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Conserved domains on  [gi|491169658|ref|WP_005028027|]
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ATP-dependent Clp protease ATP-binding subunit ClpX [Bilophila wadsworthia]

Protein Classification

ATP-dependent Clp protease ATP-binding subunit ClpX( domain architecture ID 11440654)

ATP-dependent Clp protease ATP-binding subunit ClpX is an ATP-dependent specificity component of the Clp protease that uses cycles of ATP-binding and hydrolysis to unfold proteins and translocate them to the ClpP protease

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-411 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 807.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   1 MPNTTPpNEPRCSFCGKTETQANQLVSGPdGVHICDECIATCNEMMAQNAIEQVREDER--LLTPQEIKARLDEYVIGQD 78
Cdd:COG1219    1 MAGDSK-KELKCSFCGKSQDEVRKLIAGP-GVYICDECVELCNEIIEEELKEEEAEEELkkLPKPKEIKAFLDEYVIGQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  79 EAKKILAVAVHNHYKRVFYADalKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVE 158
Cdd:COG1219   79 RAKKVLSVAVYNHYKRLNSGS--KDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 159 NILVQLLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMD 238
Cdd:COG1219  157 NILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQID 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 239 TSNILFIVGGAFIGLDKIVEQRMRGGSMGFGAKVETKKERTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDD 318
Cdd:COG1219  237 TTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 319 LVRILTEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDA 398
Cdd:COG1219  317 LVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKE 396
                        410
                 ....*....|...
gi 491169658 399 VIEKKAPPLYIYD 411
Cdd:COG1219  397 VVEGKAKPILVYK 409
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-411 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 807.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   1 MPNTTPpNEPRCSFCGKTETQANQLVSGPdGVHICDECIATCNEMMAQNAIEQVREDER--LLTPQEIKARLDEYVIGQD 78
Cdd:COG1219    1 MAGDSK-KELKCSFCGKSQDEVRKLIAGP-GVYICDECVELCNEIIEEELKEEEAEEELkkLPKPKEIKAFLDEYVIGQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  79 EAKKILAVAVHNHYKRVFYADalKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVE 158
Cdd:COG1219   79 RAKKVLSVAVYNHYKRLNSGS--KDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 159 NILVQLLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMD 238
Cdd:COG1219  157 NILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQID 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 239 TSNILFIVGGAFIGLDKIVEQRMRGGSMGFGAKVETKKERTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDD 318
Cdd:COG1219  237 TTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 319 LVRILTEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDA 398
Cdd:COG1219  317 LVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKE 396
                        410
                 ....*....|...
gi 491169658 399 VIEKKAPPLYIYD 411
Cdd:COG1219  397 VVEGKAKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
8-414 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 775.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   8 NEPRCSFCGKTETQANQLVSGPdGVHICDECIATCNEMMAQNAIEQVREDERLLTPQEIKARLDEYVIGQDEAKKILAVA 87
Cdd:PRK05342   8 KLLYCSFCGKSQHEVRKLIAGP-GVYICDECIELCNEIIREELKEEAVELKELPTPKEIKAHLDQYVIGQERAKKVLSVA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  88 VHNHYKRVFYADalKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVENILVQLLQN 167
Cdd:PRK05342  87 VYNHYKRLRHGD--KKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 168 ADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMDTSNILFIVG 247
Cdd:PRK05342 165 ADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNILFICG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 248 GAFIGLDKIVEQRMRGGSMGFGAKVETKKE-RTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDDLVRILTEP 326
Cdd:PRK05342 245 GAFDGLEKIIKQRLGKKGIGFGAEVKSKKEkRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRILTEP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 327 KNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDAVIEKKAPP 406
Cdd:PRK05342 325 KNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEGKAKP 404

                 ....*...
gi 491169658 407 LYIYDTEA 414
Cdd:PRK05342 405 LLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
12-409 0e+00

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: 592.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   12 CSFCGKTETQANQLVSGPdGVHICDECIATCNEMM-----AQNAIEQVRED---ERLLTPQEIKARLDEYVIGQDEAKKI 83
Cdd:TIGR00382  10 CSFCGKSQDEVRKLIAGP-GVYICDECIELCHDILeeelgTRKESKEYEEEfelSYLPTPKEIKAHLDEYVIGQEQAKKV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   84 LAVAVHNHYKRVFYADALKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVENILVQ 163
Cdd:TIGR00382  89 LSVAVYNHYKRLNFEKNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  164 LLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMDTSNIL 243
Cdd:TIGR00382 169 LLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNIL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  244 FIVGGAFIGLDKIVEQRMRGGSMGFGAKVEtKKERTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDDLVRIL 323
Cdd:TIGR00382 249 FICGGAFVGLEKIIKKRTGKSSIGFGAEVK-KKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAIL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  324 TEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDAVIEKK 403
Cdd:TIGR00382 328 TKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQ 407

                  ....*.
gi 491169658  404 APPLYI 409
Cdd:TIGR00382 408 SEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
61-310 2.14e-162

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: 456.68  E-value: 2.14e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  61 LTPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVfYADALKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFA 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRI-RNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 141 IADATTLTEAGYVGEDVENILVQLLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEAN 220
Cdd:cd19497   80 IADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVAN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 221 IPPKGGRKHPQQEFIRMDTSNILFIVGGAFIGLDKIVEQRMRGGSMGFGAKVE-TKKERTLGELLEQVHPADLVQFGLIP 299
Cdd:cd19497  160 VPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSsEKDEKERDELLSKVEPEDLIKFGLIP 239
                        250
                 ....*....|.
gi 491169658 300 EFVGRIPVLTH 310
Cdd:cd19497  240 EFVGRLPVIVT 250
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
110-307 1.84e-35

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: 128.47  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  110 EKSNILLVGPSGSGKTLLAKTLARVLRV---PFAIADATTLTEagyvgedvENILVQLLQNADYDLEAARKG-------- 178
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  179 ----IIYIDEIDKISRkadgpsitrdvsgeGVQQALLKIIEGTEANipPKGGRKhpqqefirMDTSNILFIVGGAFiGLD 254
Cdd:pfam07724  74 kpysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT--DKQGRT--------VDFKNTLFIMTGNF-GSE 128
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491169658  255 KIVEQRMRGGSmgfgakvetkkertLGELLEQVHPADLVQFGLIPEFVGRIPV 307
Cdd:pfam07724 129 KISDASRLGDS--------------PDYELLKEEVMDLLKKGFIPEFLGRLPI 167
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
314-395 3.54e-20

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: 84.42  E-value: 3.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   314 LGEDDLVRILTEPKNALTRQYqklfELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPS---MPGV 390
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILsgeLKDG 76

                   ....*
gi 491169658   391 KECVI 395
Cdd:smart01086  77 DTVVV 81
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-411 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 807.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   1 MPNTTPpNEPRCSFCGKTETQANQLVSGPdGVHICDECIATCNEMMAQNAIEQVREDER--LLTPQEIKARLDEYVIGQD 78
Cdd:COG1219    1 MAGDSK-KELKCSFCGKSQDEVRKLIAGP-GVYICDECVELCNEIIEEELKEEEAEEELkkLPKPKEIKAFLDEYVIGQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  79 EAKKILAVAVHNHYKRVFYADalKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVE 158
Cdd:COG1219   79 RAKKVLSVAVYNHYKRLNSGS--KDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 159 NILVQLLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMD 238
Cdd:COG1219  157 NILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQID 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 239 TSNILFIVGGAFIGLDKIVEQRMRGGSMGFGAKVETKKERTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDD 318
Cdd:COG1219  237 TTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 319 LVRILTEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDA 398
Cdd:COG1219  317 LVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKE 396
                        410
                 ....*....|...
gi 491169658 399 VIEKKAPPLYIYD 411
Cdd:COG1219  397 VVEGKAKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
8-414 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 775.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   8 NEPRCSFCGKTETQANQLVSGPdGVHICDECIATCNEMMAQNAIEQVREDERLLTPQEIKARLDEYVIGQDEAKKILAVA 87
Cdd:PRK05342   8 KLLYCSFCGKSQHEVRKLIAGP-GVYICDECIELCNEIIREELKEEAVELKELPTPKEIKAHLDQYVIGQERAKKVLSVA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  88 VHNHYKRVFYADalKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVENILVQLLQN 167
Cdd:PRK05342  87 VYNHYKRLRHGD--KKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 168 ADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMDTSNILFIVG 247
Cdd:PRK05342 165 ADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNILFICG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 248 GAFIGLDKIVEQRMRGGSMGFGAKVETKKE-RTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDDLVRILTEP 326
Cdd:PRK05342 245 GAFDGLEKIIKQRLGKKGIGFGAEVKSKKEkRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRILTEP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 327 KNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDAVIEKKAPP 406
Cdd:PRK05342 325 KNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEGKAKP 404

                 ....*...
gi 491169658 407 LYIYDTEA 414
Cdd:PRK05342 405 LLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
12-409 0e+00

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: 592.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   12 CSFCGKTETQANQLVSGPdGVHICDECIATCNEMM-----AQNAIEQVRED---ERLLTPQEIKARLDEYVIGQDEAKKI 83
Cdd:TIGR00382  10 CSFCGKSQDEVRKLIAGP-GVYICDECIELCHDILeeelgTRKESKEYEEEfelSYLPTPKEIKAHLDEYVIGQEQAKKV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   84 LAVAVHNHYKRVFYADALKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYVGEDVENILVQ 163
Cdd:TIGR00382  89 LSVAVYNHYKRLNFEKNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  164 LLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEANIPPKGGRKHPQQEFIRMDTSNIL 243
Cdd:TIGR00382 169 LLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNIL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  244 FIVGGAFIGLDKIVEQRMRGGSMGFGAKVEtKKERTLGELLEQVHPADLVQFGLIPEFVGRIPVLTHVDDLGEDDLVRIL 323
Cdd:TIGR00382 249 FICGGAFVGLEKIIKKRTGKSSIGFGAEVK-KKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAIL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  324 TEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPSMPGVKECVINDAVIEKK 403
Cdd:TIGR00382 328 TKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQ 407

                  ....*.
gi 491169658  404 APPLYI 409
Cdd:TIGR00382 408 SEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
61-310 2.14e-162

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: 456.68  E-value: 2.14e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  61 LTPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVfYADALKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFA 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRI-RNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 141 IADATTLTEAGYVGEDVENILVQLLQNADYDLEAARKGIIYIDEIDKISRKADGPSITRDVSGEGVQQALLKIIEGTEAN 220
Cdd:cd19497   80 IADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVAN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 221 IPPKGGRKHPQQEFIRMDTSNILFIVGGAFIGLDKIVEQRMRGGSMGFGAKVE-TKKERTLGELLEQVHPADLVQFGLIP 299
Cdd:cd19497  160 VPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSsEKDEKERDELLSKVEPEDLIKFGLIP 239
                        250
                 ....*....|.
gi 491169658 300 EFVGRIPVLTH 310
Cdd:cd19497  240 EFVGRLPVIVT 250
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
61-403 1.33e-56

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 192.21  E-value: 1.33e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  61 LTPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVFYADALKgddgVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFA 140
Cdd:PRK05201   4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELR----DEVTPKNILMIGPTGVGKTEIARRLAKLANAPFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 141 IADATTLTEAGYVGEDVENI-------------------------------LVQLL----------QNADYDLEAARK-- 177
Cdd:PRK05201  80 KVEATKFTEVGYVGRDVESIirdlveiavkmvreekrekvrekaeeaaeerILDALlppaknnwgeEEEKEEISATRQkf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658     --------------------------------------------------------------------------------
Cdd:PRK05201 160 rkklregelddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaaklidmeei 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 178 -----------GIIYIDEIDKISRKAD--GPsitrDVSGEGVQQALLKIIEGTeaNIPPKGGRkhpqqefirMDTSNILF 244
Cdd:PRK05201 240 kqeaierveqnGIVFIDEIDKIAARGGssGP----DVSREGVQRDLLPLVEGS--TVSTKYGM---------VKTDHILF 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 245 IVGGAFigldkiveqrmrggsmgfgakvetkkertlgelleqvH---PADLvqfglIPEFVGRIPVLTHVDDLGEDDLVR 321
Cdd:PRK05201 305 IASGAF-------------------------------------HvskPSDL-----IPELQGRFPIRVELDALTEEDFVR 342
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 322 ILTEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIE--RKT---GARGLRNVMESVMLDIMYQLPSMPGvKECVIN 396
Cdd:PRK05201 343 ILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQvnEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVTID 421

                 ....*..
gi 491169658 397 DAVIEKK 403
Cdd:PRK05201 422 AAYVDEK 428
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
61-403 3.00e-54

ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 186.41  E-value: 3.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  61 LTPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVFYADALKGddgvELEKSNILLVGPSGSGKTLLAKTLARVLRVPFA 140
Cdd:COG1220    4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRD----EITPKNILMIGPTGVGKTEIARRLAKLANAPFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 141 IADATTLTEAGYVGEDVENI-------------------------------LVQLL--------------QNADYDLEA- 174
Cdd:COG1220   80 KVEATKFTEVGYVGRDVESMirdlveiavkmvreekmekvrekaeeaaeerILDLLlpppkkkagsnnpfEEEEEEEEEe 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 175 ------------------------------------------------------------------------ARK----- 177
Cdd:COG1220  160 eeisrtrekfrkklregelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkeARKiltqe 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 178 ----------------------GIIYIDEIDKISRKAD--GPsitrDVSGEGVQQALLKIIEGTeaNIPPKGGrkhpqqe 233
Cdd:COG1220  240 eaaklidmdevkqeaieraeqnGIIFIDEIDKIASRGGgsGP----DVSREGVQRDLLPIVEGS--TVNTKYG------- 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 234 firM-DTSNILFIVGGAFigldkiveqrmrggsmgfgakvetkkertlgelleqvH---PADlvqfgLIPEFVGRIPVLT 309
Cdd:COG1220  307 ---MvKTDHILFIAAGAF-------------------------------------HvskPSD-----LIPELQGRFPIRV 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 310 HVDDLGEDDLVRILTEPKNALTRQYQKLFELDNVTLRFTSDALRAIAHRAIE--RKT---GARGLRNVMESVMLDIMYQL 384
Cdd:COG1220  342 ELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEvnERTeniGARRLHTVMEKLLEDISFEA 421
                        490
                 ....*....|....*....
gi 491169658 385 PSMPGvKECVINDAVIEKK 403
Cdd:COG1220  422 PDLSG-KTVVIDAAYVDEK 439
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
61-403 2.24e-49

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: 173.46  E-value: 2.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   61 LTPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVFYADALKGddgvELEKSNILLVGPSGSGKTLLAKTLARVLRVPFA 140
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKD----EVTPKNILMIGPTGVGKTEIARRLAKLANAPFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  141 IADATTLTEAGYVGEDVENILVQLLQNA---------------------------------------------------- 168
Cdd:TIGR00390  77 KVEATKFTEVGYVGRDVESMVRDLTDAAvklvkeeaiekvrdraeelaeerivdvllppaknqwgqteqqqepesareaf 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  169 ----------DYDLEA----------------------------------------------ARK--------------- 177
Cdd:TIGR00390 157 rkklregeldDKEIEIdvsakmpsgieimappgmeemtmqlqslfqnlggqkkkkrklkikdAKKaliaeeaaklvdpee 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  178 ------------GIIYIDEIDKISRKADGPSitRDVSGEGVQQALLKIIEGTEANIppkggrKHPQqefirMDTSNILFI 245
Cdd:TIGR00390 237 ikqeaidaveqsGIIFIDEIDKIAKKGESSG--ADVSREGVQRDLLPIVEGSTVNT------KYGM-----VKTDHILFI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  246 VGGAFigldkiveqrmrggsmgfgakvetkkertlgellEQVHPADLvqfglIPEFVGRIPVLTHVDDLGEDDLVRILTE 325
Cdd:TIGR00390 304 AAGAF----------------------------------QLAKPSDL-----IPELQGRFPIRVELQALTTDDFERILTE 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  326 PKNALTRQYQKLFELDNVTLRFTSDALRAIAHRA--IERKT---GARGLRNVMESVMLDIMYQLPSMPGvKECVINDAVI 400
Cdd:TIGR00390 345 PKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAynVNEKTeniGARRLHTVLERLLEDISFEAPDLSG-QNITIDADYV 423

                  ...
gi 491169658  401 EKK 403
Cdd:TIGR00390 424 SKK 426
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
62-250 5.37e-44

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: 151.38  E-value: 5.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  62 TPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVFYADALKGddgvELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAI 141
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRD----EVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 142 ADATTLTEAGYVGEDVENILVQLLqnadydleaarKGIIYIDEIDKISRKADGPSitRDVSGEGVQQALLKIIEGTEANI 221
Cdd:cd19498   77 VEATKFTEVGYVGRDVESIIRDLV-----------EGIVFIDEIDKIAKRGGSSG--PDVSREGVQRDLLPIVEGSTVST 143
                        170       180
                 ....*....|....*....|....*....
gi 491169658 222 ppKGGrkhpqqefiRMDTSNILFIVGGAF 250
Cdd:cd19498  144 --KYG---------PVKTDHILFIAAGAF 161
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
110-307 1.84e-35

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: 128.47  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  110 EKSNILLVGPSGSGKTLLAKTLARVLRV---PFAIADATTLTEagyvgedvENILVQLLQNADYDLEAARKG-------- 178
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  179 ----IIYIDEIDKISRkadgpsitrdvsgeGVQQALLKIIEGTEANipPKGGRKhpqqefirMDTSNILFIVGGAFiGLD 254
Cdd:pfam07724  74 kpysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT--DKQGRT--------VDFKNTLFIMTGNF-GSE 128
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491169658  255 KIVEQRMRGGSmgfgakvetkkertLGELLEQVHPADLVQFGLIPEFVGRIPV 307
Cdd:pfam07724 129 KISDASRLGDS--------------PDYELLKEEVMDLLKKGFIPEFLGRLPI 167
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
314-395 3.54e-20

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: 84.42  E-value: 3.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   314 LGEDDLVRILTEPKNALTRQYqklfELDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPS---MPGV 390
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILsgeLKDG 76

                   ....*
gi 491169658   391 KECVI 395
Cdd:smart01086  77 DTVVV 81
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
80-220 4.35e-19

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: 83.49  E-value: 4.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  80 AKKILAVAVHNHYKRvfyadaLKGDDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAgYVGEDVEN 159
Cdd:cd19481    1 LKASLREAVEAPRRG------SRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491169658 160 IlvQLLqnadydLEAARK---GIIYIDEIDKISRKADGPSITRDVSgeGVQQALLKIIEGTEAN 220
Cdd:cd19481   74 L--RKI------FERARRlapCILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDGVNSR 127
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
10-48 6.06e-19

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 79.50  E-value: 6.06e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 491169658   10 PRCSFCGKTETQANQLVSGPDGVHICDECIATCNEMMAQ 48
Cdd:pfam06689   1 LRCSFCGKSEDEVKKLIAGPNGVYICDECVELCYEILEE 39
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
114-223 7.01e-17

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: 76.48  E-value: 7.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEaGYVGEDVENIlVQLLQNAdydlEAARKGIIYIDEIDKISRKAD 193
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRL-RELFEAA----KKLAPCVIFIDEIDALAGSRG 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 491169658  194 GPSitrDVSGEGVQQALLKIIEGTEANIPP 223
Cdd:pfam00004  75 SGG---DSESRRVVNQLLTELDGFTSSNSK 101
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
70-188 1.04e-15

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 76.08  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  70 LDEyVIGQDEAKKILAVAVHNHYKRvfyaDALKGddgVELEKS-NILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLT 148
Cdd:COG1223    1 LDD-VVGQEEAKKKLKLIIKELRRR----ENLRK---FGLWPPrKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491169658 149 EAgYVGEDVENiLVQLLQNAdydleAARKGIIYIDEIDKI 188
Cdd:COG1223   73 GS-YLGETARN-LRKLFDFA-----RRAPCVIFFDEFDAI 105
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
55-221 6.10e-15

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: 76.10  E-value: 6.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  55 REDERLLTPQEIKARLDEY--VIGQDEAKKILAVAVhnhyKRVFYADALKGDDGVELEKSnILLVGPSGSGKTLLAKTLA 132
Cdd:COG0464  138 YEDIGGLEEELLELREAILddLGGLEEVKEELRELV----ALPLKRPELREEYGLPPPRG-LLLYGPPGTGKTLLARALA 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 133 RVLRVPFAIADATTLTeAGYVGEDVENIlVQLLQNAdydlEAARKGIIYIDEIDKISRKADGpsiTRDVSGEGVQQALLK 212
Cdd:COG0464  213 GELGLPLIEVDLSDLV-SKYVGETEKNL-REVFDKA----RGLAPCVLFIDEADALAGKRGE---VGDGVGRRVVNTLLT 283

                 ....*....
gi 491169658 213 IIEGTEANI 221
Cdd:COG0464  284 EMEELRSDV 292
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
10-48 2.51e-14

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 66.44  E-value: 2.51e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 491169658    10 PRCSFCGKTETQANQLVSGPdGVHICDECIATCNEMMAQ 48
Cdd:smart00994   1 LRCSFCGKSESEVRKLIAGP-GVYICDECVELCYEILEE 38
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
75-193 6.66e-14

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: 68.71  E-value: 6.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  75 IGQDEAKKILAVAVHNHYKRvfyadalkgddgveleksNILLVGPSGSGKTLLAKTLARVL---RVPFAIADATTLTEAG 151
Cdd:cd00009    1 VGQEEAIEALREALELPPPK------------------NLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGL 62
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491169658 152 YVGEDVENILVQLLQNAdydLEAARKGIIYIDEIDKISRKAD 193
Cdd:cd00009   63 VVAELFGHFLVRLLFEL---AEKAKPGVLFIDEIDSLSRGAQ 101
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
314-386 4.57e-12

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, 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: 61.27  E-value: 4.57e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491169658  314 LGEDDLVRILTEpknALTRQYQKLFElDNVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLDIMYQLPS 386
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEIL 69
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
114-220 5.04e-09

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 57.32  E-value: 5.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAgYVGEDvENILVQLLQNAdydlEAARKGIIYIDEIDKISRKAD 193
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK-YIGEG-ARNVREVFELA----REKAPSIIFIDEIDAIAARRT 188
                         90       100
                 ....*....|....*....|....*....
gi 491169658 194 GpSITrdvSGEG--VQQALLKIIEGTEAN 220
Cdd:COG1222  189 D-DGT---SGEVqrTVNQLLAELDGFESR 213
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
74-191 1.19e-08

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: 53.90  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  74 VIGQDEAKKILAVAVHNHYKRvfyADALKGDDGVeleKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYV 153
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLR---PDLFPGLRGP---PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWV 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491169658 154 GEDvENILVQLlqnadydLEAARK---GIIYIDEIDKISRK 191
Cdd:cd19509   74 GES-EKIVRAL-------FALARElqpSIIFIDEIDSLLSE 106
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
74-191 2.04e-08

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 53.39  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  74 VIGQDEAKKILAVAVhnhykrvfyaDALKGDD-----GVELEKSnILLVGPSGSGKTLLAKTLARVLRVPF-AIAdattl 147
Cdd:cd19501    6 VAGCEEAKEELKEVV----------EFLKNPEkftklGAKIPKG-VLLVGPPGTGKTLLAKAVAGEAGVPFfSIS----- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491169658 148 teagyvGEDVENILVQLLQNADYDL-EAARKG---IIYIDEIDKISRK 191
Cdd:cd19501   70 ------GSDFVEMFVGVGASRVRDLfEQAKKNapcIVFIDEIDAVGRK 111
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
114-194 3.35e-08

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: 52.68  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDVENiLVQLLQNAdydlEAARKGIIYIDEIDKI--SRK 191
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN-LREIFEEA----RSHAPSIIFIDEIDALapKRE 110

                 ...
gi 491169658 192 ADG 194
Cdd:cd19503  111 EDQ 113
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
114-210 4.50e-08

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: 52.41  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDVENILvQLLQNAdydlEAARKGIIYIDEIDKISRKAD 193
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEKIR-ELFDQA----ISNAPCIVFIDEIDAITPKRE 110
                         90
                 ....*....|....*..
gi 491169658 194 GPSitRDVSGEGVQQAL 210
Cdd:cd19518  111 SAQ--REMERRIVSQLL 125
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
45-190 9.76e-08

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 53.21  E-value: 9.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  45 MMAQNAIEQVREDERLLTPQeikaRLDEYvIGQDEAKKILAVAVHNHYKRvfyADALkgdDgveleksNILLVGPSGSGK 124
Cdd:PRK00080   3 VSPETLEEEEDEIERSLRPK----SLDEF-IGQEKVKENLKIFIEAAKKR---GEAL---D-------HVLLYGPPGLGK 64
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491169658 125 TLLAKTLARVLRVPFAIADATTLTEAGyvgeDVENILVqLLQNADydleaarkgIIYIDEIDKISR 190
Cdd:PRK00080  65 TTLANIIANEMGVNIRITSGPALEKPG----DLAAILT-NLEEGD---------VLFIDEIHRLSP 116
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
74-224 1.03e-07

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: 51.52  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  74 VIGQDEAKKILAVAVhnhYKRVFYADALKGddgVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYV 153
Cdd:cd19522    2 IADLEEAKKLLEEAV---VLPMWMPEFFKG---IRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYR 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491169658 154 GEDVEniLVQLLqnadydLEAAR---KGIIYIDEIDKISRKADGPS---ITRDVSGEGVQQalLKIIEGTEANIPPK 224
Cdd:cd19522   75 GESEK--LVRLL------FEMARfyaPTTIFIDEIDSICSRRGTSEeheASRRVKSELLVQ--MDGVGGASENDDPS 141
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
59-220 1.14e-07

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 53.88  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  59 RLLTPQEIKARLDEyVIGQDEAKKILAVAVhNHYKRVFYADALKGddgvELEKSnILLVGPSGSGKTLLAKTLARVLRVP 138
Cdd:PRK10733 140 RMLTEDQIKTTFAD-VAGCDEAKEEVAELV-EYLREPSRFQKLGG----KIPKG-VLMVGPPGTGKTLLAKAIAGEAKVP 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 139 FAIADATTLTEAgYVGEDVENILvQLLQNAdydlEAARKGIIYIDEIDKISR-KADGPSITRDVSGEGVQQALLKiIEGT 217
Cdd:PRK10733 213 FFTISGSDFVEM-FVGVGASRVR-DMFEQA----KKAAPCIIFIDEIDAVGRqRGAGLGGGHDEREQTLNQMLVE-MDGF 285

                 ...
gi 491169658 218 EAN 220
Cdd:PRK10733 286 EGN 288
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
111-192 1.76e-07

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: 50.45  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   111 KSNILLVGPSGSGKTLLAKTLARVLRVP---FAIADATTLTEAGYVGEDVENIL--------VQLLQNADYDLEAARKGI 179
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGgkkasgsgELRLRLALALARKLKPDV 81
                           90
                   ....*....|...
gi 491169658   180 IYIDEIDKISRKA 192
Cdd:smart00382  82 LILDEITSLLDAE 94
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
113-192 3.09e-07

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: 49.21  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  113 NILLVGPSGSGKTLLAKTLARVL--RVPFAIADATTLTEAGYVGEdvENILVQLLQNADYDL-EAARKG-IIYIDEIDKI 188
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsnRPVFYVQLTRDTTEEDLFGR--RNIDPGGASWVDGPLvRAAREGeIAVLDEINRA 78

                  ....
gi 491169658  189 SRKA 192
Cdd:pfam07728  79 NPDV 82
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
69-215 4.30e-07

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 49.87  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  69 RLDEYVIGQDEAKKILAVAVHNHykRVFYADALKGDdgvelekSNILLVGPSGSGKTLLAKTLARVL--------RVPFA 140
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIRRA--RAGLSDPNRPI-------GSFLFLGPTGVGKTELAKALAELLfgdednliRIDMS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 141 IA----DATTLTEA--GYVGEDVenilvqllqnADYDLEAARK---GIIYIDEIDkisrKADGPsitrdvsgegVQQALL 211
Cdd:cd19499   79 EYmekhSVSRLIGAppGYVGYTE----------GGQLTEAVRRkpySVVLLDEIE----KAHPD----------VQNLLL 134

                 ....
gi 491169658 212 KIIE 215
Cdd:cd19499  135 QVLD 138
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
62-191 5.48e-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: 50.94  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  62 TPQEIKARLDEYVIGQDEAKKILAVAVhnhykrvfyadALKGddgveleksNILLVGPSGSGKTLLAKTLARVLRVPFAI 141
Cdd:COG0714    2 TEARLRAEIGKVYVGQEELIELVLIAL-----------LAGG---------HLLLEGVPGVGKTTLAKALARALGLPFIR 61
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491169658 142 ---------ADATtlteaG---YVGEDVENILVQ--LLQNadydleaarkgIIYIDEIDKISRK 191
Cdd:COG0714   62 iqftpdllpSDIL-----GtyiYDQQTGEFEFRPgpLFAN-----------VLLADEINRAPPK 109
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
106-216 5.72e-07

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: 51.83  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  106 GVELEKSnILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDVENiLVQLLQNADYDLEAarkgIIYIDEI 185
Cdd:TIGR01243 208 GIEPPKG-VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER-LREIFKEAEENAPS----IIFIDEI 280
                          90       100       110
                  ....*....|....*....|....*....|.
gi 491169658  186 DKISRKADgpSITRDVSGEGVQQaLLKIIEG 216
Cdd:TIGR01243 281 DAIAPKRE--EVTGEVEKRVVAQ-LLTLMDG 308
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
114-187 1.25e-06

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. 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: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 48.13  E-value: 1.25e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDVENiLVQLLQNAdydlEAARKGIIYIDEIDK 187
Cdd:cd19507   34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGESESR-LRQMIQTA----EAIAPCVLWIDEIEK 101
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
114-219 1.39e-06

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 48.25  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVL--RVPFAIADATTLTEagYVGEDVENILVQLlqnADYDLEAARKG------IIYIDEI 185
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLnaREPKIVNGPEILNK--YVGESEANIRKLF---ADAEEEQRRLGansglhIIIFDEI 112
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491169658 186 DKISRK----ADGPSItrdvsGEGVQQALLKIIEGTEA 219
Cdd:cd19504  113 DAICKQrgsmAGSTGV-----HDTVVNQLLSKIDGVEQ 145
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
69-185 3.13e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.93  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  69 RLDEyVIGQD---EAKKILavavhnhyKRVFYADALkgddgvelekSNILLVGPSGSGKTLLAKTLARVLRVPFAIADAT 145
Cdd:PRK13342  10 TLDE-VVGQEhllGPGKPL--------RRMIEAGRL----------SSMILWGPPGTGKTTLARIIAGATDAPFEALSAV 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491169658 146 TlteAGyVgEDVENIlvqlLQNADYDLEAARKGIIYIDEI 185
Cdd:PRK13342  71 T---SG-V-KDLREV----IEEARQRRSAGRRTILFIDEI 101
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
106-194 7.47e-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: 46.13  E-value: 7.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 106 GVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDvENILVQLLQNADYDLEAarkgIIYIDEI 185
Cdd:cd19525   50 GLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-EKMVRALFSVARCKQPA----VIFIDEI 123
                         90
                 ....*....|
gi 491169658 186 DK-ISRKADG 194
Cdd:cd19525  124 DSlLSQRGEG 133
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
74-188 7.99e-06

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 45.61  E-value: 7.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  74 VIGQDEAKKIL--AVAVHNHYKRVFyadalkgdDGVELEKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAG 151
Cdd:cd19524    2 IAGQDLAKQALqeMVILPSLRPELF--------TGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SK 72
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491169658 152 YVGEDvENILVQLLQNAdydlEAARKGIIYIDEIDKI 188
Cdd:cd19524   73 YVGEG-EKLVRALFAVA----RELQPSIIFIDEVDSL 104
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
114-190 8.36e-06

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: 45.88  E-value: 8.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAGYvGEDvenilvQLLQNADYDLeaARK---GIIYIDEIDKISR 190
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GES------QKLVAAVFSL--ASKlqpSIIFIDEIDSFLR 108
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
56-379 8.55e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 8.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  56 EDERLLTpqeIKARLDEYVIGQDEAKKILAVAVhnhyKR-------------VFyadalkgddgveleksniLLVGPSGS 122
Cdd:COG0542  536 EREKLLN---LEEELHERVIGQDEAVEAVADAI----RRsraglkdpnrpigSF------------------LFLGPTGV 590
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 123 GKTLLAKTLARVLrvpFAIADA-TTL-----TEA-----------GYVGedvenilvqllqnadYD----L-EAARK--- 177
Cdd:COG0542  591 GKTELAKALAEFL---FGDEDAlIRIdmseyMEKhsvsrligappGYVG---------------YEeggqLtEAVRRrpy 652
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 178 GIIYIDEIDkisrKADgPSitrdvsgegVQQALLKIIEgteanippKG------GRKhpqQEF----IRMdTSNilfivg 247
Cdd:COG0542  653 SVVLLDEIE----KAH-PD---------VFNILLQVLD--------DGrltdgqGRT---VDFrntiIIM-TSN------ 700
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 248 gafIGLDKIVEQRMRGGSmgfgakVETKKERTLGELLEQVHpadlvqfgliPEFVGRIpvlthvDD------LGEDDLVR 321
Cdd:COG0542  701 ---IGSELILDLAEDEPD------YEEMKEAVMEELKKHFR----------PEFLNRI------DEiivfhpLSKEELRK 755
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491169658 322 ILtepKNALTRQYQKLFELDnVTLRFTSDALRAIAHRAIERKTGARGLRNVMESVMLD 379
Cdd:COG0542  756 IV---DLQLKRLRKRLAERG-ITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELED 809
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
114-220 8.78e-06

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: 45.89  E-value: 8.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDVENilvqlLQNADYDLEAARKGIIYIDEIDKISRKAD 193
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN-----LRKAFEEAEKNAPAIIFIDEIDAIAPKRE 110
                         90       100
                 ....*....|....*....|....*..
gi 491169658 194 gpSITRDVSGEGVQQaLLKIIEGTEAN 220
Cdd:cd19519  111 --KTHGEVERRIVSQ-LLTLMDGLKQR 134
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
114-219 9.20e-06

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: 45.35  E-value: 9.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPF-AIADATTLTEagYVGEDvENILVQLLQNAdydlEAARKGIIYIDEIDKISRKa 192
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFiSVKGPELFSK--YVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLAPR- 101
                         90       100       110
                 ....*....|....*....|....*....|..
gi 491169658 193 dgpsitRDVSGEG-----VQQALLKIIEGTEA 219
Cdd:cd19511  102 ------RGQSDSSgvtdrVVSQLLTELDGIES 127
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
110-196 9.73e-06

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 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. This subfamily represents the second ATPase domain of PEX6. 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: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 45.58  E-value: 9.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 110 EKSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAgYVGEDVENILvQLLQNAdydlEAARKGIIYIDEIDKI- 188
Cdd:cd19527   25 KRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEANVR-EVFQKA----RDAKPCVIFFDELDSLa 98

                 ....*....
gi 491169658 189 -SRKADGPS 196
Cdd:cd19527   99 pSRGNSGDS 107
ftsH CHL00176
cell division protein; Validated
114-191 1.01e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 47.74  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTE--AGYVGEDVENILVQLLQNAdydleaarKGIIYIDEIDKISRK 191
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVGVGAARVRDLFKKAKENS--------PCIVFIDEIDAVGRQ 290
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
112-201 3.67e-05

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 45.59  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 112 SNILLVGPSGSGKTLLAKTLARVlrvpfaiADATTLTEAG------YVGEDVEniLVQllqnadyDL-EAARK---GIIY 181
Cdd:PRK03992 166 KGVLLYGPPGTGKTLLAKAVAHE-------TNATFIRVVGselvqkFIGEGAR--LVR-------ELfELAREkapSIIF 229
                         90       100
                 ....*....|....*....|..
gi 491169658 182 IDEIDKI--SRKADGPSITRDV 201
Cdd:PRK03992 230 IDEIDAIaaKRTDSGTSGDREV 251
AAA_22 pfam13401
AAA domain;
107-192 4.40e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.71  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  107 VELEKSNILLVGPSGSGKTLLAKTL--------ARVLRV---------PFAIADATTLTEAGYVGEDVENILVQLLQNAd 169
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLleqlpevrDSVVFVdlpsgtspkDLLRALLRALGLPLSGRLSKEELLAALQQLL- 79
                          90       100
                  ....*....|....*....|...
gi 491169658  170 ydLEAARKGIIYIDEIDKISRKA 192
Cdd:pfam13401  80 --LALAVAVVLIIDEAQHLSLEA 100
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
106-214 5.75e-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: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 106 GVELEKSnILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTEAgYVGEDVEniLVQLLqnadydLEAARK---GIIYI 182
Cdd:cd19502   33 GIEPPKG-VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGAR--LVREL------FEMAREkapSIIFI 102
                         90       100       110
                 ....*....|....*....|....*....|....
gi 491169658 183 DEIDKI--SRKADGPSITRDvsgegVQQALLKII 214
Cdd:cd19502  103 DEIDAIgaKRFDSGTGGDRE-----VQRTMLELL 131
ycf46 CHL00195
Ycf46; Provisional
114-187 1.05e-04

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 44.24  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDvENILVQLLQNAdydlEAARKGIIYIDEIDK 187
Cdd:CHL00195 262 LLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF-GGIVGES-ESRMRQMIRIA----EALSPCILWIDEIDK 329
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
74-135 1.44e-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: 43.88  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491169658  74 VIGQDEAKKILAVAV---HNhykrvfyadalkgddgveleksnILLVGPSGSGKTLLAKTLARVL 135
Cdd:COG0606  194 VKGQEQAKRALEIAAaggHN-----------------------LLMIGPPGSGKTMLARRLPGIL 235
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
112-196 1.47e-04

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 42.16  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 112 SNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDvENILVQLLQNAdydlEAARKGIIYIDEIDKI-SR 190
Cdd:cd19521   41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFAMA----RENKPSIIFIDEVDSLcGT 114

                 ....*.
gi 491169658 191 KADGPS 196
Cdd:cd19521  115 RGEGES 120
clpC CHL00095
Clp protease ATP binding subunit
56-132 2.15e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 43.51  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  56 EDERLLTPQEIkarLDEYVIGQDEAkkilAVAVHNHYKRVFyadalkgddgVELEKSN-----ILLVGPSGSGKTLLAKT 130
Cdd:CHL00095 496 ESEKLLHMEET---LHKRIIGQDEA----VVAVSKAIRRAR----------VGLKNPNrpiasFLFSGPTGVGKTELTKA 558

                 ..
gi 491169658 131 LA 132
Cdd:CHL00095 559 LA 560
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
114-232 2.35e-04

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 41.34  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPF-AIADATTLTEagYVGEDVENILvQLLQNAdydlEAARKGIIYIDEIDKISRKA 192
Cdd:cd19528   30 VLFYGPPGCGKTLLAKAIANECQANFiSVKGPELLTM--WFGESEANVR-DIFDKA----RAAAPCVLFFDELDSIAKAR 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491169658 193 DGPSITRDVSGEGVQQALLKIIEGTEA--NIPPKGGRKHPQQ 232
Cdd:cd19528  103 GGNIGDAGGAADRVINQILTEMDGMNTkkNVFIIGATNRPDI 144
PRK04195 PRK04195
replication factor C large subunit; Provisional
69-222 2.92e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.99  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  69 RLDEyVIGQDEAKKILAVavhnhykrvfYADA-LKGDDgveleKSNILLVGPSGSGKTLLAKTLARVLRVPfAI----AD 143
Cdd:PRK04195  12 TLSD-VVGNEKAKEQLRE----------WIESwLKGKP-----KKALLLYGPPGVGKTSLAHALANDYGWE-VIelnaSD 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491169658 144 ATTlteagyvGEDVENILVQLLQNAdyDLEAARKGIIYIDEIDKISRKADgpsitrdvsgEGVQQALLKIIEgtEANIP 222
Cdd:PRK04195  75 QRT-------ADVIERVAGEAATSG--SLFGARRKLILLDEVDGIHGNED----------RGGARAILELIK--KAKQP 132
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
114-218 2.96e-04

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 40.94  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPF-AIADATTLTEagYVGEDvENILVQLLQNAdydlEAARKGIIYIDEIDKISRKA 192
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFiSVKGPELLSK--WVGES-EKAIREIFRKA----RQVAPCVIFFDEIDSIAPRR 102
                         90       100
                 ....*....|....*....|....*.
gi 491169658 193 dGPSITRDVSGEGVQQaLLKIIEGTE 218
Cdd:cd19529  103 -GTTGDSGVTERVVNQ-LLTELDGLE 126
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
74-135 3.02e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 41.75  E-value: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491169658   74 VIGQDEAKKILAVAV---HNhykrvfyadalkgddgveleksnILLVGPSGSGKTLLAKTLARVL 135
Cdd:pfam01078   5 VKGQEQAKRALEIAAaggHN-----------------------LLMIGPPGSGKTMLAKRLPGIL 46
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
113-139 3.23e-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: 41.00  E-value: 3.23e-04
                         10        20
                 ....*....|....*....|....*..
gi 491169658 113 NILLVGPSGSGKTLLAKTLARVLRVPF 139
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPF 27
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
106-194 4.81e-04

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: 40.55  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 106 GVELEkSNILLVGPSGSGKTLLAKTLARVLRVPF-AIADATTLTEagYVGEDvENILVQLLQNAdydlEAARKGIIYIDE 184
Cdd:cd19530   26 GIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFiSVKGPELLNK--YVGES-ERAVRQVFQRA----RASAPCVIFFDE 97
                         90
                 ....*....|
gi 491169658 185 IDKISRKADG 194
Cdd:cd19530   98 VDALVPKRGD 107
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
90-188 5.73e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.13  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  90 NHYKRVFYADALKGDDGvELE----------KSNILLVGPSGSGKTLLAKTLA-RVLR--VPFAIADATT--------LT 148
Cdd:PRK11034 177 NQLARVGGIDPLIGREK-ELEraiqvlcrrrKNNPLLVGESGVGKTAIAEGLAwRIVQgdVPEVMADCTIysldigslLA 255
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491169658 149 EAGYVGeDVENILVQLLQNadydLEAARKGIIYIDEIDKI 188
Cdd:PRK11034 256 GTKYRG-DFEKRFKALLKQ----LEQDTNSILFIDEIHTI 290
aroK PRK00131
shikimate kinase; Reviewed
109-139 5.97e-04

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 40.56  E-value: 5.97e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 491169658 109 LEKSNILLVGPSGSGKTLLAKTLARVLRVPF 139
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
111-218 6.83e-04

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: 40.10  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 111 KSNILLVGPSGSGKTLLAKTLARVLRVPFAIADATTLTeAGYVGEDVENILvQLLQNAdydlEAARKGIIYIDEIDKIS- 189
Cdd:cd19526   27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVR-DLFSRA----QSAKPCILFFDEFDSIAp 100
                         90       100       110
                 ....*....|....*....|....*....|
gi 491169658 190 -RKADGPSITRDVsgegVQQaLLKIIEGTE 218
Cdd:cd19526  101 kRGHDSTGVTDRV----VNQ-LLTQLDGVE 125
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
76-220 6.96e-04

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: 41.82  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658   76 GQDEAKKILAVAVH--NHYKRVFYADALKGDDGVeleksniLLVGPSGSGKTLLAKTLARVLRVPF-AIADATTLTEagY 152
Cdd:TIGR01243 457 GLEEVKQELREAVEwpLKHPEIFEKMGIRPPKGV-------LLFGPPGTGKTLLAKAVATESGANFiAVRGPEILSK--W 527
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491169658  153 VGEDvENILVQLLQNAdydlEAARKGIIYIDEIDKISrKADGPSITRDVSGEGVQQaLLKIIEGTEAN 220
Cdd:TIGR01243 528 VGES-EKAIREIFRKA----RQAAPAIIFFDEIDAIA-PARGARFDTSVTDRIVNQ-LLTEMDGIQEL 588
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
113-200 7.17e-04

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. 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: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 39.82  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 113 NILLVGPSGSGKTLLAKTLARVLRVPFAIadaTTLTEAGYVGEDVENILVQLLQNADydleAARKG-IIYIDEIDKISRK 191
Cdd:cd19512   24 NILFYGPPGTGKTLFAKKLALHSGMDYAI---MTGGDVAPMGREGVTAIHKVFDWAN----TSRRGlLLFVDEADAFLRK 96

                 ....*....
gi 491169658 192 ADGPSITRD 200
Cdd:cd19512   97 RSTEKISED 105
MCM_arch cd17761
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ...
76-213 8.99e-04

archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork


Pssm-ID: 350667 [Multi-domain]  Cd Length: 308  Bit Score: 40.90  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  76 GQDEAKKILAVAVhnhykrvFYADALKGDDGVELEKS-NILLVGPSGSGKTLLAKTLARVL-RVPFAIADATT---LTeA 150
Cdd:cd17761   13 GHEDVKEAIALQL-------FGGVPKVLPDGTRIRGDiHILLVGDPGTAKSQLLKYVSKVApRAVYTTGKGSTaagLT-A 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491169658 151 GYVGEDVEnilvqllqnADYDLEA-----ARKGIIYIDEIDKIsRKADgpsitRDVSGEGVQQALLKI 213
Cdd:cd17761   85 AVVRDEGT---------GEWYLEAgalvlADKGIAVVDEIDKM-RKED-----RSALHEAMEQQTISI 137
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
59-191 9.39e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 41.56  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  59 RLLTPQEIKARLDEyVIGQDEAKKILAVAV---HNHYKrvfYAdAL-----KGddgveleksnILLVGPSGSGKTLLAKt 130
Cdd:COG0465  130 KLYDEDKPKVTFDD-VAGVDEAKEELQEIVdflKDPEK---FT-RLgakipKG----------VLLVGPPGTGKTLLAK- 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 131 larvlrvpfAIADattltEAG--------------YVG---EDVEnilvqllqnadyDL-EAARKG---IIYIDEIDKIS 189
Cdd:COG0465  194 ---------AVAG-----EAGvpffsisgsdfvemFVGvgaSRVR------------DLfEQAKKNapcIIFIDEIDAVG 247

                 ..
gi 491169658 190 RK 191
Cdd:COG0465  248 RQ 249
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
56-139 1.21e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  56 EDERLLTPQEIKARLDEYVIGQDEAKKILAVAVHNHYKRVF--YADALKgddgvelEKSNILLVGPSGSGKTLLAKTLA- 132
Cdd:COG1401  171 DLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLeaFLAALK-------TKKNVILAGPPGTGKTYLARRLAe 243
                         90
                 ....*....|....*
gi 491169658 133 --------RVLRVPF 139
Cdd:COG1401  244 alggedngRIEFVQF 258
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
114-139 1.24e-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: 1.24e-03
                         10        20
                 ....*....|....*....|....*.
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPF 139
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPF 26
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
114-137 1.70e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 39.44  E-value: 1.70e-03
                         10        20
                 ....*....|....*....|....
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRV 137
Cdd:COG0572   10 IGIAGPSGSGKTTFARRLAEQLGA 33
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
100-182 4.56e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.61  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 100 ALKGDDgVELEKSNIL-LVGPSGSGKTLLAKTLARVLRVPfaiadattlteAGyvgedveNILVQLLQNADYDLEAARKG 178
Cdd:cd00267   14 ALDNVS-LTLKAGEIVaLVGPNGSGKSTLLRAIAGLLKPT-----------SG-------EILIDGKDIAKLPLEELRRR 74

                 ....
gi 491169658 179 IIYI 182
Cdd:cd00267   75 IGYV 78
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
114-144 4.75e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 37.42  E-value: 4.75e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLRVPFAIADA 144
Cdd:COG3265    4 IVVMGVSGSGKSTVGQALAERLGWPFIDGDD 34
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
74-215 4.83e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 38.63  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  74 VIGQDEAKKILAVAVHNHykRVFYAdalkgddgveleksnILLVGPSGSGKTLLAKTLARVL----RVPF---------- 139
Cdd:COG2812   12 VVGQEHVVRTLKNALASG--RLAHA---------------YLFTGPRGVGKTTLARILAKALncenGPTGepcgecescr 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658 140 AIADATTL------TEAGYVGedVENILvQLLQNADYD-LEAARKgiIY-IDEIDKISRKAdgpsitrdvsgegvQQALL 211
Cdd:COG2812   75 AIAAGSHPdvieidAEASNIG--VDDIR-ELIEKVSYApVEGRYK--VYiIDEAHMLTTEA--------------FNALL 135

                 ....
gi 491169658 212 KIIE 215
Cdd:COG2812  136 KTLE 139
MCM pfam00493
MCM P-loop domain;
113-191 5.27e-03

MCM P-loop domain;


Pssm-ID: 459830 [Multi-domain]  Cd Length: 224  Bit Score: 38.28  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  113 NILLVGPSGSGKTLLAKTLARVLrvPFAI-ADATTLTEAG---YVGEDVENIlvqllqnaDYDLEA-----ARKGIIYID 183
Cdd:pfam00493  59 NVLLVGDPGTAKSQLLKYVEKIA--PRAVyTSGKGSSAAGltaAVVRDPVTG--------EFVLEAgalvlADGGVCCID 128

                  ....*...
gi 491169658  184 EIDKISRK 191
Cdd:pfam00493 129 EFDKMNDE 136
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
114-133 6.26e-03

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 37.87  E-value: 6.26e-03
                         10        20
                 ....*....|....*....|
gi 491169658 114 ILLVGPSGSGKTLLAKTLAR 133
Cdd:COG4619   29 VAITGPSGSGKSTLLRALAD 48
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
105-137 7.13e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 37.87  E-value: 7.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 491169658 105 DGV--ELEKSNIL-LVGPSGSGKTLLAKTLARVLRV 137
Cdd:cd03257   22 DDVsfSIKKGETLgLVGESGSGKSTLARAILGLLKP 57
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
114-162 8.16e-03

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 38.21  E-value: 8.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491169658 114 ILLVGPSGSGKTLLAKTLARVLR----------VPFAIADATTLTEA-GYVGEDV--------ENILV 162
Cdd:COG4987  364 VAIVGPSGSGKSTLLALLLRFLDpqsgsitlggVDLRDLDEDDLRRRiAVVPQRPhlfdttlrENLRL 431
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
116-136 8.92e-03

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 38.35  E-value: 8.92e-03
                         10        20
                 ....*....|....*....|.
gi 491169658 116 LVGPSGSGKTLLAKTLARVLR 136
Cdd:COG1123  296 LVGESGSGKSTLARLLLGLLR 316
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
113-216 9.21e-03

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 36.84  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  113 NILLVGPSGSGKTLLAKTLARVL--------------------RVPFAIADATT-----LTEAGYVG-----------ED 156
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLkssgvkvggfytpevreggrRIGFKIVDLASgeegwLARVGAVSgprvgkyvvnvES 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491169658  157 VENILVQLLQNADYDleaarKGIIYIDEIDKISRKAdgpsitrdvsgEGVQQALLKIIEG 216
Cdd:pfam03266  81 FEEIAVPALRRALEE-----ADLIIIDEIGPMELKS-----------KKFREAVREVLDS 124
 
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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