NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2298853246|emb|CAI0951169|]
View 

ATP-dependent Clp protease ATP-binding subunit ClpA [Serratia ficaria]

Protein Classification

ATP-dependent Clp protease ATP-binding subunit( domain architecture ID 11485160)

ClpA/ClpB family ATP-dependent Clp protease ATP-binding subunit is a component of the Clp chaperone-protease complex that is involved in protein degradation and disaggregation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
1-759 0e+00

ATP-dependent Clp protease ATP-binding subunit; Provisional


:

Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 1604.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQP 80
Cdd:PRK11034    1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  81 TLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQ-APNAENPVNE 159
Cdd:PRK11034   81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQsSDPGSQPNSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 160 EQSGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 239
Cdd:PRK11034  161 EQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 240 ADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 319
Cdd:PRK11034  241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 320 STTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAID 399
Cdd:PRK11034  321 STTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 400 VIDEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAG 479
Cdd:PRK11034  401 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 480 LGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSV 559
Cdd:PRK11034  481 LGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 560 VLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNSTDAMEEIKKVFTPEF 639
Cdd:PRK11034  561 LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEF 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 640 RNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANEL 719
Cdd:PRK11034  641 RNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 2298853246 720 LFGSLVDGGSVKVELDKDKKQLTYHFLSAQKRKADegAVH 759
Cdd:PRK11034  721 LFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAE--AAH 758
 
Name Accession Description Interval E-value
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
1-759 0e+00

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 1604.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQP 80
Cdd:PRK11034    1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  81 TLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQ-APNAENPVNE 159
Cdd:PRK11034   81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQsSDPGSQPNSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 160 EQSGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 239
Cdd:PRK11034  161 EQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 240 ADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 319
Cdd:PRK11034  241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 320 STTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAID 399
Cdd:PRK11034  321 STTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 400 VIDEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAG 479
Cdd:PRK11034  401 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 480 LGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSV 559
Cdd:PRK11034  481 LGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 560 VLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNSTDAMEEIKKVFTPEF 639
Cdd:PRK11034  561 LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEF 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 640 RNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANEL 719
Cdd:PRK11034  641 RNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 2298853246 720 LFGSLVDGGSVKVELDKDKKQLTYHFLSAQKRKADegAVH 759
Cdd:PRK11034  721 LFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAE--AAH 758
ClpA TIGR02639
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ...
2-734 0e+00

ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274241 [Multi-domain]  Cd Length: 730  Bit Score: 1118.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPaSEEERDTQPT 81
Cdd:TIGR02639   1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  82 LSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDePGQAPNAENPVNEEQ 161
Cdd:TIGR02639  80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKD-DGKDQLGEEAGKEEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 162 SGgEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMAD 241
Cdd:TIGR02639 159 KG-QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 242 CTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGST 321
Cdd:TIGR02639 238 AKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGST 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 322 TYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVI 401
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 402 DEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLG 481
Cdd:TIGR02639 398 DEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLG 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 482 HDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVL 561
Cdd:TIGR02639 478 DPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLL 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 562 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVqQDNSTDAMEE-IKKVFTPEFR 640
Cdd:TIGR02639 558 LDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFG-GENRESKSLKaIKKLFSPEFR 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 641 NRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:TIGR02639 637 NRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEIL 716
                         730
                  ....*....|....
gi 2298853246 721 FGSLVDGGSVKVEL 734
Cdd:TIGR02639 717 FGKLKKGGSVKISL 730
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
2-738 0e+00

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 859.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--AAREALEACTVDLAALRQELEAFIEQTTPTLPASEeerdtQ 79
Cdd:COG0542     6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGegLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSG-----Q 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  80 PTLS--FQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFIShGTRKDEPGQAPNAEnpv 157
Cdd:COG0542    81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALE-ELRGGSRVTSQNPE--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 158 neeqsGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 237
Cdd:COG0542   157 -----SKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 238 VMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DQNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIR 316
Cdd:COG0542   232 SLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARGELR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 317 VIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDK 396
Cdd:COG0542   311 CIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 397 AIDVIDEAGARSRLMPVSK------------------------------------------------------------- 415
Cdd:COG0542   391 AIDLIDEAAARVRMEIDSKpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarweaekeli 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 416 -------------------------------------RKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKML 458
Cdd:COG0542   471 eeiqelkeeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHER 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 459 VFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM-DIE--LLRFDMSEYMERHTVSRLIGA 535
Cdd:COG0542   551 VIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEKHSVSRLIGA 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 536 PPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRE-TERK 614
Cdd:COG0542   631 PPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELiLDLA 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 615 SIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGY 694
Cdd:COG0542   711 EDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGY 790
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 2298853246 695 DRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKDK 738
Cdd:COG0542   791 DPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
448-649 6.33e-88

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: 274.44  E-value: 6.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 448 LRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DIELLRFDMSEYM 524
Cdd:cd19499     2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 525 ERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTT 604
Cdd:cd19499    82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2298853246 605 NAgvreterksiglvqqdnstdameeikkvFTPEFRNRLDNIIWF 649
Cdd:cd19499   162 NH----------------------------FRPEFLNRIDEIVVF 178
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
485-646 7.92e-79

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: 250.19  E-value: 7.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 485 KPVGSFLFAGPTGVGKTEVTVQLAKAMDI---ELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVL 561
Cdd:pfam07724   1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 562 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNST---DAMEEIKKVFTPE 638
Cdd:pfam07724  81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELlkeEVMDLLKKGFIPE 160

                  ....*...
gi 2298853246 639 FRNRLDNI 646
Cdd:pfam07724 161 FLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
652-741 5.12e-27

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: 105.22  E-value: 5.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  652 LSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVK 731
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
                           90
                   ....*....|
gi 2298853246  732 VELDKDKKQL 741
Cdd:smart01086  81 VDVDDGELVF 90
 
Name Accession Description Interval E-value
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
1-759 0e+00

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 1604.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQP 80
Cdd:PRK11034    1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  81 TLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQ-APNAENPVNE 159
Cdd:PRK11034   81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQsSDPGSQPNSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 160 EQSGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 239
Cdd:PRK11034  161 EQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 240 ADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 319
Cdd:PRK11034  241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 320 STTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAID 399
Cdd:PRK11034  321 STTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 400 VIDEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAG 479
Cdd:PRK11034  401 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 480 LGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSV 559
Cdd:PRK11034  481 LGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 560 VLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNSTDAMEEIKKVFTPEF 639
Cdd:PRK11034  561 LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEF 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 640 RNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANEL 719
Cdd:PRK11034  641 RNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 2298853246 720 LFGSLVDGGSVKVELDKDKKQLTYHFLSAQKRKADegAVH 759
Cdd:PRK11034  721 LFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAE--AAH 758
ClpA TIGR02639
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ...
2-734 0e+00

ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274241 [Multi-domain]  Cd Length: 730  Bit Score: 1118.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPaSEEERDTQPT 81
Cdd:TIGR02639   1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  82 LSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDePGQAPNAENPVNEEQ 161
Cdd:TIGR02639  80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKD-DGKDQLGEEAGKEEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 162 SGgEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMAD 241
Cdd:TIGR02639 159 KG-QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 242 CTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGST 321
Cdd:TIGR02639 238 AKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGST 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 322 TYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVI 401
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 402 DEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLG 481
Cdd:TIGR02639 398 DEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLG 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 482 HDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVL 561
Cdd:TIGR02639 478 DPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLL 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 562 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVqQDNSTDAMEE-IKKVFTPEFR 640
Cdd:TIGR02639 558 LDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFG-GENRESKSLKaIKKLFSPEFR 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 641 NRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:TIGR02639 637 NRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEIL 716
                         730
                  ....*....|....
gi 2298853246 721 FGSLVDGGSVKVEL 734
Cdd:TIGR02639 717 FGKLKKGGSVKISL 730
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
2-738 0e+00

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 859.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--AAREALEACTVDLAALRQELEAFIEQTTPTLPASEeerdtQ 79
Cdd:COG0542     6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGegLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSG-----Q 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  80 PTLS--FQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFIShGTRKDEPGQAPNAEnpv 157
Cdd:COG0542    81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALE-ELRGGSRVTSQNPE--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 158 neeqsGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 237
Cdd:COG0542   157 -----SKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 238 VMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DQNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIR 316
Cdd:COG0542   232 SLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARGELR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 317 VIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDK 396
Cdd:COG0542   311 CIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 397 AIDVIDEAGARSRLMPVSK------------------------------------------------------------- 415
Cdd:COG0542   391 AIDLIDEAAARVRMEIDSKpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarweaekeli 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 416 -------------------------------------RKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKML 458
Cdd:COG0542   471 eeiqelkeeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHER 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 459 VFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM-DIE--LLRFDMSEYMERHTVSRLIGA 535
Cdd:COG0542   551 VIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEKHSVSRLIGA 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 536 PPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRE-TERK 614
Cdd:COG0542   631 PPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELiLDLA 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 615 SIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGY 694
Cdd:COG0542   711 EDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGY 790
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 2298853246 695 DRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKDK 738
Cdd:COG0542   791 DPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
17-738 0e+00

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 686.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  17 AREHRHEFMTVEHLLLALL--SNPAAREALEACTVDLAALRQELEAFIEQttptLPA-SEEERDTQPTLSFQRVLQRAVF 93
Cdd:TIGR03346  16 ALGRDHQQIEPEHLLKALLdqEGGLARPLLQKAGVNVGALRQALEKELER----LPKvSGPGGQVYLSPDLNRLLNLAEK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  94 HVQSSGRSEVSGANVLVAIfSEQESQAAYLLRKHDVSRLDVVNFIsHGTRKDEPGQAPNAENpvneeqsgGEDRMENFTT 173
Cdd:TIGR03346  92 LAQKRGDEFISSEHLLLAL-LDDKGTLGKLLKEAGATADALEAAI-NAVRGGQKVTDANAED--------QYEALEKYAR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 174 NLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTLYSLDIGSLL 253
Cdd:TIGR03346 162 DLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGALI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 254 AGTKYRGDFEKRFKALLKQLE-QDQNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEK 332
Cdd:TIGR03346 242 AGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGA-MDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 333 DRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRL-- 410
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMei 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 411 --MP---------------------------------------------------------------------------- 412
Cdd:TIGR03346 401 dsKPeeldeldrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasiqgiqqikeeieqvrle 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 413 --VSKR-------------------------------------KKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGD 453
Cdd:TIGR03346 481 leQAERegdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 454 RLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM-DIE--LLRFDMSEYMERHTVS 530
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLfDSEdaMVRIDMSEYMEKHSVA 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 531 RLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRE 610
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 611 TERKSIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLS 690
Cdd:TIGR03346 721 IQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 2298853246 691 VKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKDK 738
Cdd:TIGR03346 801 EAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
clpC CHL00095
Clp protease ATP binding subunit
1-739 0e+00

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 671.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   1 MLNQELelslnmafarAREHRHEFMTVEHLLLALL--SNPAAREALEACTVDLAALRQELEAFIEQTTpTLPASEeerdT 78
Cdd:CHL00095   14 MLSQEE----------ARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKIIGRGT-GFVAVE----I 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  79 QPTLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVS----RLDVVNFISHGTRKDEPGQAPNAE 154
Cdd:CHL00095   79 PFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDlskiRSLILNLIGEIIEAILGAEQSRSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 155 NPVNEEqsggedrmenFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGD 234
Cdd:CHL00095  159 TPTLEE----------FGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 235 VPEVMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGK 314
Cdd:CHL00095  229 VPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGA-IDAANILKPALARGE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 315 IRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLP 394
Cdd:CHL00095  308 LQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLP 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 395 DKAIDVIDEAGARSRLM-----------------------------------------------------------PVSK 415
Cdd:CHL00095  388 DKAIDLLDEAGSRVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeEKRL 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 416 RKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGP 495
Cdd:CHL00095  468 EVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGP 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 496 TGVGKTEVTVQLAKAM---DIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDV 572
Cdd:CHL00095  548 TGVGKTELTKALASYFfgsEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDI 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 573 FNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGL------VQQDNSTDAM------EEIKKVFTPEFR 640
Cdd:CHL00095  628 FNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLgfelseNQLSEKQYKRlsnlvnEELKQFFRPEFL 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 641 NRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:CHL00095  708 NRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVL 787
                         810
                  ....*....|....*....
gi 2298853246 721 FGSLVDGGSVKVELDKDKK 739
Cdd:CHL00095  788 SFKIKPGDIIIVDVNDEKE 806
VI_ClpV1 TIGR03345
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ...
2-720 0e+00

type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274528 [Multi-domain]  Cd Length: 852  Bit Score: 556.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPA--AREALEACTVDLAALRQELEAFIEQttptLPASEEERdtq 79
Cdd:TIGR03345   1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDK----LPRGNTRT--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  80 PTLS--FQRVLQRAvFHVQSS--GRSEVSGANVLVAIFSEQE-----SQAAYLLRKHDVSRLD-VVNFISHGTRkdEPGQ 149
Cdd:TIGR03345  74 PVFSphLVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPElrrllGSISPELAKIDREALReALPALVEGSA--EASA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 150 APNAENPVNEEQS-GGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAW 228
Cdd:TIGR03345 151 AAADAAPAGAAAGaAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLAL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 229 RIVQGDVPEVMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DQNSILFIDEIHTIIGAGAASgGQVDAANLIK 307
Cdd:TIGR03345 231 RIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAsPQPIILFIDEAHTLIGAGGQA-GQGDAANLLK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 308 PLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKY 387
Cdd:TIGR03345 310 PALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 388 INDRHLPDKAIDVIDEAGARSRL--------------------------------------------------------- 410
Cdd:TIGR03345 390 IPGRQLPDKAVSLLDTACARVALsqnatpaaledlrrriaaleleldalereaalgadhderlaelraelaaleaelaal 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 411 --------------------------MPVSKRKKT------------------------VNVADIESVVARIARIPEKTV 440
Cdd:TIGR03345 470 earwqqekelveailalraeleadadAPADDDDALraqlaeleaalasaqgeeplvfpeVDAQAVAEVVADWTGIPVGRM 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 441 SASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DIELLR 517
Cdd:TIGR03345 550 VRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyggEQNLIT 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 518 FDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRN 597
Cdd:TIGR03345 630 INMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKN 709
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 598 VILVMTTNAGvreTERKSIGLVQQDNSTDA-------MEEIKKVFTPEFRNRLdNIIWFNHLSTEVIQQVVDKFIVELQA 670
Cdd:TIGR03345 710 TVILLTSNAG---SDLIMALCADPETAPDPeallealRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIAR 785
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2298853246 671 QLDAK-GVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:TIGR03345 786 RLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
2-737 0e+00

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 545.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAA--REALEACTVDLAALRQEleafIEQTTPTLPASE-EERDT 78
Cdd:PRK10865    6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGsvRPLLTSAGINAGQLRTD----INQALSRLPQVEgTGGDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  79 QPTLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFsEQESQAAYLLRKHDVSRLDVVNFIShgtrkdepgQAPNAENpVN 158
Cdd:PRK10865   82 QPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIE---------QMRGGES-VN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 159 EEqsGGEDR---MENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDV 235
Cdd:PRK10865  151 DQ--GAEDQrqaLKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 236 PEVMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDQNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGK 314
Cdd:PRK10865  229 PEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 315 IRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLP 394
Cdd:PRK10865  308 LHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLP 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 395 DKAIDVIDEAGARSRLMPVSK---------------------RKKT---------------------------------- 419
Cdd:PRK10865  388 DKAIDLIDEAASSIRMQIDSKpeeldrldrriiqlkleqqalMKESdeaskkrldmlneelsdkerqyseleeewkaeka 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 420 ---------------------------------------------------------------VNVADIESVVARIARIP 436
Cdd:PRK10865  468 slsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTGIP 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 437 EKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DI 513
Cdd:PRK10865  548 VSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDD 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 514 ELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKA 593
Cdd:PRK10865  628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 594 DFRNVILVMTTNAGVRETERKSIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLD 673
Cdd:PRK10865  708 DFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLE 787
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2298853246 674 AKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKD 737
Cdd:PRK10865  788 ERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
448-649 6.33e-88

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: 274.44  E-value: 6.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 448 LRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DIELLRFDMSEYM 524
Cdd:cd19499     2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 525 ERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTT 604
Cdd:cd19499    82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2298853246 605 NAgvreterksiglvqqdnstdameeikkvFTPEFRNRLDNIIWF 649
Cdd:cd19499   162 NH----------------------------FRPEFLNRIDEIVVF 178
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
485-646 7.92e-79

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: 250.19  E-value: 7.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 485 KPVGSFLFAGPTGVGKTEVTVQLAKAMDI---ELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVL 561
Cdd:pfam07724   1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 562 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNST---DAMEEIKKVFTPE 638
Cdd:pfam07724  81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELlkeEVMDLLKKGFIPE 160

                  ....*...
gi 2298853246 639 FRNRLDNI 646
Cdd:pfam07724 161 FLGRLPII 168
AAA_lid_9 pfam17871
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
349-451 1.17e-35

AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465544 [Multi-domain]  Cd Length: 104  Bit Score: 130.30  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 349 TPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRLmpvSKRKKTVNVADIESV 428
Cdd:pfam17871   1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRL---SQESKPEELEDLERE 77
                          90       100
                  ....*....|....*....|...
gi 2298853246 429 VARIARIPEKTVSASDRDVLRSL 451
Cdd:pfam17871  78 LAKLEIEKEALEREQDFEKAERL 100
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
652-732 2.93e-28

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: 108.26  E-value: 2.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 652 LSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVK 731
Cdd:pfam10431   1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80

                  .
gi 2298853246 732 V 732
Cdd:pfam10431  81 V 81
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
652-741 5.12e-27

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: 105.22  E-value: 5.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  652 LSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVK 731
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
                           90
                   ....*....|
gi 2298853246  732 VELDKDKKQL 741
Cdd:smart01086  81 VDVDDGELVF 90
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
188-343 6.00e-22

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: 92.98  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 188 IGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPevmadctLYSLDIGSLLAGTKYRGDFE-KRF 266
Cdd:cd00009     1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2298853246 267 KALLKQLEQDQNSILFIDEIHTIigAGAASGGQVDAAN-LIKPLLSSGKIRVIGSTTYqefSNIFEKDRALARRFQKI 343
Cdd:cd00009    74 RLLFELAEKAKPGVLFIDEIDSL--SRGAQNALLRVLEtLNDLRIDRENVRVIGATNR---PLLGDLDRALYDRLDIR 146
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
210-343 9.80e-17

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 77.25  E-value: 9.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWrivqgdvpevMADCTLYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAK----------ELGAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2298853246 290 IGAGAASGGQV--DAANLIKPLL-----SSGKIRVIGSTTYqefsnIFEKDRALARRFQKI 343
Cdd:pfam00004  70 AGSRGSGGDSEsrRVVNQLLTELdgftsSNSKVIVIAATNR-----PDKLDPALLGRFDRI 125
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
26-402 2.85e-16

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: 81.50  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  26 TVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRSEVSG 105
Cdd:COG0464     5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 106 ANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQAPNAENPVNEEQSGGEDRmENFTTNLNQLARVGGID 185
Cdd:COG0464    85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEE-ELLELREAILDDLGGLE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 186 PLIGRDPELERAIQVLCRRRKNNP-------LLVGESGVGKTAIAEGLAwRIVQGDvpevmadctLYSLDIGSLLAgtKY 258
Cdd:COG0464   164 EVKEELRELVALPLKRPELREEYGlppprglLLYGPPGTGKTLLARALA-GELGLP---------LIEVDLSDLVS--KY 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 259 RGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDA----------ANLIKPLLssgkirVIGsTTYQeFSN 328
Cdd:COG0464   232 VGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvntlltemEELRSDVV------VIA-ATNR-PDL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 329 IfekDRALARRFQ-KIDITEPTPEETVQIINGLKTKYEAHHDVRYTA------------------KAIRAAVELSVKYIN 389
Cdd:COG0464   304 L---DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEElaeateglsgadirnvvrRAALQALRLGREPVT 380
                         410
                  ....*....|...
gi 2298853246 390 DRHLpDKAIDVID 402
Cdd:COG0464   381 TEDL-LEALERED 392
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
460-616 1.06e-13

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: 69.10  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 460 FGQDQAIEALTEAIKmsraglghdRKPVGSFLFAGPTGVGKTEVTVQLAKA---MDIELLRFDMSEYMERHTVSRLIgap 536
Cdd:cd00009     1 VGQEEAIEALREALE---------LPPPKNLLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAELF--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 537 pgyvGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGtltdnNGRKADFRNVILVMTTNAGVRETERKSI 616
Cdd:cd00009    69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATNRPLLGDLDRAL 139
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
205-343 1.33e-12

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: 65.86  E-value: 1.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  205 RKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCT-----LYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNS 279
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileeVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2298853246  280 ILFIDEIHTIIGAGAASGGQVDA-ANLIKPLLSSGKIRVIGSTTYQEFSnifeKDRALARRFQKI 343
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILTTNDEKDL----GPALLRRRFDRR 141
Clp_N pfam02861
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ...
13-63 6.20e-12

Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.


Pssm-ID: 460724 [Multi-domain]  Cd Length: 53  Bit Score: 61.00  E-value: 6.20e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2298853246  13 AFARAREHRHEFMTVEHLLLALLSNP--AAREALEACTVDLAALRQELEAFIE 63
Cdd:pfam02861   1 AQELARALGHQYIGTEHLLLALLEEDdgLAARLLKKAGVDLDALREAIEKLLG 53
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
210-343 1.14e-11

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: 63.46  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19481    30 LLYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 290 IGAGAASGGQVDAA-------NLIKPLLSSGKIRVIGSTtyqefSNIFEKDRALAR--RFQKI 343
Cdd:cd19481    98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAAT-----NRPDLLDPALLRpgRFDEV 155
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
489-605 1.27e-11

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: 62.70  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 489 SFLFAGPTGVGKTEVTVQLAKAMD-----IELLRFDMSEymerhtvSRLIGappGYVGYDQGGLLTDAVI----KHPHsV 559
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrpvfYVQLTRDTTE-------EDLFG---RRNIDPGGASWVDGPLvraaREGE-I 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2298853246 560 VLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGR---KADFRNVILVMTTN 605
Cdd:pfam07728  70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
207-403 8.85e-11

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 62.98  E-value: 8.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 207 NNPLLVGESGVGKTAIAEGLAWRIvqgDVPevmadctLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQnSILFIDEI 286
Cdd:COG1223    36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARRAP-CVIFFDEF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 287 HTIigagaasGGQVDAANL---IKPLLSS---------GKIRVIGSTTYQEFSnifekDRALARRFQ-KIDITEPTPEET 353
Cdd:COG1223   103 DAI-------AKDRGDQNDvgeVKRVVNAllqeldglpSGSVVIAATNHPELL-----DSALWRRFDeVIEFPLPDKEER 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2298853246 354 VQI----INGLKTKYEAHHD--------------VRYTAKAIRAAVELSVKYINDRHLpDKAIDVIDE 403
Cdd:COG1223   171 KEIlelnLKKFPLPFELDLKklakkleglsgadiEKVLKTALKKAILEDREKVTKEDL-EEALKQRKE 237
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
464-605 1.45e-10

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: 60.37  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 464 QAIEALTEAIKMSRAGLGHDRkpvgSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHtvsrligappGYVGYD 543
Cdd:cd19481     7 EAVEAPRRGSRLRRYGLGLPK----GILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY----------VGESEK 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2298853246 544 QGGLLTDAVIKHPHSVVLLDEIEKAHPD------------VFNLLLQVMDNGTLTDnngrkadfrNVILVMTTN 605
Cdd:cd19481    73 NLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
184-438 5.20e-09

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 58.48  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 184 IDPLigRDPELERAIQVLCRRRKnnpLLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFE 263
Cdd:COG1222    95 ELPL--KNPELFRKYGIEPPKGV---LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGA 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 264 KRFKALLKQLEQDQNSILFIDEIHTIIGA--GAASGGQVDaaNLIKPLL-------SSGKIRVIGSTTYQEfsnifEKDR 334
Cdd:COG1222   158 RNVREVFELAREKAPSIIFIDEIDAIAARrtDDGTSGEVQ--RTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 335 ALAR--RF-QKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAvELSVKYIndrhlpdKAIdvIDEAGARSrlm 411
Cdd:COG1222   231 ALLRpgRFdRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTE-GFSGADL-------KAI--VTEAGMFA--- 297
                         250       260
                  ....*....|....*....|....*..
gi 2298853246 412 pVSKRKKTVNVADIESVVARIARIPEK 438
Cdd:COG1222   298 -IREGRDTVTMEDLEKAIEKVKKKTET 323
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
491-605 5.52e-09

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: 54.91  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 491 LFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEymerhTVSRLIGAPPGYVgydqGGLLTDAVIKHPhSVVLLDEIEKAHP 570
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALAG 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2298853246 571 -----------DVFNLLLQVMDngtltdnnGRKADFRNVILVMTTN 605
Cdd:pfam00004  72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
210-342 2.45e-08

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 53.90  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRIvqgdvpevmaDCTLYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19509    36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 290 IgaGAASGGQVDAANLIKPLL----------SSGKIRVIGSTtyqefSNIFEKDRALARRFQK 342
Cdd:cd19509   104 L--SERGSGEHEASRRVKTEFlvqmdgvlnkPEDRVLVLGAT-----NRPWELDEAFLRRFEK 159
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
210-342 5.89e-08

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: 52.94  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19521    44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 290 igAGAASGGQVDAANLIKPLL---------SSGKIRVIGSTtyqefsNI-FEKDRALARRFQK 342
Cdd:cd19521   112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGAT------NIpWQLDSAIRRRFEK 166
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
491-605 8.18e-08

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: 51.99  E-value: 8.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246  491 LFAGPTGVGKTEVTVQLAKAMDIE---LLRFDMSEYMERHTVSRLIGAPPGYVGYDQGG----LLTDAVIKHPHSVVLLD 563
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2298853246  564 EIEKAHPDVFNLLLQVMDNGTLTDnngRKADFRNVILVMTTN 605
Cdd:smart00382  86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
210-514 5.21e-07

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 53.37  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRI----VQGDVPEVMadctlysldigsllagTKYRGDFEKRFKALLKQLEQDQNSILFIDE 285
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAgayfISINGPEIM----------------SKYYGESEERLREIFKEAEENAPSIIFIDE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 286 IHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGSTTYQEfsnifEKDRALAR--RFQK-IDITEPTPEETVQI 356
Cdd:TIGR01243 280 IDAIAPKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEI 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 357 INGLKTKYEAHHDVR----------YTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRL--MPVSKRKKTVNVAD 424
Cdd:TIGR01243 355 LKVHTRNMPLAEDVDldklaevthgFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLkeLKVTMKDFMEALKM 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 425 IESVVARIARIPEKTVSASDrdvlrslgdrlkmlVFGQDQAIEALTEAIK--------MSRAGLghdRKPVGSFLFaGPT 496
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSD--------------IGGLEEVKQELREAVEwplkhpeiFEKMGI---RPPKGVLLF-GPP 496
                         330
                  ....*....|....*...
gi 2298853246 497 GVGKTevtvQLAKAMDIE 514
Cdd:TIGR01243 497 GTGKT----LLAKAVATE 510
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
190-321 1.08e-06

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: 49.21  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 190 RDPELERAIQVLCRRrknNPLLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLAgtKYRGDFEKRFKAL 269
Cdd:cd19503    21 KYPELFRALGLKPPR---GVLLHGPPGTGKTLLARAVANE----------AGANFLSISGPSIVS--KYLGESEKNLREI 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2298853246 270 LKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGST 321
Cdd:cd19503    86 FEEARSHAPSIIFIDEIDALAPKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
206-289 5.82e-06

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: 48.37  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 206 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTlysldigSLL-AGtkYRG-DFEKRFKALLK----QLEQDQNS 279
Cdd:cd19497    50 KSNILLIGPTGSGKTLLAQTLA-KIL--DVPFAIADAT-------TLTeAG--YVGeDVENILLKLLQaadyDVERAQRG 117
                          90
                  ....*....|
gi 2298853246 280 ILFIDEIHTI 289
Cdd:cd19497   118 IVYIDEIDKI 127
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
192-342 8.05e-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: 46.90  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 192 PELERAIqvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTLYSLDIGSLLAGTKYRGDFEKRFKALLK 271
Cdd:cd19522    23 PEFFKGI----RRPWKGVLMVGPPGTGKTLLAKAVA------------TECGTTFFNVSSSTLTSKYRGESEKLVRLLFE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 272 QLEQDQNSILFIDEIHTIIGAgAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNI----------FEKDRALARRFQ 341
Cdd:cd19522    87 MARFYAPTTIFIDEIDSICSR-RGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMvmvlaatnfpWDIDEALRRRLE 165

                  .
gi 2298853246 342 K 342
Cdd:cd19522   166 K 166
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
176-344 8.84e-06

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 46.66  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 176 NQLARVGGIDPLIGRDPELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLA------WRIVQGdvPEVMadctlysldi 249
Cdd:cd19519     7 KQLAQIREMVELPLRHPELFKAIGI---KPPRGILLYGPPGTGKTLIARAVAnetgafFFLING--PEIM---------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 250 gsllagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGSTty 323
Cdd:cd19519    72 ------SKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRivsqllTLMDGLKQRAHVIVMAAT-- 143
                         170       180
                  ....*....|....*....|.
gi 2298853246 324 qefSNIFEKDRALaRRFQKID 344
Cdd:cd19519   144 ---NRPNSIDPAL-RRFGRFD 160
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
491-605 1.46e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 46.40  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 491 LFAGPTGVGKTEVTVQLAKAMDIELLRF------DMSEYM-ERHTvsrLIGAPPGYVgyDQGglLTDAVIKHPhsVVLLD 563
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2298853246 564 EIEK----AHPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVILVMTTN 605
Cdd:cd19500   112 EIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATAN 161
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
459-511 1.73e-05

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 47.49  E-value: 1.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 459 VFGQDQAIEALTEAIKMSRagLGHdrkpvgSFLFAGPTGVGKTEVTVQLAKAM 511
Cdd:COG2812    12 VVGQEHVVRTLKNALASGR--LAH------AYLFTGPRGVGKTTLARILAKAL 56
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
186-245 3.72e-05

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 44.80  E-value: 3.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 186 PLIGRDPELERAIQVLCRRRKNNP---LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTLY 245
Cdd:pfam13191   1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEN 63
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
210-298 4.54e-05

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 44.28  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLA--WRIvqgdvpevmadcTLYSLDIGSLLAGtkYRGDFEKRFKALLKQLEQDQNSILFIDEIH 287
Cdd:cd19507    35 LLVGIQGTGKSLTAKAIAgvWQL------------PLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                          90
                  ....*....|.
gi 2298853246 288 TIIGaGAASGG 298
Cdd:cd19507   101 KGFS-NADSKG 110
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
333-605 4.74e-05

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: 46.44  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 333 DRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRLMP 412
Cdd:COG0464    34 AAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 413 VSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVfGQDQAIEALTEAI----KMSRAGLGHDRKPVG 488
Cdd:COG0464   114 LERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG-GLEEVKEELRELValplKRPELREEYGLPPPR 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 489 SFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEymerhtvsrLIGappGYVGydQGGLLTDAVIK----HPHSVVLLDE 564
Cdd:COG0464   193 GLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVG--ETEKNLREVFDkargLAPCVLFIDE 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2298853246 565 IEKAHPD-----------VFNLLLQVMDNGTltdnngrkadfRNVILVMTTN 605
Cdd:COG0464   259 ADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
491-567 4.81e-05

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: 44.68  E-value: 4.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2298853246 491 LFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMErhtvsrligapPGYVGYDQGGLLTDAVikhpHSVVLLDEIEK 567
Cdd:cd19498    50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE-----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
210-342 7.25e-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: 44.21  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19525    59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSL 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 290 IgaGAASGGQVDAANLIKPLL----------SSGKIRVIGSTTYQEfsnifEKDRALARRFQK 342
Cdd:cd19525   127 L--SQRGEGEHESSRRIKTEFlvqldgattsSEDRILVVGATNRPQ-----EIDEAARRRLVK 182
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
206-286 1.61e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.76  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 206 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTlysldigSLL-AGtkYRG-DFEkrfKALLKQL-------EQD 276
Cdd:PRK05342  108 KSNILLIGPTGSGKTLLAQTLA-RIL--DVPFAIADAT-------TLTeAG--YVGeDVE---NILLKLLqaadydvEKA 172
                          90
                  ....*....|
gi 2298853246 277 QNSILFIDEI 286
Cdd:PRK05342  173 QRGIVYIDEI 182
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
210-342 1.76e-04

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 42.91  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19524    37 LLFGPPGNGKTMLAKAVAAE----------SNATFFNISAASLT--SKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298853246 290 IgaGAASGGQVDAANLIKP--------LLSSG--KIRVIGSTTYQEfsnifEKDRALARRFQK 342
Cdd:cd19524   105 L--SERSEGEHEASRRLKTefliefdgVQSNGddRVLVMGATNRPQ-----ELDDAVLRRFTK 160
TniB pfam05621
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ...
193-343 2.38e-04

Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein which is involved in Tn5053 mercury resistance transposition. This entry represents a P-loop domain.


Pssm-ID: 428547  Cd Length: 189  Bit Score: 42.96  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 193 ELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWR---IVQGD---VPEVMADC-------TLYSLDIGSLLAGTKYR 259
Cdd:pfam05621  22 RLEDLLDYPKRLRMPNLLLVGDSNNGKTMIVERFARLhppTDDEDaeiVPVVVVQMppkpdekRLYVAILEALGAPFRPR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 260 GDFEKRFKALLKQLEQDQNSILFIDEIHTIIgAGAASgGQVDAANLIKPLLSSGKIRVIGSTTyQEFSNIFEKDRALARR 339
Cdd:pfam05621 102 DRLSKLEQQVLRLLRAVGVRMLIIDEFHNLL-AGSAR-KQREFLNVLKSLGNELRIPIVGVGT-REAVRAIRTDPQLASR 178

                  ....
gi 2298853246 340 FQKI 343
Cdd:pfam05621 179 FEPI 182
PRK13341 PRK13341
AAA family ATPase;
183-339 2.91e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 44.28  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 183 GIDPLIGRDPELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVpevmadctlysLDIGSLLAGTKyrgDF 262
Cdd:PRK13341   32 GQDHILGEGRLLRRAIKA---DRVGSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DL 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2298853246 263 EKRFKALLKQLEQ-DQNSILFIDEIHTIIGAgaasggQVDAanlIKPLLSSGKIRVIGSTTYQEFsniFEKDRALARR 339
Cdd:PRK13341   94 RAEVDRAKERLERhGKRTILFIDEVHRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSR 159
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
210-342 3.87e-04

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 41.64  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19520    39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2298853246 290 IGAGAASGGQVDAA------NLIKPLLSSGKIRVI--GSTtyqefSNIFEKDRALARRFQK 342
Cdd:cd19520   107 LRQRSSTDHEATAMmkaefmSLWDGLSTDGNCRVIvmGAT-----NRPQDLDEAILRRMPK 162
DNA_pol3_delta2 pfam13177
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ...
461-511 5.20e-04

DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.


Pssm-ID: 433013 [Multi-domain]  Cd Length: 161  Bit Score: 41.43  E-value: 5.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2298853246 461 GQDQAIEALTEAIKMSRagLGHdrkpvgSFLFAGPTGVGKTEVTVQLAKAM 511
Cdd:pfam13177   1 GQPEAIQLLQNSLENGR--LSH------AYLFSGPEGVGKLELALAFAKAL 43
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
187-322 8.10e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.38  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 187 LIGRDPELERAIQvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTLYSLDigSLLAGTKyrgDFEKRF 266
Cdd:PRK13342   20 LLGPGKPLRRMIE---AGRLSSMILWGPPGTGKTTLARIIA----------GATDAPFEALS--AVTSGVK---DLREVI 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2298853246 267 KALLKQLEQDQNSILFIDEIHTIigagaaSGGQVDAanLIkPLLSSGKIRVIGSTT 322
Cdd:PRK13342   82 EEARQRRSAGRRTILFIDEIHRF------NKAQQDA--LL-PHVEDGTITLIGATT 128
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
187-286 1.55e-03

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: 40.24  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 187 LIGRDPELERAIQVLCR-----RRKNNP----LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTLYS-LDIGSLLAGT 256
Cdd:cd19499    13 VVGQDEAVKAVSDAIRRaraglSDPNRPigsfLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMeKHSVSRLIGA 92
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2298853246 257 --KYRGdFEKRFKaLLKQLEQDQNSILFIDEI 286
Cdd:cd19499    93 ppGYVG-YTEGGQ-LTEAVRRKPYSVVLLDEI 122
PRK14969 PRK14969
DNA polymerase III subunits gamma and tau; Provisional
461-514 1.90e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237873 [Multi-domain]  Cd Length: 527  Bit Score: 41.66  E-value: 1.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2298853246 461 GQDQAIEALTEAIKMSRagLGHdrkpvgSFLFAGPTGVGKTEVTVQLAKAMDIE 514
Cdd:PRK14969   20 GQEHVVRALTNALEQQR--LHH------AYLFTGTRGVGKTTLARILAKSLNCE 65
AAA_22 pfam13401
AAA domain;
203-287 2.46e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 203 RRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP----EVMADCTLYSL--DIGSLLAGTKYRGDFEKRFKALLKQLEQD 276
Cdd:pfam13401   2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDLlrALLRALGLPLSGRLSKEELLAALQQLLLA 81
                          90
                  ....*....|...
gi 2298853246 277 QNS--ILFIDEIH 287
Cdd:pfam13401  82 LAVavVLIIDEAQ 94
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
207-310 2.54e-03

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: 39.67  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 207 NNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTLYSlDIGsllagtkYRG-DFEKRFKALLkqleqdqNSILFIDE 285
Cdd:cd19498    47 KNILMIGPTGVGKTEIARRLA-KLA--GAPFIKVEATKFT-EVG-------YVGrDVESIIRDLV-------EGIVFIDE 108
                          90       100
                  ....*....|....*....|....*
gi 2298853246 286 IHTIIGAGAASGGQVDAANLIKPLL 310
Cdd:cd19498   109 IDKIAKRGGSSGPDVSREGVQRDLL 133
PRK07399 PRK07399
DNA polymerase III subunit delta'; Validated
459-510 3.87e-03

DNA polymerase III subunit delta'; Validated


Pssm-ID: 236011 [Multi-domain]  Cd Length: 314  Bit Score: 40.27  E-value: 3.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2298853246 459 VFGQDQAIEALTEAIKMSRAGLGhdrkpvgsFLFAGPTGVGKTEVTVQLAKA 510
Cdd:PRK07399    6 LIGQPLAIELLTAAIKQNRIAPA--------YLFAGPEGVGRKLAALCFIEG 49
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
210-321 3.87e-03

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 39.03  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRIVQGD--VPEVM---ADCTlysldigsllagTKYRGDFEKRFKALLKQLEQDQNSILFID 284
Cdd:cd19517    38 LFHGPPGTGKTLMARALAAECSKGGqkVSFFMrkgADCL------------SKWVGEAERQLRLLFEEAYRMQPSIIFFD 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2298853246 285 EIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGST 321
Cdd:cd19517   106 EIDGLAPVRSSKQEQIHASivstllALMDGLDNRGQVVVIGAT 148
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
185-286 4.32e-03

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 40.27  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 185 DPLIGRDPELERAIQVLCR-RRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDVPEVMADCTLYSLD-IGSLLAGTKyRGD 261
Cdd:COG3284   321 AALAGGDPAMRRALRRARRlADRDIPVLIlGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEElIESELFGYE-PGA 399
                          90       100
                  ....*....|....*....|....*..
gi 2298853246 262 F--EKRFKALLKqLEQDQNSILFIDEI 286
Cdd:COG3284   400 FtgARRKGRPGK-IEQADGGTLFLDEI 425
PRK12723 PRK12723
flagellar biosynthesis regulator FlhF; Provisional
462-610 5.83e-03

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 183702 [Multi-domain]  Cd Length: 388  Bit Score: 39.88  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 462 QDQAIEALTEAIKMSRAGLGHDRKPVgsFLFAGPTGVGKTEVTVQLA---------KAMDIELLRFD---MSEYMERHTV 529
Cdd:PRK12723  151 RDSVIIYIAKTIKCSGSIIDNLKKRV--FILVGPTGVGKTTTIAKLAaiyginsddKSLNIKIITIDnyrIGAKKQIQTY 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 530 SRLIGAPPGYVGYDQgGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLllqvMDNGTLTDNNGRKADFRNVILVMTTNAGVR 609
Cdd:PRK12723  229 GDIMGIPVKAIESFK-DLKEEITQSKDFDLVLVDTIGKSPKDFMKL----AEMKELLNACGRDAEFHLAVSSTTKTSDVK 303

                  .
gi 2298853246 610 E 610
Cdd:PRK12723  304 E 304
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
210-321 6.72e-03

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: 38.09  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLdIGSLLAgTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19502    41 LLYGPPGTGKTLLAKAVANH----------TDATFIRV-VGSELV-QKYIGEGARLVRELFEMAREKAPSIIFIDEIDAI 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2298853246 290 IGA--GAASGGQVDAANLIKPLL-------SSGKIRVIGST 321
Cdd:cd19502   109 GAKrfDSGTGGDREVQRTMLELLnqldgfdPRGNIKVIMAT 149
AAA_22 pfam13401
AAA domain;
488-584 8.73e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 488 GSFLFAGPTGVGKTEVTVQLAK---AMDIELLRFDMSEYME----RHTVSRLIGAPPgyVGYDQGGLLTDAVIKH----- 555
Cdd:pfam13401   6 GILVLTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPSGTSpkdlLRALLRALGLPL--SGRLSKEELLAALQQLllala 83
                          90       100
                  ....*....|....*....|....*....
gi 2298853246 556 PHSVVLLDEIEKAHPDVFNLLLQVMDNGT 584
Cdd:pfam13401  84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
COG3899 COG3899
Predicted ATPase [General function prediction only];
4-235 9.01e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 39.46  E-value: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246    4 QELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQPTLS 83
Cdd:COG3899    112 ALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAAAARAARLRRARAARLAALALRA 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246   84 FQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQAPNAEnpvneeQSG 163
Cdd:COG3899    192 LLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAA------ALL 265
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2298853246  164 GEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVL--CRRRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDV 235
Cdd:COG3899    266 LLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALerARAGRGELVLVsGEAGIGKSRLVRELARRARARGG 340
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
210-289 9.37e-03

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: 37.77  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298853246 210 LLVGESGVGKTAIAEGLAWRIvqgDVPevmadctLYSLDIGSLLAGTKyrGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19518    38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH