding subunit
 2-74 6.43e-05

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 45.43  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   2 AESLTPRQIVEKLDQFIVGQKEAKKAVAIALRnRYRRSLldeklrdevmpKNI-------LMIGPTGVGKTEIARRLAKL 74
Cdd:CHL00095  495 SESEKLLHMEETLHKRIIGQDEAVVAVSKAIR-RARVGL-----------KNPnrpiasfLFSGPTGVGKTELTKALASY 562
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 51-106 6.95e-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: 43.48  E-value: 6.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVGrDVESMVRDLVE 106
Cdd:cd19502    37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVRELFE 90
aroK PRK00131
shikimate kinase; Reviewed
 50-104 9.41e-05

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 42.87  E-value: 9.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1493997673  50 MPKNILMIGPTGVGKTEIARRLAKLVGAPFI----KVEATK-------FTEVGYVG-RDVES-MVRDL 104
Cdd:PRK00131    3 KGPNIVLIGFMGAGKSTIGRLLAKRLGYDFIdtdhLIEARAgksipeiFEEEGEAAfRELEEeVLAEL 70
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 53-89 1.02e-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: 42.28  E-value: 1.02e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1493997673  53 NILMIGPTGVGKTEIARRLAK-LVGAPFIKVEATKFTE 89
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 51-106 1.06e-04

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 42.66  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVGrDVESMVRDLVE 106
Cdd:cd19503    34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVS-KYLG-ESEKNLREIFE 87
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 51-104 1.52e-04

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 42.67  E-value: 1.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVGRDvESMVRDL 104
Cdd:cd19525    55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVGEG-EKMVRAL 106
ftsH CHL00176
cell division protein; Validated
 18-107 1.59e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 44.27  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  18 IVGQKEAKK---AVAIALRNRYRRSLLDEKLrdevmPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTE--VGy 92
Cdd:CHL00176  185 IAGIEEAKEefeEVVSFLKKPERFTAVGAKI-----PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG- 258

                          90
                  ....*....|....*
gi 1493997673  93 VGrdvESMVRDLVET 107
Cdd:CHL00176  259 VG---AARVRDLFKK 270
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 18-107 1.71e-04

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 41.95  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  18 IVGQKEAKKAVaialrnryRRSLLDEKLRDEVM------PKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTeVG 91
Cdd:cd19509     1 IAGLDDAKEAL--------KEAVILPSLRPDLFpglrgpPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SK 71

                          90
                  ....*....|....*.
gi 1493997673  92 YVGrDVESMVRDLVET 107
Cdd:cd19509    72 WVG-ESEKIVRALFAL 86
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 53-112 2.84e-04

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


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 41.39  E-value: 2.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673  53 NILMIGPTGVGKTEIARRLAKLVGAPFIKV-----EATK------FTEVGYVG-RDVESMVRDLVETSVRIV 112
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLdelieQRAGmsipeiFAEEGEEGfRELEREVLLLLLTKENAV 72
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 51-130 3.88e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.82  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   51 PKNILMIGPTGVGKTEIARRLAKLV---GAPFIKVEATKFTEVGYVGRDVESMVRDLVETSvrivKERKMNEVKDRAEQQ 127
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----GELRLRLALALARKL 77


                   ...
gi 1493997673  128 ANK 130
Cdd:smart00382  78 KPD 80
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 51-92 4.39e-04

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 40.87  E-value: 4.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEVGY 92
Cdd:cd19520    35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY 76
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 52-106 5.86e-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: 40.74  E-value: 5.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1493997673  52 KNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVGrDVESMVRDLVE 106
Cdd:cd19522    34 KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTS-KYRG-ESEKLVRLLFE 86
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 51-104 7.07e-04

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 39.96  E-value: 7.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIkveATKFTEV--GYVGrDVESMVRDL 104
Cdd:cd19511    27 PKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREI 78
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 18-71 7.59e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 41.95  E-value: 7.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1493997673  18 IVGQKEAKKAVAIAlrnryrrslldeklrdevmpkNILMIGPTGVGKTEIARRL 71
Cdd:COG0606   194 VKGQEQAKRALEIAaag----------------ghNLLMIGPPGSGKTMLARRL 231
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
54-80 1.24e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.51  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*..
gi 1493997673  54 ILMIGPTGVGKTEIARRLAKLVGAPFI 80
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRL 28
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
 36-84 1.35e-03

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 40.91  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1493997673  36 YRRSLLDEkLRDEVMPKNILMI-GPTGVGKTEIARRLAKLvGAPFIKVEA 84
Cdd:COG2603   126 YRRFVLDE-LERLPAPLPLIVLgGPTGSGKTRLLHALAAQ-GAQVLDLEG 173
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 54-80 1.43e-03

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 39.34  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....*..
gi 1493997673  54 ILMIGPTGVGKTEIARRLAKLVGAPFI 80
Cdd:COG0703     1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 372-428 1.53e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1493997673 372 LIKQYQALLATEGISLEFSDDAIRKIAEVAFEVNQttdniGARRLHTILEKLLEDLL 428
Cdd:COG0542   760 QLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEY-----GARPLKRAIQRELEDPL 811
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
12-97 2.60e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 40.21  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  12 EKLDQFIVGQKEAKKAVAIALRnRYRRSLLDEKlrdevMP-KNILMIGPTGVGKTEIARRLAKLV---GAPFIKVEATKF 87
Cdd:PRK10865  564 QELHHRVIGQNEAVEAVSNAIR-RSRAGLSDPN-----RPiGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRIDMSEF 637

                          90
                  ....*....|
gi 1493997673  88 TEVGYVGRDV 97
Cdd:PRK10865  638 MEKHSVSRLV 647
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
50-107 3.22e-03

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 40.02  E-value: 3.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  50 MPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTE--VGyVGrdvESMVRDLVET 107
Cdd:COG0465   174 IPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVG-VG---ASRVRDLFEQ 229
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 44-82 3.68e-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: 38.31  E-value: 3.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1493997673  44 KLRDEVMPKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:cd19500    30 KLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRI 68
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 55-105 3.72e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.82  E-value: 3.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493997673  55 LMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTE-----------VGYVGRDVESMVRDLV 105
Cdd:PRK11034  492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGLLTDAV 553
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 18-161 4.15e-03

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: 37.91  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673  18 IVGQKEAKKAVAIALRNRYRRSLLDEKLRDEvmPKNILMIGPTGVGKTEIARRLAKLVGAPFIKVEATKFTEvGYVGrDV 97
Cdd:cd19524     2 IAGQDLAKQALQEMVILPSLRPELFTGLRAP--ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493997673  98 ESMVRDL------VETSVRIVKE--RKMNEVKDrAEQQANKRL-VELLVPGKQKQTIKNPLELLFGGQGNPSD 161
Cdd:cd19524    78 EKLVRALfavareLQPSIIFIDEvdSLLSERSE-GEHEASRRLkTEFLIEFDGVQSNGDDRVLVMGATNRPQE 149
PRK13946 PRK13946
shikimate kinase; Provisional
 52-80 5.84e-03

shikimate kinase; Provisional


Pssm-ID: 184411 [Multi-domain]  Cd Length: 184  Bit Score: 37.98  E-value: 5.84e-03
                          10        20
                  ....*....|....*....|....*....
gi 1493997673  52 KNILMIGPTGVGKTEIARRLAKLVGAPFI 80
Cdd:PRK13946   11 RTVVLVGLMGAGKSTVGRRLATMLGLPFL 39
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 54-80 6.14e-03

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: 37.23  E-value: 6.14e-03
                          10        20
                  ....*....|....*....|....*..
gi 1493997673  54 ILMIGPTGVGKTEIARRLAKLVGAPFI 80
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFI 28
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 2-85 6.41e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.91  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493997673   2 AESLTPRqiveKLDQFiVGQK---EAKKAVAIALRNRYRRSlldeklrdevmpknilMI--GPTGVGKTEIARRLAKLVG 76
Cdd:PRK13342    3 AERMRPK----TLDEV-VGQEhllGPGKPLRRMIEAGRLSS----------------MIlwGPPGTGKTTLARIIAGATD 61


                  ....*....
gi 1493997673  77 APFIKVEAT 85
Cdd:PRK13342   62 APFEALSAV 70
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 51-82 7.86e-03

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 37.03  E-value: 7.86e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1493997673  51 PKNILMIGPTGVGKTEIARRLAKLVGAPFIKV 82
Cdd:cd19519    34 PRGILLYGPPGTGKTLIARAVANETGAFFFLI 65
PRK13947 PRK13947
shikimate kinase; Provisional
 52-84 9.98e-03

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 36.99  E-value: 9.98e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1493997673  52 KNILMIGPTGVGKTEIARRLAKLVGAPFIKVEA 84
Cdd:PRK13947    2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDK 34
 
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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