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Conserved domains on  [gi|767983141|ref|XP_011519466|]
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ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

Zn-ribbon and AAA domain-containing protein( domain architecture ID 11641334)

Zn-ribbon and AAA domain-containing protein

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 ...
172-591 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 559.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:COG1219   66 IKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSG----------------------------------------------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevlDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:COG1219   99 ----------SKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKI---GSVPGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASG 407
Cdd:COG1219  169 DVEKAERGIIYIDEIDKIarkSENPSI--TRDVSGEGVQQALLKILEGTVANVPPQGGRKhPQQEFIQIDTTNILFICGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 408 AFNGLDRIISRRKNEKYLGFGTpsnlgkgrraaaaadlanrsgESNTHQDIEEKDrLLRHVEARDLIEFGMIPEFVGRLP 487
Cdd:COG1219  247 AFDGLEKIIERRLGKKSIGFGA---------------------EVKSKKEKDEGE-LLKQVEPEDLIKFGLIPEFIGRLP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 488 VVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN 567
Cdd:COG1219  305 VIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPS 384
                        410       420
                 ....*....|....*....|....*
gi 767983141 568 -SDIVCVEVDKEVVEGKKEPGYIRA 591
Cdd:COG1219  385 rKDVKKVVITKEVVEGKAKPILVYK 409
Zn-ribbon super family cl02609
C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit; The ...
104-132 7.55e-03

C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit; The homologous C-terminal zinc ribbon domains of subunits A12.2, Rpb9, and C11 in RNA Polymerases (Pol) I, II, and III, respectively are required for intrinsic transcript cleavage. TFS is a related archaeal protein that is involved in RNA cleavage by archaeal polymerase. These proteins have two zinc-binding beta-ribbon domains, N-terminal zinc ribbon (N-ribbon) and C-terminal zinc ribbon (C-ribbon). Transcription Factor IIS (TFIIS) domain III is homologous to the C-ribbon domain that stimulates the weak cleavage activity of Rpb9 for Pol II.


The actual alignment was detected with superfamily member cd00656:

Pssm-ID: 445850  Cd Length: 45  Bit Score: 34.60  E-value: 7.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767983141 104 RCPKCGdlctHVETFV----------SSTRFVKCEKCHH 132
Cdd:cd00656    8 TCPKCG----HDEAYWwmlqtrsadePPTRFYKCTKCGH 42
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
172-591 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 559.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:COG1219   66 IKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSG----------------------------------------------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevlDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:COG1219   99 ----------SKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKI---GSVPGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASG 407
Cdd:COG1219  169 DVEKAERGIIYIDEIDKIarkSENPSI--TRDVSGEGVQQALLKILEGTVANVPPQGGRKhPQQEFIQIDTTNILFICGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 408 AFNGLDRIISRRKNEKYLGFGTpsnlgkgrraaaaadlanrsgESNTHQDIEEKDrLLRHVEARDLIEFGMIPEFVGRLP 487
Cdd:COG1219  247 AFDGLEKIIERRLGKKSIGFGA---------------------EVKSKKEKDEGE-LLKQVEPEDLIKFGLIPEFIGRLP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 488 VVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN 567
Cdd:COG1219  305 VIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPS 384
                        410       420
                 ....*....|....*....|....*
gi 767983141 568 -SDIVCVEVDKEVVEGKKEPGYIRA 591
Cdd:COG1219  385 rKDVKKVVITKEVVEGKAKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
172-594 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 553.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:PRK05342  65 IKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHG----------------------------------------------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevlDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:PRK05342  98 ----------DKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKI---GSVPGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASG 407
Cdd:PRK05342 168 DVEKAQRGIVYIDEIDKIarkSENPSI--TRDVSGEGVQQALLKILEGTVASVPPQGGRKhPQQEFIQVDTTNILFICGG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 408 AFNGLDRIISRRKNEKYLGFGTpsnlgkgrraaaaadlanrsgESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLP 487
Cdd:PRK05342 246 AFDGLEKIIKQRLGKKGIGFGA---------------------EVKSKKEKRTEGELLKQVEPEDLIKFGLIPEFIGRLP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 488 VVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN 567
Cdd:PRK05342 305 VVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPS 384
                        410       420
                 ....*....|....*....|....*...
gi 767983141 568 -SDIVCVEVDKEVVEGKKEPGYIRAPTK 594
Cdd:PRK05342 385 rEDVEKVVITKEVVEGKAKPLLIYREKS 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
172-492 6.78e-144

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: 417.00  E-value: 6.78e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:cd19497    6 IKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNN----------------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:cd19497   39 ---------LKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKIGSVPG-IHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASGAF 409
Cdd:cd19497  110 DVERAQRGIVYIDEIDKIARKSEnPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKhPQQEFIQVDTTNILFICGGAF 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 410 NGLDRIISRRKNEKYLGFGTPSNLgkgrraaaaadlanrsgesntHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVV 489
Cdd:cd19497  190 VGLEKIIARRLGKKSLGFGAETSS---------------------EKDEKERDELLSKVEPEDLIKFGLIPEFVGRLPVI 248

                 ...
gi 767983141 490 VPL 492
Cdd:cd19497  249 VTL 251
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
102-586 4.13e-143

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: 421.48  E-value: 4.13e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  102 QLRCPKCGDLCTHVETFVSSTRFVKCEKC----HHffvVLSEADSKKSIIKEPESAAEAVKLAFQQKpppppkkIYNYLD 177
Cdd:TIGR00382   7 TLYCSFCGKSQDEVRKLIAGPGVYICDECielcHD---ILEEELGTRKESKEYEEEFELSYLPTPKE-------IKAHLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  178 KYVVGQSFAKKVLSVAVYNHYKRIynnipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqipqekrG 257
Cdd:TIGR00382  77 EYVIGQEQAKKVLSVAVYNHYKRL-------------------------------------------------------N 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  258 GEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQ 337
Cdd:TIGR00382 102 FEKNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQ 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  338 QGIVFLDEVDKIGSV---PGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKL-RGETVQVDTTNILFVASGAFNGLD 413
Cdd:TIGR00382 182 KGIIYIDEIDKISRKsenPSI--TRDVSGEGVQQALLKIIEGTVANVPPQGGRKHpYQEFIQIDTSNILFICGGAFVGLE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  414 RIISRRKNEKYLGFGTPSNlgkgrraaaaadlanrsgesnthQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLH 493
Cdd:TIGR00382 260 KIIKKRTGKSSIGFGAEVK-----------------------KKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLE 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  494 SLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN-SDIVC 572
Cdd:TIGR00382 317 KLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSlEDLEK 396
                         490
                  ....*....|....
gi 767983141  573 VEVDKEVVEGKKEP 586
Cdd:TIGR00382 397 VVITKETVLKQSEP 410
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
271-489 4.23e-32

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: 121.92  E-value: 4.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  271 EKSNILLLGPTGSGKTLLAQTLAKCLDV---PFAICDCTTLTQagyvgediESVIAKLLQDANYNVEKAQQG-------- 339
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  340 ----IVFLDEVDKIGSvpgihqlrdvggeGVQQGLLKLLEGTIVNVpeknsrklrGETVQVDTTNILFVASGAFNGLDRI 415
Cdd:pfam07724  74 kpysIVLIDEIEKAHP-------------GVQNDLLQILEGGTLTD---------KQGRTVDFKNTLFIMTGNFGSEKIS 131
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983141  416 ISRRknekylgfgtpsnlgkgrraaaaadlanrsgesnthqDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVV 489
Cdd:pfam07724 132 DASR-------------------------------------LGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
495-589 4.48e-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: 84.80  E-value: 4.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141   495 LDEKTLVQILTEPRNAVIPQYqalfSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVcVE 574
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGEL-KD 75
                           90
                   ....*....|....*
gi 767983141   575 VDKEVVEGKKEPGYI 589
Cdd:smart01086  76 GDTVVVDVDDGELVF 90
Zn-ribbon cd00656
C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit; The ...
104-132 7.55e-03

C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit; The homologous C-terminal zinc ribbon domains of subunits A12.2, Rpb9, and C11 in RNA Polymerases (Pol) I, II, and III, respectively are required for intrinsic transcript cleavage. TFS is a related archaeal protein that is involved in RNA cleavage by archaeal polymerase. These proteins have two zinc-binding beta-ribbon domains, N-terminal zinc ribbon (N-ribbon) and C-terminal zinc ribbon (C-ribbon). Transcription Factor IIS (TFIIS) domain III is homologous to the C-ribbon domain that stimulates the weak cleavage activity of Rpb9 for Pol II.


Pssm-ID: 259791  Cd Length: 45  Bit Score: 34.60  E-value: 7.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767983141 104 RCPKCGdlctHVETFV----------SSTRFVKCEKCHH 132
Cdd:cd00656    8 TCPKCG----HDEAYWwmlqtrsadePPTRFYKCTKCGH 42
RPB9 COG1594
DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]; ...
104-132 7.99e-03

DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]; DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441202 [Multi-domain]  Cd Length: 103  Bit Score: 36.46  E-value: 7.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767983141 104 RCPKCGdlctHVETFV----------SSTRFVKCEKCHH 132
Cdd:COG1594   64 ICPKCG----NDEAYWwlkqtrsadePETRFFRCTKCGH 98
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
172-591 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 559.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:COG1219   66 IKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSG----------------------------------------------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevlDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:COG1219   99 ----------SKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKI---GSVPGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASG 407
Cdd:COG1219  169 DVEKAERGIIYIDEIDKIarkSENPSI--TRDVSGEGVQQALLKILEGTVANVPPQGGRKhPQQEFIQIDTTNILFICGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 408 AFNGLDRIISRRKNEKYLGFGTpsnlgkgrraaaaadlanrsgESNTHQDIEEKDrLLRHVEARDLIEFGMIPEFVGRLP 487
Cdd:COG1219  247 AFDGLEKIIERRLGKKSIGFGA---------------------EVKSKKEKDEGE-LLKQVEPEDLIKFGLIPEFIGRLP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 488 VVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN 567
Cdd:COG1219  305 VIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPS 384
                        410       420
                 ....*....|....*....|....*
gi 767983141 568 -SDIVCVEVDKEVVEGKKEPGYIRA 591
Cdd:COG1219  385 rKDVKKVVITKEVVEGKAKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
172-594 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 553.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:PRK05342  65 IKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHG----------------------------------------------- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevlDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:PRK05342  98 ----------DKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKI---GSVPGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASG 407
Cdd:PRK05342 168 DVEKAQRGIVYIDEIDKIarkSENPSI--TRDVSGEGVQQALLKILEGTVASVPPQGGRKhPQQEFIQVDTTNILFICGG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 408 AFNGLDRIISRRKNEKYLGFGTpsnlgkgrraaaaadlanrsgESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLP 487
Cdd:PRK05342 246 AFDGLEKIIKQRLGKKGIGFGA---------------------EVKSKKEKRTEGELLKQVEPEDLIKFGLIPEFIGRLP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 488 VVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN 567
Cdd:PRK05342 305 VVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPS 384
                        410       420
                 ....*....|....*....|....*...
gi 767983141 568 -SDIVCVEVDKEVVEGKKEPGYIRAPTK 594
Cdd:PRK05342 385 rEDVEKVVITKEVVEGKAKPLLIYREKS 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
172-492 6.78e-144

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: 417.00  E-value: 6.78e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqi 251
Cdd:cd19497    6 IKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNN----------------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANY 331
Cdd:cd19497   39 ---------LKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADY 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 332 NVEKAQQGIVFLDEVDKIGSVPG-IHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRK-LRGETVQVDTTNILFVASGAF 409
Cdd:cd19497  110 DVERAQRGIVYIDEIDKIARKSEnPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKhPQQEFIQVDTTNILFICGGAF 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 410 NGLDRIISRRKNEKYLGFGTPSNLgkgrraaaaadlanrsgesntHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVV 489
Cdd:cd19497  190 VGLEKIIARRLGKKSLGFGAETSS---------------------EKDEKERDELLSKVEPEDLIKFGLIPEFVGRLPVI 248

                 ...
gi 767983141 490 VPL 492
Cdd:cd19497  249 VTL 251
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
102-586 4.13e-143

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: 421.48  E-value: 4.13e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  102 QLRCPKCGDLCTHVETFVSSTRFVKCEKC----HHffvVLSEADSKKSIIKEPESAAEAVKLAFQQKpppppkkIYNYLD 177
Cdd:TIGR00382   7 TLYCSFCGKSQDEVRKLIAGPGVYICDECielcHD---ILEEELGTRKESKEYEEEFELSYLPTPKE-------IKAHLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  178 KYVVGQSFAKKVLSVAVYNHYKRIynnipanlrqqaevekqtsltprellqiagisphgnalgasmqqqvnqqipqekrG 257
Cdd:TIGR00382  77 EYVIGQEQAKKVLSVAVYNHYKRL-------------------------------------------------------N 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  258 GEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQ 337
Cdd:TIGR00382 102 FEKNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQ 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  338 QGIVFLDEVDKIGSV---PGIhqLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKL-RGETVQVDTTNILFVASGAFNGLD 413
Cdd:TIGR00382 182 KGIIYIDEIDKISRKsenPSI--TRDVSGEGVQQALLKIIEGTVANVPPQGGRKHpYQEFIQIDTSNILFICGGAFVGLE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  414 RIISRRKNEKYLGFGTPSNlgkgrraaaaadlanrsgesnthQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLH 493
Cdd:TIGR00382 260 KIIKKRTGKSSIGFGAEVK-----------------------KKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLE 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  494 SLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPN-SDIVC 572
Cdd:TIGR00382 317 KLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSlEDLEK 396
                         490
                  ....*....|....
gi 767983141  573 VEVDKEVVEGKKEP 586
Cdd:TIGR00382 397 VVITKETVLKQSEP 410
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
172-583 1.30e-43

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 161.78  E-value: 1.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRiyNNIPANLRQqaEVekqtslTPRellqiagisphgnalgasmqqqvnqqi 251
Cdd:PRK05201   9 IVSELDKYIIGQDDAKRAVAIALRNRWRR--MQLPEELRD--EV------TPK--------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevldsshddikleksNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVI--------- 322
Cdd:PRK05201  52 ----------------------NILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGRDVESIIrdlveiavk 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141     --------------------------------------------------------------------------------
Cdd:PRK05201 110 mvreekrekvrekaeeaaeerildallppaknnwgeeeekeeisatrqkfrkklregelddkeieievaeaapmmeimgp 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 323 -----------------------------------------AKLL------QDANYNVEkaQQGIVFLDEVDKIGSVPGI 355
Cdd:PRK05201 190 pgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaAKLIdmeeikQEAIERVE--QNGIVFIDEIDKIAARGGS 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 356 HQlRDVGGEGVQQGLLKLLEGTIVNVpeknsrKLrGetvQVDTTNILFVASGAFNgldriISRrknekylgfgtPSNLgk 435
Cdd:PRK05201 268 SG-PDVSREGVQRDLLPLVEGSTVST------KY-G---MVKTDHILFIASGAFH-----VSK-----------PSDL-- 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 436 grraaaaadlanrsgesnthqdieekdrllrhveardliefgmIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQY 515
Cdd:PRK05201 319 -------------------------------------------IPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQY 355
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767983141 516 QALFSMDKCELNVTEDALKAIARLALE--RKT---GARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGK 583
Cdd:PRK05201 356 QALLATEGVTLEFTDDAIRRIAEIAYQvnEKTeniGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEK 428
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
172-583 1.89e-39

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 150.58  E-value: 1.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRiyNNIPANLRQqaEVekqtslTPRellqiagisphgnalgasmqqqvnqqi 251
Cdd:COG1220    9 IVAELDKYIIGQDEAKRAVAIALRNRWRR--QQLPEELRD--EI------TPK--------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevldsshddikleksNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVI--------- 322
Cdd:COG1220   52 ----------------------NILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGRDVESMIrdlveiavk 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141     --------------------------------------------------------------------------------
Cdd:COG1220  110 mvreekmekvrekaeeaaeerildlllpppkkkagsnnpfeeeeeeeeeeeeisrtrekfrkklregelddreieievee 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 323 ----------------------------------------------------AKLL------QDANYNVEkaQQGIVFLD 344
Cdd:COG1220  190 ssspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkearkiltqeeaAKLIdmdevkQEAIERAE--QNGIIFID 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 345 EVDKIGSvPGIHQLRDVGGEGVQQGLLKLLEGTivnvpeknsrklrgeTVQ-----VDTTNILFVASGAFNgldriISRr 419
Cdd:COG1220  268 EIDKIAS-RGGGSGPDVSREGVQRDLLPIVEGS---------------TVNtkygmVKTDHILFIAAGAFH-----VSK- 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 420 knekylgfgtPSNLgkgrraaaaadlanrsgesnthqdieekdrllrhveardliefgmIPEFVGRLPVVVPLHSLDEKT 499
Cdd:COG1220  326 ----------PSDL---------------------------------------------IPELQGRFPIRVELDSLTEED 350
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 500 LVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALE--RKT---GARGLRSIMEKLLLEPMFEVPNSDIVCVE 574
Cdd:COG1220  351 FVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEvnERTeniGARRLHTVMEKLLEDISFEAPDLSGKTVV 430

                 ....*....
gi 767983141 575 VDKEVVEGK 583
Cdd:COG1220  431 IDAAYVDEK 439
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
172-410 1.86e-33

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: 126.34  E-value: 1.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRiynnipanlrQQAEVEKQTSLTPRellqiagisphgnalgasmqqqvnqqi 251
Cdd:cd19498    5 IVSELDKYIIGQDEAKRAVAIALRNRWRR----------MQLPEELRDEVTPK--------------------------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 252 pqekrggevldsshddikleksNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLqdany 331
Cdd:cd19498   48 ----------------------NILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGYVGRDVESIIRDLV----- 100
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767983141 332 nvekaqQGIVFLDEVDKIGSVPGIHQlRDVGGEGVQQGLLKLLEGTIVNVpeknsrklrgETVQVDTTNILFVASGAFN 410
Cdd:cd19498  101 ------EGIVFIDEIDKIAKRGGSSG-PDVSREGVQRDLLPIVEGSTVST----------KYGPVKTDHILFIAAGAFH 162
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
172-583 2.21e-33

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: 133.02  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  172 IYNYLDKYVVGQSFAKKVLSVAVYNHYKRIynnipanlrqQAEVEKQTSLTPRellqiagisphgnalgasmqqqvnqqi 251
Cdd:TIGR00390   6 IVAELDKYIIGQDNAKKSVAIALRNRYRRS----------QLNEELKDEVTPK--------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  252 pqekrggevldsshddikleksNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVI--------- 322
Cdd:TIGR00390  49 ----------------------NILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGRDVESMVrdltdaavk 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  323 -------AKLLQDANYNVEK------------------------------------------------------------ 335
Cdd:TIGR00390 107 lvkeeaiEKVRDRAEELAEErivdvllppaknqwgqteqqqepesareafrkklregelddkeieidvsakmpsgieima 186
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  336 -----------------------------------------------------------AQQGIVFLDEVDKIgSVPGIH 356
Cdd:TIGR00390 187 ppgmeemtmqlqslfqnlggqkkkkrklkikdakkaliaeeaaklvdpeeikqeaidavEQSGIIFIDEIDKI-AKKGES 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  357 QLRDVGGEGVQQGLLKLLEGTIVNVPEKnsrklrgetvQVDTTNILFVASGAFNgldriISRrknekylgfgtPSNLgkg 436
Cdd:TIGR00390 266 SGADVSREGVQRDLLPIVEGSTVNTKYG----------MVKTDHILFIAAGAFQ-----LAK-----------PSDL--- 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  437 rraaaaadlanrsgesnthqdieekdrllrhveardliefgmIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQ 516
Cdd:TIGR00390 317 ------------------------------------------IPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYK 354
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767983141  517 ALFSMDKCELNVTEDALKAIARLA--LERKT---GARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGK 583
Cdd:TIGR00390 355 ALMKTEGVNIEFSDEAIKRIAELAynVNEKTeniGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKK 426
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
271-489 4.23e-32

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: 121.92  E-value: 4.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  271 EKSNILLLGPTGSGKTLLAQTLAKCLDV---PFAICDCTTLTQagyvgediESVIAKLLQDANYNVEKAQQG-------- 339
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  340 ----IVFLDEVDKIGSvpgihqlrdvggeGVQQGLLKLLEGTIVNVpeknsrklrGETVQVDTTNILFVASGAFNGLDRI 415
Cdd:pfam07724  74 kpysIVLIDEIEKAHP-------------GVQNDLLQILEGGTLTD---------KQGRTVDFKNTLFIMTGNFGSEKIS 131
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983141  416 ISRRknekylgfgtpsnlgkgrraaaaadlanrsgesnthqDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVV 489
Cdd:pfam07724 132 DASR-------------------------------------LGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
495-589 4.48e-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: 84.80  E-value: 4.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141   495 LDEKTLVQILTEPRNAVIPQYqalfSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVcVE 574
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGEL-KD 75
                           90
                   ....*....|....*
gi 767983141   575 VDKEVVEGKKEPGYI 589
Cdd:smart01086  76 GDTVVVDVDDGELVF 90
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
272-418 3.01e-16

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: 76.03  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 272 KSNILLLGPTGSGKTLLAQTLAKCL---DVPFAICDCTTLTQAGYVGEDIESVIAKLLQDAnynVEKAQQGIVFLDEVDK 348
Cdd:cd00009   19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL---AEKAKPGVLFIDEIDS 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 349 IgsvpgihqlrdvgGEGVQQGLLKLLEGtivnvpEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISR 418
Cdd:cd00009   96 L-------------SRGAQNALLRVLET------LNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
272-376 4.00e-16

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: 76.17  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 272 KSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEdIESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGS 351
Cdd:cd19481   26 PKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLL-SKYVGE-SEKNLRKIFERA----RRLAPCILFIDEIDAIGR 99
                         90       100
                 ....*....|....*....|....*
gi 767983141 352 VPGIHQLRDVGGEGVQQgLLKLLEG 376
Cdd:cd19481  100 KRDSSGESGELRRVLNQ-LLTELDG 123
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
275-376 3.32e-12

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: 63.77  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQaGYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGSVPG 354
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGES-EKRLRELFEAA----KKLAPCVIFIDEIDALAGSRG 74
                          90       100
                  ....*....|....*....|..
gi 767983141  355 IHQLRDvgGEGVQQGLLKLLEG 376
Cdd:pfam00004  75 SGGDSE--SRRVVNQLLTELDG 94
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
275-376 2.47e-11

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: 65.70  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEdIESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGsvPG 354
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYVGE-TEKNLREVFDKA----RGLAPCVLFIDEADALA--GK 265
                         90       100
                 ....*....|....*....|..
gi 767983141 355 IHQLRDVGGEGVQQGLLKLLEG 376
Cdd:COG0464  266 RGEVGDGVGRRVVNTLLTEMEE 287
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
495-566 4.30e-10

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: 56.26  E-value: 4.30e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767983141  495 LDEKTLVQILTEprnAVIPQYQALFSmDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVP 566
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEI 68
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
272-379 5.76e-09

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: 55.07  E-value: 5.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141   272 KSNILLLGPTGSGKTLLAQTLAKCLDVP---FAICDCTTLTQAGYVGEDIESVI--------AKLLQDANYNVEKAQQGI 340
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGgkkasgsgELRLRLALALARKLKPDV 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767983141   341 VFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIV 379
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
275-376 8.54e-09

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: 54.99  E-value: 8.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLtQAGYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGSVPG 354
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSI-VSKYLGES-EKNLREIFEEA----RSHAPSIIFIDEIDALAPKRE 110
                         90       100
                 ....*....|....*....|..
gi 767983141 355 IHQlRDVGGEGVQQgLLKLLEG 376
Cdd:cd19503  111 EDQ-REVERRVVAQ-LLTLMDG 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
275-351 2.26e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 53.09  E-value: 2.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAgYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGS 351
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK-YIGEG-ARNVREVFELA----REKAPSIIFIDEIDAIAA 185
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
274-418 6.23e-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: 48.83  E-value: 6.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  274 NILLLGPTGSGKTLLAQTLAKcldvpfAICDCTTLTQAGYvgEDIESviAKLLQDANYN-----------VEKAQQG-IV 341
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAA------ALSNRPVFYVQLT--RDTTE--EDLFGRRNIDpggaswvdgplVRAAREGeIA 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983141  342 FLDEVDKIGSVpgihqlrdvggegVQQGLLKLLEGTIVNVPEknsrklRGETVQVDTTNILFVASGafNGLDRIISR 418
Cdd:pfam07728  71 VLDEINRANPD-------------VLNSLLSLLDERRLLLPD------GGELVKAAPDGFRLIATM--NPLDRGLNE 126
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
431-578 8.38e-07

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 52.39  E-value: 8.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 431 SNLGkgrraaaAADLANRSGESNTHQDIEEK--DRLLRHVEardliefgmiPEFVGRLPVVVPLHSLDEKTLVQI----L 504
Cdd:COG0542  699 SNIG-------SELILDLAEDEPDYEEMKEAvmEELKKHFR----------PEFLNRIDEIIVFHPLSKEELRKIvdlqL 761
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 505 TEPRNAVIPQyqalfsmdKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPM------FEVPNSDIVCVEVDKE 578
Cdd:COG0542  762 KRLRKRLAER--------GITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLaeeilaGEIKEGDTITVDVDDG 833
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
275-374 1.51e-06

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: 48.49  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAgYVGEDiesviAKLLQDANYNVEKAQQGIVFLDEVDKIGSvpg 354
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEG-----ARLVRELFEMAREKAPSIIFIDEIDAIGA--- 110
                         90       100
                 ....*....|....*....|...
gi 767983141 355 ihQLRDVGGEG---VQQGLLKLL 374
Cdd:cd19502  111 --KRFDSGTGGdreVQRTMLELL 131
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
275-351 1.69e-06

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 48.55  E-value: 1.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEDiESVIAKLLQDANYNVEkaqqGIVFLDEVDKIGS 351
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGES-EEKIRELFDQAISNAP----CIVFIDEIDAITP 107
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
275-351 1.73e-06

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 48.12  E-value: 1.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEDiESVIAKLLQDANynveKAQQGIVFLDEVDKIGS 351
Cdd:cd19509   35 ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGES-EKIVRALFALAR----ELQPSIIFIDEIDSLLS 105
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
275-354 5.43e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 49.65  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFaicdcTTLTQAGYVgEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPG 354
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPF-----FTISGSDFV-EMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRG 261
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
275-350 1.10e-05

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: 46.07  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFaicdcttLTQAG------YVGediesVIAKLLQDANYNVEKAQQGIVFLDEVDK 348
Cdd:cd19501   40 VLLVGPPGTGKTLLAKAVAGEAGVPF-------FSISGsdfvemFVG-----VGASRVRDLFEQAKKNAPCIVFIDEIDA 107

                 ..
gi 767983141 349 IG 350
Cdd:cd19501  108 VG 109
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
275-351 3.69e-05

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 44.20  E-value: 3.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAgYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGS 351
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK-YVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLAP 100
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
275-347 4.77e-05

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 44.34  E-value: 4.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYvGEdiesviAKLLQDANYNV-EKAQQGIVFLDEVD 347
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GE------SQKLVAAVFSLaSKLQPSIIFIDEID 104
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
275-349 8.04e-05

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: 43.30  E-value: 8.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKI 349
Cdd:cd19524   36 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEG-EKLVRALFAVA----RELQPSIIFIDEVDSL 104
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
255-415 9.29e-05

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 43.70  E-value: 9.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 255 KRGGEVLDSSH---DDIK---LE-----------KSNILLL-GPTGSGKTLLAQTLAKCLDVPFA------ICDCTTL-- 308
Cdd:cd19500    2 KKARKVLDADHyglEDVKeriLEylavrklkgsmKGPILCLvGPPGVGKTSLGKSIARALGRKFVrislggVRDEAEIrg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 309 ---TqagYVGEdIESVIAKLLQDAnynveKAQQGIVFLDEVDKIGSvpgihqlrDVGGEGvQQGLLKLLEgtivnvPEKN 385
Cdd:cd19500   82 hrrT---YVGA-MPGRIIQALKKA-----GTNNPVFLLDEIDKIGS--------SFRGDP-ASALLEVLD------PEQN 137
                        170       180       190
                 ....*....|....*....|....*....|.
gi 767983141 386 SRKL-RGETVQVDTTNILFVASGafNGLDRI 415
Cdd:cd19500  138 STFSdHYLDVPFDLSKVLFIATA--NSLDTI 166
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
273-379 2.46e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 43.92  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 273 SNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTltqAGyVgEDIESVIAKllqdANYNVEKAQQGIVFLDEvdkigsv 352
Cdd:PRK13342  37 SSMILWGPPGTGKTTLARIIAGATDAPFEALSAVT---SG-V-KDLREVIEE----ARQRRSAGRRTILFIDE------- 100
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767983141 353 pgIH-----QlrdvggegvQQGLLKLLE-GTIV 379
Cdd:PRK13342 101 --IHrfnkaQ---------QDALLPHVEdGTIT 122
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
275-349 2.87e-04

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 42.04  E-value: 2.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLtQAGYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKI 349
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEI-MSKLAGES-ESNLRKAFEEA----EKNAPAIIFIDEIDAI 105
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
275-400 2.91e-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: 44.13  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLtQAGYVGEDiESVIAKLLQDANYNVEkaqqGIVFLDEVDKIGSvpg 354
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI-MSKYYGES-EERLREIFKEAEENAP----SIIFIDEIDAIAP--- 285
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767983141  355 ihQLRDVGGE---GVQQGLLKLLEGTivnvpeknsrKLRGETVQVDTTN 400
Cdd:TIGR01243 286 --KREEVTGEvekRVVAQLLTLMDGL----------KGRGRVIVIGATN 322
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
276-348 5.63e-04

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: 41.01  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 276 LLLGPTGSGKTLLAQTLAK----------CLDVPFAIC--DCTTLTQA--GYVGEDIESVIAKLLQDANYNVekaqqgiV 341
Cdd:cd19499   45 LFLGPTGVGKTELAKALAEllfgdednliRIDMSEYMEkhSVSRLIGAppGYVGYTEGGQLTEAVRRKPYSV-------V 117

                 ....*..
gi 767983141 342 FLDEVDK 348
Cdd:cd19499  118 LLDEIEK 124
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
275-354 7.99e-04

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 40.74  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEDiESVIAKLLQDANYNVEKAqqgiVFLDEVDKIGSVPG 354
Cdd:cd19522   36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGES-EKLVRLLFEMARFYAPTT----IFIDEIDSICSRRG 109
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
275-351 9.70e-04

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 40.74  E-value: 9.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTqAGYVGEDiESVIAKLlqdanYNVEKAQQ-GIVFLDEVDKIGS 351
Cdd:cd19525   58 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-EKMVRAL-----FSVARCKQpAVIFIDEIDSLLS 128
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
275-397 1.05e-03

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 40.55  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDV--PFAICDCTTLTQagYVGEDiESVIAKLLQDA--NYNVEKAQQG--IVFLDEVDK 348
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEILNK--YVGES-EANIRKLFADAeeEQRRLGANSGlhIIIFDEIDA 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767983141 349 IGSVPGIHQlrdvGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVD 397
Cdd:cd19504  115 ICKQRGSMA----GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKD 159
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
275-348 1.42e-03

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: 40.92  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTtltqagyvgEDIEsvIAKLLQDANYNVEKAQ---------QGIVFLDE 345
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFT---------PDLL--PSDILGTYIYDQQTGEfefrpgplfANVLLADE 102

                 ...
gi 767983141 346 VDK 348
Cdd:COG0714  103 INR 105
MCM8 cd17759
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a ...
271-382 1.48e-03

DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a complex with Mcm9 that is required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350665 [Multi-domain]  Cd Length: 289  Bit Score: 40.98  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 271 EKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVeKAQQGIVFLDEVDKIG 350
Cdd:cd17759   42 GDPHVLIVGDPGLGKSQMLQAACNIAPRGVYVCGNTTTTSGLTVTLTKDGRSGDFALEAGALV-LGDQGICGIDEFDKMG 120
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767983141 351 SvpgihqlrdvggegVQQGLLKLLEGTIVNVP 382
Cdd:cd17759  121 S--------------QHQALLEAMEQQSVSLA 138
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
271-349 1.58e-03

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: 39.42  E-value: 1.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767983141 271 EKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAgYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKI 349
Cdd:cd19527   25 KRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGES-EANVREVFQKA----RDAKPCVIFFDELDSL 97
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
270-353 1.65e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 39.53  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  270 LEKSNILLLGPTGSGKTL-----LAQTLAKCLDVPFAICDCTT--LTQagyvgeDIESVIAKLLQDANYNVEKAQQGIVF 342
Cdd:pfam00270  12 LEGRDVLVQAPTGSGKTLafllpALEALDKLDNGPQALVLAPTreLAE------QIYEELKKLGKGLGLKVASLLGGDSR 85
                          90
                  ....*....|.
gi 767983141  343 LDEVDKIGSVP 353
Cdd:pfam00270  86 KEQLEKLKGPD 96
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
273-354 2.59e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 40.60  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 273 SNILLLGPTGSGKTLLAQTLAKCL-------DVPFAIC--DC---TTLTQagyvgediesVIAKLLQDANYNVEKAQQG- 339
Cdd:COG1474   52 SNVLIYGPTGTGKTAVAKYVLEELeeeaeerGVDVRVVyvNCrqaSTRYR----------VLSRILEELGSGEDIPSTGl 121
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767983141 340 --------------------IVFLDEVDKIGSVPG 354
Cdd:COG1474  122 stdelfdrlyealderdgvlVVVLDEIDYLVDDEG 156
aroK PRK00131
shikimate kinase; Reviewed
270-300 3.11e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.02  E-value: 3.11e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767983141 270 LEKSNILLLGPTGSGKTLLAQTLAKCLDVPF 300
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
274-347 3.27e-03

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: 38.66  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983141 274 NILLLGPTGSGKTLLAQTLAKCLDVPFAIcdcTTLTQAGYVGEDIESVIAKLLQDANynveKAQQG-IVFLDEVD 347
Cdd:cd19512   24 NILFYGPPGTGKTLFAKKLALHSGMDYAI---MTGGDVAPMGREGVTAIHKVFDWAN----TSRRGlLLFVDEAD 91
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
275-378 3.52e-03

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 38.83  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  275 ILLLGPTGSGKTLLAQTLA---------KCLDVPFAICdCTTLTQAG--------------YVGEDIESVIAKLLqdany 331
Cdd:pfam05729   3 VILQGEAGSGKTTLLQKLAllwaqgklpQGFDFVFFLP-CRELSRSGnarsladllfsqwpEPAAPVSEVWAVIL----- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767983141  332 nvEKAQQGIVFLDEVDKIGSVPGIHQlrdvGGEGVQQGLLKLLEGTI 378
Cdd:pfam05729  77 --ELPERLLLILDGLDELVSDLGQLD----GPCPVLTLLSSLLRKKL 117
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
275-376 3.75e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 38.63  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPF-AICDCTTLTQagYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGSVP 353
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFiSVKGPELLSK--WVGES-EKAIREIFRKA----RQVAPCVIFFDEIDSIAPRR 102
                         90       100
                 ....*....|....*....|...
gi 767983141 354 GIHQLRDVGGEGVQQgLLKLLEG 376
Cdd:cd19529  103 GTTGDSGVTERVVNQ-LLTELDG 124
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
275-374 4.67e-03

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 39.75  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 275 ILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAgYVGEDiesviAKLLQDANYNVEKAQQGIVFLDEVDKIGSVpg 354
Cdd:PTZ00361 220 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQK-YLGDG-----PKLVRELFRVAEENAPSIVFIDEIDAIGTK-- 291
                         90       100
                 ....*....|....*....|.
gi 767983141 355 iHQLRDVGGEG-VQQGLLKLL 374
Cdd:PTZ00361 292 -RYDATSGGEKeIQRTMLELL 311
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
273-351 5.68e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.43  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141 273 SNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAgYVGEDiesviAKLLQDA-NYNVEKAqQGIVFLDEVDKIGS 351
Cdd:PRK03992 166 KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK-FIGEG-----ARLVRELfELAREKA-PSIIFIDEIDAIAA 238
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
275-376 5.69e-03

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 39.89  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983141  275 ILLLGPTGSGKTLLAQTLAKCLDVPF-AICDCTTLTQagYVGEDiESVIAKLLQDAnynvEKAQQGIVFLDEVDKIGSVP 353
Cdd:TIGR01243 490 VLLFGPPGTGKTLLAKAVATESGANFiAVRGPEILSK--WVGES-EKAIREIFRKA----RQAAPAIIFFDEIDAIAPAR 562
                          90       100
                  ....*....|....*....|...
gi 767983141  354 GIHQLRDVGGEGVQQgLLKLLEG 376
Cdd:TIGR01243 563 GARFDTSVTDRIVNQ-LLTEMDG 584
Zn-ribbon cd00656
C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit; The ...
104-132 7.55e-03

C-terminal zinc ribbon domain of RNA polymerase intrinsic transcript cleavage subunit; The homologous C-terminal zinc ribbon domains of subunits A12.2, Rpb9, and C11 in RNA Polymerases (Pol) I, II, and III, respectively are required for intrinsic transcript cleavage. TFS is a related archaeal protein that is involved in RNA cleavage by archaeal polymerase. These proteins have two zinc-binding beta-ribbon domains, N-terminal zinc ribbon (N-ribbon) and C-terminal zinc ribbon (C-ribbon). Transcription Factor IIS (TFIIS) domain III is homologous to the C-ribbon domain that stimulates the weak cleavage activity of Rpb9 for Pol II.


Pssm-ID: 259791  Cd Length: 45  Bit Score: 34.60  E-value: 7.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767983141 104 RCPKCGdlctHVETFV----------SSTRFVKCEKCHH 132
Cdd:cd00656    8 TCPKCG----HDEAYWwmlqtrsadePPTRFYKCTKCGH 42
RPB9 COG1594
DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]; ...
104-132 7.99e-03

DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]; DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441202 [Multi-domain]  Cd Length: 103  Bit Score: 36.46  E-value: 7.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767983141 104 RCPKCGdlctHVETFV----------SSTRFVKCEKCHH 132
Cdd:COG1594   64 ICPKCG----NDEAYWwlkqtrsadePETRFFRCTKCGH 98
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
274-292 9.83e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 38.87  E-value: 9.83e-03
                         10
                 ....*....|....*....
gi 767983141 274 NILLLGPTGSGKTLLAQTL 292
Cdd:COG0606  213 NLLMIGPPGSGKTMLARRL 231
 
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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