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Conserved domains on  [gi|504510796|ref|WP_014697898|]
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ATP-dependent Clp protease ATP-binding subunit ClpX [Bifidobacterium animalis]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
6-432 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 679.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   6 SYNDGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEENAK-DSRLEVLKLPKPSQIRDVLDQYVIGQNDAKR 84
Cdd:COG1219    3 GDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEeEAEEELKKLPKPKEIKAFLDEYVIGQERAKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  85 TLSVAVYNHFKRaqIERHDANAhrqfeqsgladsarsildplDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIV 164
Cdd:COG1219   83 VLSVAVYNHYKR--LNSGSKDD--------------------DDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 165 DATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTLVHV 244
Cdd:COG1219  141 DATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKS-ENPSITRDVSGEGVQQALLKILEGTVANV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 245 PVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWR-VNPIDEHEIYRQVNAEDLAEFGLLPEF 323
Cdd:COG1219  220 PPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKsKKEKDEGELLKQVEPEDLIKFGLIPEF 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 324 IGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETM 403
Cdd:COG1219  300 IGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVM 379
                        410       420
                 ....*....|....*....|....*....
gi 504510796 404 FELPNMDDVTEVVVNADCVTEGVPPQMVR 432
Cdd:COG1219  380 YELPSRKDVKKVVITKEVVEGKAKPILVY 408
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
6-432 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 679.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   6 SYNDGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEENAK-DSRLEVLKLPKPSQIRDVLDQYVIGQNDAKR 84
Cdd:COG1219    3 GDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEeEAEEELKKLPKPKEIKAFLDEYVIGQERAKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  85 TLSVAVYNHFKRaqIERHDANAhrqfeqsgladsarsildplDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIV 164
Cdd:COG1219   83 VLSVAVYNHYKR--LNSGSKDD--------------------DDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 165 DATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTLVHV 244
Cdd:COG1219  141 DATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKS-ENPSITRDVSGEGVQQALLKILEGTVANV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 245 PVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWR-VNPIDEHEIYRQVNAEDLAEFGLLPEF 323
Cdd:COG1219  220 PPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKsKKEKDEGELLKQVEPEDLIKFGLIPEF 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 324 IGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETM 403
Cdd:COG1219  300 IGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVM 379
                        410       420
                 ....*....|....*....|....*....
gi 504510796 404 FELPNMDDVTEVVVNADCVTEGVPPQMVR 432
Cdd:COG1219  380 YELPSRKDVKKVVITKEVVEGKAKPILVY 408
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
6-436 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 671.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   6 SYNDGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEENaKDSRLEVLKLPKPSQIRDVLDQYVIGQNDAKRT 85
Cdd:PRK05342   4 GDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREEL-KEEAVELKELPTPKEIKAHLDQYVIGQERAKKV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  86 LSVAVYNHFKRAqierhdanahrqfeqsgladsaRSILDPLDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVD 165
Cdd:PRK05342  83 LSVAVYNHYKRL----------------------RHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 166 ATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTLVHVP 245
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKS-ENPSITRDVSGEGVQQALLKILEGTVASVP 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 246 VDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWRVNPID--EHEIYRQVNAEDLAEFGLLPEF 323
Cdd:PRK05342 220 PQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKrtEGELLKQVEPEDLIKFGLIPEF 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 324 IGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETM 403
Cdd:PRK05342 300 IGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVM 379
                        410       420       430
                 ....*....|....*....|....*....|...
gi 504510796 404 FELPNMDDVTEVVVNADCVTEGVPPQMVRPEQR 436
Cdd:PRK05342 380 FELPSREDVEKVVITKEVVEGKAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
9-431 0e+00

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 522.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796    9 DGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEE-----NAKDSRLEVL--KLPKPSQIRDVLDQYVIGQND 81
Cdd:TIGR00382   5 NETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEElgtrkESKEYEEEFElsYLPTPKEIKAHLDEYVIGQEQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   82 AKRTLSVAVYNHFKRAQIERHDANAhrqfeqsgladsarsildplDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPF 161
Cdd:TIGR00382  85 AKKVLSVAVYNHYKRLNFEKNKKSD--------------------NGVELSKSNILLIGPTGSGKTLLAQTLARILNVPF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  162 IIVDATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTL 241
Cdd:TIGR00382 145 AIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKS-ENPSITRDVSGEGVQQALLKIIEGTV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  242 VHVPVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWRVNPIDEHEIYRQVNAEDLAEFGLLP 321
Cdd:TIGR00382 224 ANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKKSKEKADLLRQVEPEDLVKFGLIP 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  322 EFIGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEE 401
Cdd:TIGR00382 304 EFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLD 383
                         410       420       430
                  ....*....|....*....|....*....|
gi 504510796  402 TMFELPNMDDVTEVVVNADCVTEGVPPQMV 431
Cdd:TIGR00382 384 VMFDLPSLEDLEKVVITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
63-333 1.52e-134

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: 386.96  E-value: 1.52e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  63 PKPSQIRDVLDQYVIGQNDAKRTLSVAVYNHFKR--AQIERHDanahrqfeqsgladsarsildplDEVSVAKSNILLLG 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRirNNLKQKD-----------------------DDVELEKSNILLIG 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 141 PTGVGKTYLAQTLAKAMQVPFIIVDATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSM 220
Cdd:cd19497   58 PTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKS-ENPSI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 221 TRDVSGEGVQQALLKILEGTLVHVPVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWRV--N 298
Cdd:cd19497  137 TRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSekD 216
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 504510796 299 PIDEHEIYRQVNAEDLAEFGLLPEFIGRLPVVCTL 333
Cdd:cd19497  217 EKERDELLSKVEPEDLIKFGLIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
133-330 8.66e-40

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: 140.41  E-value: 8.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  133 KSNILLLGPTGVGKTYLAQTLAKAMQV---PFIIVDATSITEAGYVgddvemvlSRLLQAADGDV------------DRA 197
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSV--------SRLIGAPPGYVgyeeggqlteavRRK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  198 RYGIVYIDEVDKIARksgdntsmtrdvsgeGVQQALLKILEGTLVhvpvdgahRHKDGETVelDTSDILFICGGAFVGLD 277
Cdd:pfam07724  75 PYSIVLIDEIEKAHP---------------GVQNDLLQILEGGTL--------TDKQGRTV--DFKNTLFIMTGNFGSEK 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504510796  278 EIVSRRLGRHESgfgaswrvnpidehEIYRQVNAEDLAEFGLLPEFIGRLPVV 330
Cdd:pfam07724 130 ISDASRLGDSPD--------------YELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
336-420 8.02e-19

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: 80.95  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   336 LTVDDLKDVLTKPTNALLKQYQKlfsvDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETMFELP---NMDDV 412
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAE----KGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELIlsgELKDG 76

                   ....*...
gi 504510796   413 TEVVVNAD 420
Cdd:smart01086  77 DTVVVDVD 84
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
57-207 8.52e-05

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 43.61  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  57 LEVLKLPkpsQIRDVLDQYVigQNDAKRTLSVA--VYNHFKRAQIERHDANAHRQFEQSGLA----------DSARSI-- 122
Cdd:NF038214   1 LRQLKLP---GMARALEELA--EQAAREELSFEefLALLLEAELAERENRRIERRLKRARFPaaktledfdfTAAPGLdk 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 123 --------LDPLDEvsvaKSNILLLGPTGVGKTYLAQTLAKAMqvpfiivdatsiTEAGY------VGDDVEmvlsRLLQ 188
Cdd:NF038214  76 aqirelatLDFIER----AENVLLLGPPGTGKTHLAIALGYAA------------CRQGYrvrfttAADLVE----QLAQ 135
                        170       180
                 ....*....|....*....|....*
gi 504510796 189 A-ADGDVDR-----ARYGIVYIDEV 207
Cdd:NF038214 136 ArADGRLGRllrrlARYDLLIIDEL 160
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
6-432 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 679.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   6 SYNDGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEENAK-DSRLEVLKLPKPSQIRDVLDQYVIGQNDAKR 84
Cdd:COG1219    3 GDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEeEAEEELKKLPKPKEIKAFLDEYVIGQERAKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  85 TLSVAVYNHFKRaqIERHDANAhrqfeqsgladsarsildplDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIV 164
Cdd:COG1219   83 VLSVAVYNHYKR--LNSGSKDD--------------------DDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 165 DATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTLVHV 244
Cdd:COG1219  141 DATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKS-ENPSITRDVSGEGVQQALLKILEGTVANV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 245 PVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWR-VNPIDEHEIYRQVNAEDLAEFGLLPEF 323
Cdd:COG1219  220 PPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKsKKEKDEGELLKQVEPEDLIKFGLIPEF 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 324 IGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETM 403
Cdd:COG1219  300 IGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVM 379
                        410       420
                 ....*....|....*....|....*....
gi 504510796 404 FELPNMDDVTEVVVNADCVTEGVPPQMVR 432
Cdd:COG1219  380 YELPSRKDVKKVVITKEVVEGKAKPILVY 408
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
6-436 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 671.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   6 SYNDGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEENaKDSRLEVLKLPKPSQIRDVLDQYVIGQNDAKRT 85
Cdd:PRK05342   4 GDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREEL-KEEAVELKELPTPKEIKAHLDQYVIGQERAKKV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  86 LSVAVYNHFKRAqierhdanahrqfeqsgladsaRSILDPLDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVD 165
Cdd:PRK05342  83 LSVAVYNHYKRL----------------------RHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 166 ATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTLVHVP 245
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKS-ENPSITRDVSGEGVQQALLKILEGTVASVP 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 246 VDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWRVNPID--EHEIYRQVNAEDLAEFGLLPEF 323
Cdd:PRK05342 220 PQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKrtEGELLKQVEPEDLIKFGLIPEF 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 324 IGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETM 403
Cdd:PRK05342 300 IGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVM 379
                        410       420       430
                 ....*....|....*....|....*....|...
gi 504510796 404 FELPNMDDVTEVVVNADCVTEGVPPQMVRPEQR 436
Cdd:PRK05342 380 FELPSREDVEKVVITKEVVEGKAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
9-431 0e+00

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 522.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796    9 DGVQRCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEE-----NAKDSRLEVL--KLPKPSQIRDVLDQYVIGQND 81
Cdd:TIGR00382   5 NETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEElgtrkESKEYEEEFElsYLPTPKEIKAHLDEYVIGQEQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   82 AKRTLSVAVYNHFKRAQIERHDANAhrqfeqsgladsarsildplDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQVPF 161
Cdd:TIGR00382  85 AKKVLSVAVYNHYKRLNFEKNKKSD--------------------NGVELSKSNILLIGPTGSGKTLLAQTLARILNVPF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  162 IIVDATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSMTRDVSGEGVQQALLKILEGTL 241
Cdd:TIGR00382 145 AIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKS-ENPSITRDVSGEGVQQALLKIIEGTV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  242 VHVPVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWRVNPIDEHEIYRQVNAEDLAEFGLLP 321
Cdd:TIGR00382 224 ANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKKSKEKADLLRQVEPEDLVKFGLIP 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  322 EFIGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEE 401
Cdd:TIGR00382 304 EFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLD 383
                         410       420       430
                  ....*....|....*....|....*....|
gi 504510796  402 TMFELPNMDDVTEVVVNADCVTEGVPPQMV 431
Cdd:TIGR00382 384 VMFDLPSLEDLEKVVITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
63-333 1.52e-134

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: 386.96  E-value: 1.52e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  63 PKPSQIRDVLDQYVIGQNDAKRTLSVAVYNHFKR--AQIERHDanahrqfeqsgladsarsildplDEVSVAKSNILLLG 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRirNNLKQKD-----------------------DDVELEKSNILLIG 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 141 PTGVGKTYLAQTLAKAMQVPFIIVDATSITEAGYVGDDVEMVLSRLLQAADGDVDRARYGIVYIDEVDKIARKSgDNTSM 220
Cdd:cd19497   58 PTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKS-ENPSI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 221 TRDVSGEGVQQALLKILEGTLVHVPVDGAHRHKDGETVELDTSDILFICGGAFVGLDEIVSRRLGRHESGFGASWRV--N 298
Cdd:cd19497  137 TRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSekD 216
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 504510796 299 PIDEHEIYRQVNAEDLAEFGLLPEFIGRLPVVCTL 333
Cdd:cd19497  217 EKERDELLSKVEPEDLIKFGLIPEFVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
65-424 1.81e-58

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 197.99  E-value: 1.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  65 PSQIRDVLDQYVIGQNDAKRTLSVAVYNHFKRAQierhdanahrqfeqsgLADSARsildplDEVsVAKsNILLLGPTGV 144
Cdd:PRK05201   6 PREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQ----------------LPEELR------DEV-TPK-NILMIGPTGV 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 145 GKTYLAQTLAKAMQVPFIIVDATSITEAGYVGDDVE------------MVLS----------------RLLQA------- 189
Cdd:PRK05201  62 GKTEIARRLAKLANAPFIKVEATKFTEVGYVGRDVEsiirdlveiavkMVREekrekvrekaeeaaeeRILDAllppakn 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 190 ------ADGDVDRAR----------------------------------------------------------------- 198
Cdd:PRK05201 142 nwgeeeEKEEISATRqkfrkklregelddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkea 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 199 ----------------------------YGIVYIDEVDKIARKSGDNTSmtrDVSGEGVQQALLKILEGTLV---HVPVd 247
Cdd:PRK05201 222 rkilieeeaaklidmeeikqeaierveqNGIVFIDEIDKIAARGGSSGP---DVSREGVQRDLLPLVEGSTVstkYGMV- 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 248 gahrhkdgetvelDTSDILFICGGAFvgldeivsrrlgrHESgfgaswrvNPIDeheiyrqvnaedlaefgLLPEFIGRL 327
Cdd:PRK05201 298 -------------KTDHILFIASGAF-------------HVS--------KPSD-----------------LIPELQGRF 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 328 PVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALErgV-------GARGLRSIIESILE 400
Cdd:PRK05201 327 PIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQ--VnekteniGARRLHTVMEKLLE 404
                        490       500
                 ....*....|....*....|....
gi 504510796 401 ETMFELPNMDDvTEVVVNADCVTE 424
Cdd:PRK05201 405 DISFEAPDMSG-ETVTIDAAYVDE 427
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
65-424 1.05e-54

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 188.33  E-value: 1.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  65 PSQIRDVLDQYVIGQNDAKRTLSVAVYNHFKRAQierhdanahrqfeqsgLADSARsildplDEVsVAKsNILLLGPTGV 144
Cdd:COG1220    6 PREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQ----------------LPEELR------DEI-TPK-NILMIGPTGV 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 145 GKTYLAQTLAKAMQVPFIIVDATSITEAGYVGDDVE----------------------------MVLSRLL--------- 187
Cdd:COG1220   62 GKTEIARRLAKLANAPFIKVEATKFTEVGYVGRDVEsmirdlveiavkmvreekmekvrekaeeAAEERILdlllpppkk 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 188 --------------QAADGDVDRAR------------------------------------------------------- 198
Cdd:COG1220  142 kagsnnpfeeeeeeEEEEEEISRTRekfrkklregelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkk 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 199 ---------------------------------------YGIVYIDEVDKIARKSGDNTSmtrDVSGEGVQQALLKILEG 239
Cdd:COG1220  222 kkkrkvkvkearkiltqeeaaklidmdevkqeaieraeqNGIIFIDEIDKIASRGGGSGP---DVSREGVQRDLLPIVEG 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 240 TLV---HVPVdgahrhkdgetvelDTSDILFICGGAFvgldeivsrrlgrHESgfgaswrvNPIDeheiyrqvnaedlae 316
Cdd:COG1220  299 STVntkYGMV--------------KTDHILFIAAGAF-------------HVS--------KPSD--------------- 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 317 fgLLPEFIGRLPVVCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALErgV-------GAR 389
Cdd:COG1220  329 --LIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFE--VnerteniGAR 404
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 504510796 390 GLRSIIESILEETMFELPNMDDVTeVVVNADCVTE 424
Cdd:COG1220  405 RLHTVMEKLLEDISFEAPDLSGKT-VVIDAAYVDE 438
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
65-424 1.73e-46

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: 166.14  E-value: 1.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   65 PSQIRDVLDQYVIGQNDAKRTLSVAVYNHFKRAQIERhdanahrqfeqsgladsarsildPLDEVSVAKsNILLLGPTGV 144
Cdd:TIGR00390   3 PREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNE-----------------------ELKDEVTPK-NILMIGPTGV 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  145 GKTYLAQTLAKAMQVPFIIVDATSITEAGYVGDDVE-------------------------------------------- 180
Cdd:TIGR00390  59 GKTEIARRLAKLANAPFIKVEATKFTEVGYVGRDVEsmvrdltdaavklvkeeaiekvrdraeelaeerivdvllppakn 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  181 --------------------------------------------------------MVLSRLLQAADGDVDRAR------ 198
Cdd:TIGR00390 139 qwgqteqqqepesareafrkklregelddkeieidvsakmpsgieimappgmeemtMQLQSLFQNLGGQKKKKRklkikd 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  199 -----------------------------YGIVYIDEVDKIARKsgdNTSMTRDVSGEGVQQALLKILEGTLVHVpvdga 249
Cdd:TIGR00390 219 akkaliaeeaaklvdpeeikqeaidaveqSGIIFIDEIDKIAKK---GESSGADVSREGVQRDLLPIVEGSTVNT----- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  250 hrhKDGetvELDTSDILFICGGAFvgldeivsrRLGRhesgfgaswrvnPIDeheiyrqvnaedlaefgLLPEFIGRLPV 329
Cdd:TIGR00390 291 ---KYG---MVKTDHILFIAAGAF---------QLAK------------PSD-----------------LIPELQGRFPI 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  330 VCTLGELTVDDLKDVLTKPTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALE-----RGVGARGLRSIIESILEETMF 404
Cdd:TIGR00390 327 RVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNvnektENIGARRLHTVLERLLEDISF 406
                         490       500
                  ....*....|....*....|
gi 504510796  405 ELPNMdDVTEVVVNADCVTE 424
Cdd:TIGR00390 407 EAPDL-SGQNITIDADYVSK 425
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
64-273 6.17e-43

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: 149.45  E-value: 6.17e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  64 KPSQIRDVLDQYVIGQNDAKRTLSVAVYNHFKRAQIERhdanahrqfeqsgladsarsilDPLDEVSvaKSNILLLGPTG 143
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPE----------------------ELRDEVT--PKNILMIGPTG 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 144 VGKTYLAQTLAKAMQVPFIIVDATSITEAGYVGDDVEMVLSRLLQaadgdvdraryGIVYIDEVDKIARKSGdntSMTRD 223
Cdd:cd19498   57 VGKTEIARRLAKLAGAPFIKVEATKFTEVGYVGRDVESIIRDLVE-----------GIVFIDEIDKIAKRGG---SSGPD 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504510796 224 VSGEGVQQALLKILEGTLV---HVPVdgahrhkdgetvelDTSDILFICGGAF 273
Cdd:cd19498  123 VSREGVQRDLLPIVEGSTVstkYGPV--------------KTDHILFIAAGAF 161
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
133-330 8.66e-40

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: 140.41  E-value: 8.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  133 KSNILLLGPTGVGKTYLAQTLAKAMQV---PFIIVDATSITEAGYVgddvemvlSRLLQAADGDV------------DRA 197
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSV--------SRLIGAPPGYVgyeeggqlteavRRK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  198 RYGIVYIDEVDKIARksgdntsmtrdvsgeGVQQALLKILEGTLVhvpvdgahRHKDGETVelDTSDILFICGGAFVGLD 277
Cdd:pfam07724  75 PYSIVLIDEIEKAHP---------------GVQNDLLQILEGGTL--------TDKQGRTV--DFKNTLFIMTGNFGSEK 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504510796  278 EIVSRRLGRHESgfgaswrvnpidehEIYRQVNAEDLAEFGLLPEFIGRLPVV 330
Cdd:pfam07724 130 ISDASRLGDSPD--------------YELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
336-420 8.02e-19

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: 80.95  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   336 LTVDDLKDVLTKPTNALLKQYQKlfsvDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETMFELP---NMDDV 412
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAE----KGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELIlsgELKDG 76

                   ....*...
gi 504510796   413 TEVVVNAD 420
Cdd:smart01086  77 DTVVVDVD 84
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
132-239 1.54e-17

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: 79.25  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 132 AKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGdDVEMVLSRLLQAAdgdvDRARYGIVYIDEVDKIA 211
Cdd:cd19481   25 LPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVG-ESEKNLRKIFERA----RRLAPCILFIDEIDAIG 98
                         90       100
                 ....*....|....*....|....*...
gi 504510796 212 RKSGdntSMTRDVSGEGVQQALLKILEG 239
Cdd:cd19481   99 RKRD---SSGESGELRRVLNQLLTELDG 123
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
13-49 1.32e-15

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


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 70.26  E-value: 1.32e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 504510796   13 RCTFCGKSEHEVHRLVAGA-GVAICDECIGLCVQILSE 49
Cdd:pfam06689   2 RCSFCGKSEDEVKKLIAGPnGVYICDECVELCYEILEE 39
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
136-287 3.61e-15

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: 71.86  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEaGYVGDDVEMVLSRLLQAadgdvDRARYGIVYIDEVDKIARKSG 215
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRLRELFEAA-----KKLAPCVIFIDEIDALAGSRG 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504510796  216 DNTsmtrDVSGEGVQQALLKILEGtlvhvpvdgahrhkdgetVELDTSDILFICGGAFVG-LDEIVSRRLGRH 287
Cdd:pfam00004  75 SGG----DSESRRVVNQLLTELDG------------------FTSSNSKVIVIAATNRPDkLDPALLGRFDRI 125
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
13-50 7.47e-15

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


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 67.98  E-value: 7.47e-15
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 504510796    13 RCTFCGKSEHEVHRLVAGAGVAICDECIGLCVQILSEE 50
Cdd:smart00994   2 RCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
133-238 1.63e-14

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 70.64  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 133 KSNILLLGPTGVGKTYLAQTLAKA---MQVPFIIVDATSITEAGYVGDDVEMVLSRLLQAAdgdVDRARYGIVYIDEVDK 209
Cdd:cd00009   19 PKNLLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL---AEKAKPGVLFIDEIDS 95
                         90       100
                 ....*....|....*....|....*....
gi 504510796 210 IARksgdntsmtrdvsgeGVQQALLKILE 238
Cdd:cd00009   96 LSR---------------GAQNALLRVLE 109
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
136-239 1.29e-12

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: 69.17  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGdDVEMVLSRLLQAADGDVDraryGIVYIDEVDKIARKSG 215
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYVG-ETEKNLREVFDKARGLAP----CVLFIDEADALAGKRG 267
                         90       100
                 ....*....|....*....|....
gi 504510796 216 DntsmTRDVSGEGVQQALLKILEG 239
Cdd:COG0464  268 E----VGDGVGRRVVNTLLTEMEE 287
clpC CHL00095
Clp protease ATP binding subunit
67-406 1.03e-11

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 67.00  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  67 QIRDVLDQYVIGQNDAkrtlSVAVYNHFKRAQIerhdanahrqfeqsGLADSARSIldpldevsvakSNILLLGPTGVGK 146
Cdd:CHL00095 502 HMEETLHKRIIGQDEA----VVAVSKAIRRARV--------------GLKNPNRPI-----------ASFLFSGPTGVGK 552
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 147 TYLAQTLAKAM---QVPFIIVDATSITE-----------AGYVGDDVemvlSRLLQAAdgdVDRARYGIVYIDEVDKiAR 212
Cdd:CHL00095 553 TELTKALASYFfgsEDAMIRLDMSEYMEkhtvskligspPGYVGYNE----GGQLTEA---VRKKPYTVVLFDEIEK-AH 624
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 213 KSGDNTsmtrdvsgegvqqaLLKILEgtlvhvpvDGAHRHKDGETVELDTSDILFIcggafvglDEIVSRRLGRHESGFG 292
Cdd:CHL00095 625 PDIFNL--------------LLQILD--------DGRLTDSKGRTIDFKNTLIIMT--------SNLGSKVIETNSGGLG 674
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 293 ASWRVNPIDEHEiYRQVNA---EDLAEFgLLPEFIGRLPVVCTLGELTVDDLKDVLtkptNALLKQYQKLFSVDGVTLTF 369
Cdd:CHL00095 675 FELSENQLSEKQ-YKRLSNlvnEELKQF-FRPEFLNRLDEIIVFRQLTKNDVWEIA----EIMLKNLFKRLNEQGIQLEV 748
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 504510796 370 TDAAVEAIASTALERGVGARGLRSIIESILEETMFEL 406
Cdd:CHL00095 749 TERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEE 785
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
336-407 6.68e-11

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, 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: 58.19  E-value: 6.68e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504510796  336 LTVDDLKDVLTKptnALLKQYQKLFSvDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILEETMFELP 407
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEI 68
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
64-209 8.43e-11

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: 60.65  E-value: 8.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  64 KPSQIRDVLDQYVIGQNDAKRTLSVAVynhfKRAQierhdanahrqfeqSGLADSARSILdpldevsvaksNILLLGPTG 143
Cdd:cd19499    1 KLLNLEERLHERVVGQDEAVKAVSDAI----RRAR--------------AGLSDPNRPIG-----------SFLFLGPTG 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 144 VGKTYLAQTLAKAM---QVPFIIVDATSITEA-----------GYVGDDVEMVLSrllqaadGDVDRARYGIVYIDEVDK 209
Cdd:cd19499   52 VGKTELAKALAELLfgdEDNLIRIDMSEYMEKhsvsrligappGYVGYTEGGQLT-------EAVRRKPYSVVLLDEIEK 124
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
136-239 7.04e-09

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 56.94  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDVEMVlsRLLqaadgdVDRARY---GIVYIDEVDKIAR 212
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK-YIGEGARNV--REV------FELAREkapSIIFIDEIDAIAA 185
                         90       100
                 ....*....|....*....|....*....
gi 504510796 213 KSGDNTSmtrdvSGEG--VQQALLKILEG 239
Cdd:COG1222  186 RRTDDGT-----SGEVqrTVNQLLAELDG 209
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
45-400 1.15e-08

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 57.40  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  45 QILSEENAKdsrleVLKLPkpsqirDVLDQYVIGQNDAKRTLSVAVynhfKRAQierhdanahrqfeqSGLADSARsild 124
Cdd:COG0542  531 KLLEGEREK-----LLNLE------EELHERVIGQDEAVEAVADAI----RRSR--------------AGLKDPNR---- 577
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 125 PldevsvaksnI---LLLGPTGVGKTYLAQTLAKAMqvpF------IIVDATSITEA-----------GYVGDD-----V 179
Cdd:COG0542  578 P----------IgsfLFLGPTGVGKTELAKALAEFL---FgdedalIRIDMSEYMEKhsvsrligappGYVGYEeggqlT 644
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 180 EMVlsrllqaadgdvdRAR-YGIVYIDEVDKiARksgdntsmtRDvsgegVQQALLKILEgtlvhvpvDGahRHKDGE-- 256
Cdd:COG0542  645 EAV-------------RRRpYSVVLLDEIEK-AH---------PD-----VFNILLQVLD--------DG--RLTDGQgr 686
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 257 ------TVELDTSDIlficggafvGLDEIVSRRLgrhesgfgaswrvNPIDEHEIYRQVNAEDLAEFglLPEFIGRLPVV 330
Cdd:COG0542  687 tvdfrnTIIIMTSNI---------GSELILDLAE-------------DEPDYEEMKEAVMEELKKHF--RPEFLNRIDEI 742
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 331 CTLGELTVDDLKDVltkpTNALLKQYQKLFSVDGVTLTFTDAAVEAIASTALERGVGARGLRSIIESILE 400
Cdd:COG0542  743 IVFHPLSKEELRKI----VDLQLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELE 808
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
136-225 2.83e-08

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 53.06  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDvEMVLSRLLQAAdgdvDRARYGIVYIDEVDKIA--RK 213
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGES-EKNLREIFEEA----RSHAPSIIFIDEIDALApkRE 110
                         90
                 ....*....|..
gi 504510796 214 SGDNTSMTRDVS 225
Cdd:cd19503  111 EDQREVERRVVA 122
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
136-249 4.46e-08

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: 52.29  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDvEMVLSRLLQaadgdvdRARYG---IVYIDEVDKIAR 212
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK-YVGES-ERAVREIFQ-------KARQAapcIIFFDEIDSLAP 100
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504510796 213 KSGDNTSMTrdvSGEGVQQALLKILEG--TLVHVPVDGA 249
Cdd:cd19511  101 RRGQSDSSG---VTDRVVSQLLTELDGieSLKGVVVIAA 136
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
136-250 9.24e-08

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 51.64  E-value: 9.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgyVGDDVEMVLSRLLQAADGDVDraryGIVYIDEVDKIARKsg 215
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSG--VSGESEEKIRELFDQAISNAP----CIVFIDEIDAITPK-- 108
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504510796 216 dNTSMTRDVSGEGVQQaLLKILEGtLVHVPVDGAH 250
Cdd:cd19518  109 -RESAQREMERRIVSQ-LLTCMDE-LNNEKTAGGP 140
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
132-220 1.82e-07

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: 50.89  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 132 AKSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAGYvGDDVEMV-----LSRLLQAAdgdvdrarygIVYIDE 206
Cdd:cd19520   34 PPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GESQKLVaavfsLASKLQPS----------IIFIDE 102
                         90
                 ....*....|....*.
gi 504510796 207 VDKI--ARKSGDNTSM 220
Cdd:cd19520  103 IDSFlrQRSSTDHEAT 118
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
136-241 2.67e-07

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: 50.04  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDVEMV-----LSRLLQAAdgdvdrarygIVYIDEVDKI 210
Cdd:cd19509   35 ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGESEKIVralfaLARELQPS----------IIFIDEIDSL 103
                         90       100       110
                 ....*....|....*....|....*....|...
gi 504510796 211 --ARKSGDNTSMTRdvsgegVQQALLKILEGTL 241
Cdd:cd19509  104 lsERGSGEHEASRR------VKTEFLVQMDGVL 130
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
133-239 2.98e-07

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 49.73  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 133 KSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDVEMVLSRLLQAAdgdvdRARYGIVYIDEVDKIAR 212
Cdd:cd19526   27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVRDLFSRAQ-----SAKPCILFFDEFDSIAP 100
                         90       100
                 ....*....|....*....|....*...
gi 504510796 213 KSG-DNTSMTRDVsgegVQQaLLKILEG 239
Cdd:cd19526  101 KRGhDSTGVTDRV----VNQ-LLTQLDG 123
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
133-213 3.35e-07

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 49.68  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   133 KSNILLLGPTGVGKTYLAQTLAKAMQVP---FIIVDATSITEAGYVGDDVEMVLSRLL-----QAADGDVDRARY---GI 201
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgeLRLRLALALARKlkpDV 81
                           90
                   ....*....|..
gi 504510796   202 VYIDEVDKIARK 213
Cdd:smart00382  82 LILDEITSLLDA 93
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
136-236 3.58e-07

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 52.34  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDVEMVLSRLLQAadgdvDRARYGIVYIDEVDKIARKSG 215
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVRDMFEQA-----KKAAPCIIFIDEIDAVGRQRG 261
                         90       100
                 ....*....|....*....|.
gi 504510796 216 DNTSMTRDVSGEGVQQALLKI 236
Cdd:PRK10733 262 AGLGGGHDEREQTLNQMLVEM 282
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
135-212 1.23e-06

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: 47.67  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  135 NILLLGPTGVGKTYLAQTLAKAM--QVPFIIVDATSITEAGYVGD-DVEMVLSRLlqaADGDVDRA--RYGIVYIDEVDK 209
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsnRPVFYVQLTRDTTEEDLFGRrNIDPGGASW---VDGPLVRAarEGEIAVLDEINR 77

                  ...
gi 504510796  210 IAR 212
Cdd:pfam07728  78 ANP 80
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
136-215 3.82e-06

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 46.84  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGddveMVLSRLLQAADGDVDRARyGIVYIDEVDKIARKSG 215
Cdd:cd19501   40 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVG----VGASRVRDLFEQAKKNAP-CIVFIDEIDAVGRKRG 113
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
136-237 5.39e-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: 46.56  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDVEMVlSRLLQAADgdvdRARYGIVYIDEVDKI-ARKS 214
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGARLV-RELFEMAR----EKAPSIIFIDEIDAIgAKRF 113
                         90       100
                 ....*....|....*....|...
gi 504510796 215 GDNTSMTRDvsgegVQQALLKIL 237
Cdd:cd19502  114 DSGTGGDRE-----VQRTMLELL 131
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
136-227 6.07e-06

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: 46.52  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDVEMVlsRLLqaadgdVDRARY---GIVYIDEVDKIA- 211
Cdd:cd19522   36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGESEKLV--RLL------FEMARFyapTTIFIDEIDSICs 106
                         90
                 ....*....|....*..
gi 504510796 212 -RKSGDNTSMTRDVSGE 227
Cdd:cd19522  107 rRGTSEEHEASRRVKSE 123
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
136-222 6.39e-06

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 46.00  E-value: 6.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDVEMVlsRLLQAadgdVDRARY-GIVYIDEVDKI--AR 212
Cdd:cd19524   36 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEGEKLV--RALFA----VARELQpSIIFIDEVDSLlsER 108
                         90
                 ....*....|
gi 504510796 213 KSGDNTSMTR 222
Cdd:cd19524  109 SEGEHEASRR 118
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
72-400 7.67e-06

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 48.30  E-value: 7.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  72 LDQYVIGQNDAKRtlsvAVYNHFKRAQierhdanahrqfeqSGLADSARSIldpldevsvakSNILLLGPTGVGKTYLAQ 151
Cdd:PRK10865 566 LHHRVIGQNEAVE----AVSNAIRRSR--------------AGLSDPNRPI-----------GSFLFLGPTGVGKTELCK 616
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 152 TLAKAM---QVPFIIVDATSITEAGYVgddvemvlSRLLQAADG------------DVDRARYGIVYIDEVDKiarksgd 216
Cdd:PRK10865 617 ALANFMfdsDDAMVRIDMSEFMEKHSV--------SRLVGAPPGyvgyeeggylteAVRRRPYSVILLDEVEK------- 681
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 217 ntsmtrdvSGEGVQQALLKIL-EGTLvhvpVDGAHRHKD-GETVELDTSDIlficggafvGLDEIVSRrlgrhesgFGAs 294
Cdd:PRK10865 682 --------AHPDVFNILLQVLdDGRL----TDGQGRTVDfRNTVVIMTSNL---------GSDLIQER--------FGE- 731
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 295 wrvnpIDEHEIYRQVnaEDLAEFGLLPEFIGRLPVVCT---LGELTVDDLKDVltkptnALLKQYQKLfSVDGVTLTFTD 371
Cdd:PRK10865 732 -----LDYAHMKELV--LGVVSHNFRPEFINRIDEVVVfhpLGEQHIASIAQI------QLQRLYKRL-EERGYEIHISD 797
                        330       340
                 ....*....|....*....|....*....
gi 504510796 372 AAVEAIASTALERGVGARGLRSIIESILE 400
Cdd:PRK10865 798 EALKLLSENGYDPVYGARPLKRAIQQQIE 826
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
136-237 1.45e-05

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 47.07  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDVEMVLsrllqaadgDVDR-ARY---GIVYIDEVDKIA 211
Cdd:PTZ00454 182 VLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQK-YLGEGPRMVR---------DVFRlAREnapSIIFIDEVDSIA 251
                         90       100
                 ....*....|....*....|....*..
gi 504510796 212 RKSGD-NTSMTRDvsgegVQQALLKIL 237
Cdd:PTZ00454 252 TKRFDaQTGADRE-----VQRILLELL 273
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
134-219 2.12e-05

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 44.85  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 134 SNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDvEMVLSRLLQAAdgdvDRARYGIVYIDEVDKIARK 213
Cdd:cd19521   41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFAMA----RENKPSIIFIDEVDSLCGT 114

                 ....*.
gi 504510796 214 SGDNTS 219
Cdd:cd19521  115 RGEGES 120
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
136-216 3.16e-05

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: 44.59  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDVEMV-----LSRLLQAAdgdvdrarygIVYIDEVDKI 210
Cdd:cd19525   58 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEGEKMVralfsVARCKQPA----------VIFIDEIDSL 126

                 ....*.
gi 504510796 211 ARKSGD 216
Cdd:cd19525  127 LSQRGE 132
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
136-239 3.91e-05

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: 46.05  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDvEMVLSRLLQAADGDVDraryGIVYIDEVDKIARKSG 215
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGES-EERLREIFKEAEENAP----SIIFIDEIDAIAPKRE 288
                          90       100
                  ....*....|....*....|....
gi 504510796  216 DntsMTRDVSGEGVQQaLLKILEG 239
Cdd:TIGR01243 289 E---VTGEVEKRVVAQ-LLTLMDG 308
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
135-163 4.25e-05

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 45.87  E-value: 4.25e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 504510796 135 NILLLGPTGVGKTYLAQTL---AKAMQV-----PFII 163
Cdd:COG1221  132 HTLILGPTGVGKSFFAELMyeyAIEIGVlpedaPFVV 168
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
53-233 4.69e-05

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: 45.67  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796   53 KDSRLEVLKLPKPSQIRDVLDQY-------VIGQNDAKRTLSVAVYNHFKRAQIerhdanahrqFEQSGladsarsILDP 125
Cdd:TIGR01243 425 MKDFMEALKMVEPSAIREVLVEVpnvrwsdIGGLEEVKQELREAVEWPLKHPEI----------FEKMG-------IRPP 487
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  126 ldevsvakSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDD---VEMVLSRLLQAADgdvdraryGIV 202
Cdd:TIGR01243 488 --------KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL-SKWVGESekaIREIFRKARQAAP--------AII 550
                         170       180       190
                  ....*....|....*....|....*....|.
gi 504510796  203 YIDEVDKIARKSGdnTSMTRDVSGEGVQQAL 233
Cdd:TIGR01243 551 FFDEIDAIAPARG--ARFDTSVTDRIVNQLL 579
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
134-207 6.20e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 45.08  E-value: 6.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504510796 134 SNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSiteAGyVGDdvemvLSRLLQAADGDVDRARYGIVYIDEV 207
Cdd:PRK13342  37 SSMILWGPPGTGKTTLARIIAGATDAPFEALSAVT---SG-VKD-----LREVIEEARQRRSAGRRTILFIDEI 101
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
72-212 7.76e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.35  E-value: 7.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  72 LDQYvIGQNDAKRTLSVAVynhfkraqierhdanahrqfeqsglaDSARSILDPLDEVsvaksniLLLGPTGVGKTYLAQ 151
Cdd:PRK00080  24 LDEF-IGQEKVKENLKIFI--------------------------EAAKKRGEALDHV-------LLYGPPGLGKTTLAN 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504510796 152 TLAKAMQVPFIIVDATSITEAGyvgdDVEMVLSRLlqaADGDVdrarygiVYIDEVDKIAR 212
Cdd:PRK00080  70 IIANEMGVNIRITSGPALEKPG----DLAAILTNL---EEGDV-------LFIDEIHRLSP 116
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
57-207 8.52e-05

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 43.61  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  57 LEVLKLPkpsQIRDVLDQYVigQNDAKRTLSVA--VYNHFKRAQIERHDANAHRQFEQSGLA----------DSARSI-- 122
Cdd:NF038214   1 LRQLKLP---GMARALEELA--EQAAREELSFEefLALLLEAELAERENRRIERRLKRARFPaaktledfdfTAAPGLdk 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 123 --------LDPLDEvsvaKSNILLLGPTGVGKTYLAQTLAKAMqvpfiivdatsiTEAGY------VGDDVEmvlsRLLQ 188
Cdd:NF038214  76 aqirelatLDFIER----AENVLLLGPPGTGKTHLAIALGYAA------------CRQGYrvrfttAADLVE----QLAQ 135
                        170       180
                 ....*....|....*....|....*
gi 504510796 189 A-ADGDVDR-----ARYGIVYIDEV 207
Cdd:NF038214 136 ArADGRLGRllrrlARYDLLIIDEL 160
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
136-236 1.54e-04

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 42.11  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSIteagyvgddvemvLSRLLQAADGDV----DRARYG---IVYIDEVD 208
Cdd:cd19528   30 VLFYGPPGCGKTLLAKAIANECQANFISVKGPEL-------------LTMWFGESEANVrdifDKARAAapcVLFFDELD 96
                         90       100
                 ....*....|....*....|....*...
gi 504510796 209 KIARKSGDNTSMTRDVSGEGVQQALLKI 236
Cdd:cd19528   97 SIAKARGGNIGDAGGAADRVINQILTEM 124
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
132-156 2.01e-04

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.85  E-value: 2.01e-04
                         10        20
                 ....*....|....*....|....*
gi 504510796 132 AKSNILLLGPTGVGKTYLAQTLAKA 156
Cdd:COG1484   98 RGENLILLGPPGTGKTHLAIALGHE 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 ...
136-249 2.51e-04

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 41.65  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDDvEMVLSRLLQAADGDVDraryGIVYIDEVDKIARKSG 215
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGES-ESNLRKAFEEAEKNAP----AIIFIDEIDAIAPKRE 110
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504510796 216 DNTSmtrDVSGEGVQQaLLKILEG--TLVHVPVDGA 249
Cdd:cd19519  111 KTHG---EVERRIVSQ-LLTLMDGlkQRAHVIVMAA 142
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
120-207 2.76e-04

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 43.01  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 120 RSILDPLDEVSVAKSNILLLGPTGVGKTYLAQTLAKAMQvPFIIVDATSITEAGYVGDDVEMVLSRLLQAADGDvdrary 199
Cdd:COG1373    7 RKILDKLLKLLDNRKAVVITGPRQVGKTTLLKQLAKELE-NILYINLDDPRLRALAEEDPDDLLEALKELYPGK------ 79

                 ....*...
gi 504510796 200 GIVYIDEV 207
Cdd:COG1373   80 TYLFLDEI 87
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
133-225 2.78e-04

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: 41.34  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 133 KSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDVEMVLSRLLQAADgdvdrARYGIVYIDEVDKIAR 212
Cdd:cd19527   26 RSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEANVREVFQKARD-----AKPCVIFFDELDSLAP 99
                         90
                 ....*....|....*..
gi 504510796 213 KSGDNTS----MTRDVS 225
Cdd:cd19527  100 SRGNSGDsggvMDRVVS 116
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
136-239 3.94e-04

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 40.94  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITeAGYVGDD---VEMVLSRLLQAADgdvdraryGIVYIDEVDKIAR 212
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGESekaIREIFRKARQVAP--------CVIFFDEIDSIAP 100
                         90       100
                 ....*....|....*....|....*..
gi 504510796 213 KSGdnTSMTRDVSGEGVQQaLLKILEG 239
Cdd:cd19529  101 RRG--TTGDSGVTERVVNQ-LLTELDG 124
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
133-269 4.21e-04

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: 41.00  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 133 KSNILLL-GPTGVGKTYLAQTLAKAMQVPFIIVDATSIT-EA-------GYVGddveMVLSRLLQAadgdVDRARYG--I 201
Cdd:cd19500   36 KGPILCLvGPPGVGKTSLGKSIARALGRKFVRISLGGVRdEAeirghrrTYVG----AMPGRIIQA----LKKAGTNnpV 107
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504510796 202 VYIDEVDKIARKS-GDNTSmtrdvsgegvqqALLKILEGTLVHVPVDgahRHKDgetVELDTSDILFIC 269
Cdd:cd19500  108 FLLDEIDKIGSSFrGDPAS------------ALLEVLDPEQNSTFSD---HYLD---VPFDLSKVLFIA 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
136-237 5.71e-04

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 42.07  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDVEMVlSRLLQAADGDVDraryGIVYIDEVDKIARKSG 215
Cdd:PTZ00361 220 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQK-YLGDGPKLV-RELFRVAEENAP----SIVFIDEIDAIGTKRY 293
                         90       100
                 ....*....|....*....|...
gi 504510796 216 DNTSmtrdvSGEG-VQQALLKIL 237
Cdd:PTZ00361 294 DATS-----GGEKeIQRTMLELL 311
AAA_18 pfam13238
AAA domain;
136-205 7.58e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 39.33  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDAtsITEAGYVGDD----------VEMVLSRLLQAADGDVDRARYGIVYID 205
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDL--ALENGLVLGDdpetreskrlDEDKLDRLLDLLEENAALEEGGNLIID 78
AAA_22 pfam13401
AAA domain;
133-210 8.93e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  133 KSNILLLGPTGVGKTYLAQTLAK---AMQVPFIIVDATS--------------ITEAGYVGDDVEMVLSRLLQAAdgdVD 195
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPSgtspkdllrallraLGLPLSGRLSKEELLAALQQLL---LA 81
                          90
                  ....*....|....*
gi 504510796  196 RARYGIVYIDEVDKI 210
Cdd:pfam13401  82 LAVAVVLIIDEAQHL 96
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
136-168 1.36e-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: 40.54  E-value: 1.36e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATS 168
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFTP 66
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
120-219 1.40e-03

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 39.39  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 120 RSILDPLDEVSVAKS-------NILLLGPTGVGKTYLAQTLAKAMQVPFIIVDATSITEAgYVGDDvEMVLSRLLQaadg 192
Cdd:cd19530   10 MSILRPIKRPDIYKAlgidlptGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNK-YVGES-ERAVRQVFQ---- 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 504510796 193 dvdRARYG---IVYIDEVDKIARKSGDNTS 219
Cdd:cd19530   84 ---RARASapcVIFFDEVDALVPKRGDGGS 110
aroK PRK00131
shikimate kinase; Reviewed
133-166 3.87e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 38.25  E-value: 3.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 504510796 133 KSNILLLGPTGVGKTYLAQTLAKAMQVPFIIVDA 166
Cdd:PRK00131   4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDH 37
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
136-219 5.26e-03

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 36.71  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKamqvpfiivDATSITEAGYVGDDVEMVLSRLLQAADGDVDRarygIVYIDEVDKIARKSG 215
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAE---------QALLSDEPVIFISFLDTILEAIEDLIEEKKLD----IIIIDSLSSLARASQ 67

                 ....
gi 504510796 216 DNTS 219
Cdd:cd01120   68 GDRS 71
AAA_17 pfam13207
AAA domain;
139-290 5.57e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 37.22  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796  139 LGPTGVGKTYLAQTLAKAMQVPFIivdatsitEAGyvgdDV--EMVLSRLLQAADGDVDRAryGIVYIDEVDKIARKSGD 216
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHI--------SAG----DLlrEEAKERGLVEDRDEMRKL--PLEPQKELQKLAAERIA 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504510796  217 NTSMTRDVsgegvqqallkILEGTLVHVPVDGAHRHKDGETV-ELDTSDILFIcggaFVGLDEIVSRRLGRHESG 290
Cdd:pfam13207  67 EEAGEGGV-----------IVDGHPRIKTPAGYLPGLPVEVLrELKPDAIILL----EADPEEILERRLKDRTRG 126
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
136-236 6.00e-03

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 37.47  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 136 ILLLGPTGVGKTYLAQTLAKAMQV--PfIIVDATSITEAgYVGDDVEMVlsRLLqAADGDVDRARYG------IVYIDEV 207
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLNAreP-KIVNGPEILNK-YVGESEANI--RKL-FADAEEEQRRLGansglhIIIFDEI 112
                         90       100       110
                 ....*....|....*....|....*....|..
gi 504510796 208 DKIARKSGDntsmTRDVSGEG---VQQALLKI 236
Cdd:cd19504  113 DAICKQRGS----MAGSTGVHdtvVNQLLSKI 140
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
133-162 6.63e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 38.84  E-value: 6.63e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 504510796 133 KSNILLL-GPTGVGKTYLAQTLAKAMQVPFI 162
Cdd:COG0466  351 KGPILCLvGPPGVGKTSLGKSIARALGRKFV 381
PRK09183 PRK09183
transposase/IS protein; Provisional
135-158 6.96e-03

transposase/IS protein; Provisional


Pssm-ID: 181681  Cd Length: 259  Bit Score: 38.15  E-value: 6.96e-03
                         10        20
                 ....*....|....*....|....*
gi 504510796 135 NILLLGPTGVGKTYLAQTLA-KAMQ 158
Cdd:PRK09183 104 NIVLLGPSGVGKTHLAIALGyEAVR 128
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
107-218 7.55e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 38.29  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 107 HRQFEQSGLADSARSILDplDEVSvakSNILLLGPTGVGKTYLAQTLAKAMQ---------VPFIIVDA----------T 167
Cdd:COG1474   30 HREEEIEELASALRPALR--GERP---SNVLIYGPTGTGKTAVAKYVLEELEeeaeergvdVRVVYVNCrqastryrvlS 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504510796 168 SITEAGYVGDDV-------EMVLSRLLQAadgDVDRARYGIVYIDEVDKIARKSGDNT 218
Cdd:COG1474  105 RILEELGSGEDIpstglstDELFDRLYEA---LDERDGVLVVVLDEIDYLVDDEGDDL 159
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
134-224 9.42e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 38.27  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504510796 134 SNILLLGPTGVGKTYLAQTLAKAmqvpfiiVDATSITEAG------YVGDDVEMV-----LSRllqaadgdvDRARyGIV 202
Cdd:PRK03992 166 KGVLLYGPPGTGKTLLAKAVAHE-------TNATFIRVVGselvqkFIGEGARLVrelfeLAR---------EKAP-SII 228
                         90       100
                 ....*....|....*....|...
gi 504510796 203 YIDEVDKI-ARKSGDNTSMTRDV 224
Cdd:PRK03992 229 FIDEIDAIaAKRTDSGTSGDREV 251
 
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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