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Conserved domains on  [gi|1958742965|ref|XP_038952724|]
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AFG3-like protein 2 isoform X1 [Rattus norvegicus]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
78-668 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 811.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  78 VMIYFLFKSSG---REITWKDFVNnYLSKGVVDRLEVVNKRfVRVTFTPGKTpvdgQYVWFNIGSVDTFERNLEtlqqel 154
Cdd:COG0465     6 VLLFNLFSSSSssvKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTLKDGTK----TRFTTYRVNDPELVDLLE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 155 giegENRVPVVYIAESDGSF----LLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFK 229
Cdd:COG0465    74 ----EKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 309
Cdd:COG0465   143 DVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 310 VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGR 389
Cdd:COG0465   223 VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 390 FDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQA 469
Cdd:COG0465   303 FDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEA 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 470 IERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCM 548
Cdd:COG0465   379 IDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAV 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 549 TLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVR 623
Cdd:COG0465   459 LLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVR 538
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1958742965 624 ILISEAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGP 668
Cdd:COG0465   539 RIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
78-668 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 811.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  78 VMIYFLFKSSG---REITWKDFVNnYLSKGVVDRLEVVNKRfVRVTFTPGKTpvdgQYVWFNIGSVDTFERNLEtlqqel 154
Cdd:COG0465     6 VLLFNLFSSSSssvKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTLKDGTK----TRFTTYRVNDPELVDLLE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 155 giegENRVPVVYIAESDGSF----LLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFK 229
Cdd:COG0465    74 ----EKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 309
Cdd:COG0465   143 DVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 310 VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGR 389
Cdd:COG0465   223 VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 390 FDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQA 469
Cdd:COG0465   303 FDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEA 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 470 IERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCM 548
Cdd:COG0465   379 IDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAV 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 549 TLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVR 623
Cdd:COG0465   459 LLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVR 538
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1958742965 624 ILISEAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGP 668
Cdd:COG0465   539 RIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
174-667 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 739.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 174 FLLSMLPTVLIIAFLLYTIRRGPAGIGrtgrgmGGLFSVGETTAKVLKDE-IDVKFKDVAGCEEAKLEIMEFVNFLKNPK 252
Cdd:TIGR01241   5 FLFSLLPPILLLVGVWFFFRRQMQGGG------GRAFSFGKSKAKLLNEEkPKVTFKDVAGIDEAKEELMEIVDFLKNPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 253 QYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDA 332
Cdd:TIGR01241  79 KFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 333 VGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHL 412
Cdd:TIGR01241 159 VGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 413 RPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTV 492
Cdd:TIGR01241 239 KNKKLAPDVDLKAVAR----RTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 493 AYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDL 571
Cdd:TIGR01241 315 AYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 572 RKVTQSAYAQIVQFGMNEKVGQISFDlPRQGDMVL------EKPYSEATARMIDDEVRILISEAYKRTVALLTEKKADVE 645
Cdd:TIGR01241 395 KQATNIARAMVTEWGMSDKLGPVAYG-SDGGDVFLgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELE 473
                         490       500
                  ....*....|....*....|..
gi 1958742965 646 KVALLLLEKEVLDKNDMVELLG 667
Cdd:TIGR01241 474 LLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
173-678 4.50e-179

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 525.77  E-value: 4.50e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 173 SFLLsmLPtVLIIAFLLYTIRRG---PAGIGRtgrgmgGLFSVGETTAKVLKD-EIDVKFKDVAGCEEAKLEIMEFVNFL 248
Cdd:CHL00176  132 SNLL--LP-LILIGVLWFFFQRSsnfKGGPGQ------NLMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 249 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 328
Cdd:CHL00176  203 KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFID 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 329 EIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIF 408
Cdd:CHL00176  283 EIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 409 KVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEkKTQVLQPEE 488
Cdd:CHL00176  363 KVHARNKKLSPDVSLELIARR----TPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKN 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 489 KKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLP-KEQYLYTKEQLLDRMCMTLGGRVSEEIFFG--RITT 565
Cdd:CHL00176  438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTT 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 566 GAQDDLRKVTQSAYAQIVQFGMNeKVGQISFDLPRQGD------MVLEKPYSEATARMIDDEVRILISEAYKRTVALLTE 639
Cdd:CHL00176  518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1958742965 640 KKADVEKVALLLLEKEVLDKNDMVELLGPR-PFTEKSTYE 678
Cdd:CHL00176  597 NRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
226-396 1.16e-116

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 347.68  E-value: 1.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 226 VKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 305
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 306 GPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALL 385
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1958742965 386 RPGRFDRQIFI 396
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
483-665 3.03e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 274.86  E-value: 3.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 483 VLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYTKEQLLDRMCMTLGGRVSEEIFFG 561
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 562 RITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDlPRQG------DMVLEKPYSEATARMIDDEVRILISEAYKRTVA 635
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958742965 636 LLTEKKADVEKVALLLLEKEVLDKNDMVEL 665
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
262-400 1.56e-19

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: 85.89  E-value: 1.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  262 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDLFALARKNAPCI 324
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958742965  325 LFIDEIDAVGRKRgrgnfggqSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPgRFDRQIFIGPPD 400
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
78-668 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 811.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  78 VMIYFLFKSSG---REITWKDFVNnYLSKGVVDRLEVVNKRfVRVTFTPGKTpvdgQYVWFNIGSVDTFERNLEtlqqel 154
Cdd:COG0465     6 VLLFNLFSSSSssvKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTLKDGTK----TRFTTYRVNDPELVDLLE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 155 giegENRVPVVYIAESDGSF----LLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFK 229
Cdd:COG0465    74 ----EKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 309
Cdd:COG0465   143 DVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 310 VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGR 389
Cdd:COG0465   223 VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 390 FDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQA 469
Cdd:COG0465   303 FDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEA 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 470 IERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCM 548
Cdd:COG0465   379 IDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAV 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 549 TLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVR 623
Cdd:COG0465   459 LLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVR 538
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 1958742965 624 ILISEAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGP 668
Cdd:COG0465   539 RIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
174-667 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 739.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 174 FLLSMLPTVLIIAFLLYTIRRGPAGIGrtgrgmGGLFSVGETTAKVLKDE-IDVKFKDVAGCEEAKLEIMEFVNFLKNPK 252
Cdd:TIGR01241   5 FLFSLLPPILLLVGVWFFFRRQMQGGG------GRAFSFGKSKAKLLNEEkPKVTFKDVAGIDEAKEELMEIVDFLKNPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 253 QYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDA 332
Cdd:TIGR01241  79 KFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 333 VGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHL 412
Cdd:TIGR01241 159 VGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 413 RPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTV 492
Cdd:TIGR01241 239 KNKKLAPDVDLKAVAR----RTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 493 AYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDL 571
Cdd:TIGR01241 315 AYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 572 RKVTQSAYAQIVQFGMNEKVGQISFDlPRQGDMVL------EKPYSEATARMIDDEVRILISEAYKRTVALLTEKKADVE 645
Cdd:TIGR01241 395 KQATNIARAMVTEWGMSDKLGPVAYG-SDGGDVFLgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELE 473
                         490       500
                  ....*....|....*....|..
gi 1958742965 646 KVALLLLEKEVLDKNDMVELLG 667
Cdd:TIGR01241 474 LLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
173-678 4.50e-179

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 525.77  E-value: 4.50e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 173 SFLLsmLPtVLIIAFLLYTIRRG---PAGIGRtgrgmgGLFSVGETTAKVLKD-EIDVKFKDVAGCEEAKLEIMEFVNFL 248
Cdd:CHL00176  132 SNLL--LP-LILIGVLWFFFQRSsnfKGGPGQ------NLMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 249 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 328
Cdd:CHL00176  203 KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFID 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 329 EIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIF 408
Cdd:CHL00176  283 EIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 409 KVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEkKTQVLQPEE 488
Cdd:CHL00176  363 KVHARNKKLSPDVSLELIARR----TPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKN 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 489 KKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLP-KEQYLYTKEQLLDRMCMTLGGRVSEEIFFG--RITT 565
Cdd:CHL00176  438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTT 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 566 GAQDDLRKVTQSAYAQIVQFGMNeKVGQISFDLPRQGD------MVLEKPYSEATARMIDDEVRILISEAYKRTVALLTE 639
Cdd:CHL00176  518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1958742965 640 KKADVEKVALLLLEKEVLDKNDMVELLGPR-PFTEKSTYE 678
Cdd:CHL00176  597 NRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
173-690 6.43e-162

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 481.84  E-value: 6.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 173 SFLLSMLPTVLIIAFLLYTIRRGPAGIGRtgrgmgGLFSVGETTAKVL-KDEIDVKFKDVAGCEEAKLEIMEFVNFLKNP 251
Cdd:PRK10733  101 SIFISWFPMLLLIGVWIFFMRQMQGGGGK------GAMSFGKSKARMLtEDQIKTTFADVAGCDEAKEEVAELVEYLREP 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 252 KQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEID 331
Cdd:PRK10733  175 SRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEID 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 332 AVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVH 411
Cdd:PRK10733  255 AVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVH 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 412 LRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKT 491
Cdd:PRK10733  335 MRRVPLAPDIDAAIIARG----TPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 492 VAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTL-GGRVSEEIFFG--RITTGAQ 568
Cdd:PRK10733  411 TAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLyGGRLAEEIIYGpeHVSTGAS 490
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 569 DDLRKVTQSAYAQIVQFGMNEKVGQISFdLPRQGDMVL------EKPYSEATARMIDDEVRILISEAYKRTVALLTEKKA 642
Cdd:PRK10733  491 NDIKVATNLARNMVTQWGFSEKLGPLLY-AEEEGEVFLgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMD 569
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1958742965 643 DVEKVALLLLEKEVLDKNDMVELLGPRPFTEKSTYEEfVEGTGSLDED 690
Cdd:PRK10733  570 ILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEE-PGASNNSDDN 616
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
226-396 1.16e-116

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 347.68  E-value: 1.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 226 VKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 305
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 306 GPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALL 385
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1958742965 386 RPGRFDRQIFI 396
Cdd:cd19501   161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
225-481 4.62e-112

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 341.99  E-value: 4.62e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFV-NFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 303
Cdd:COG1222    74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 383
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 384 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 463
Cdd:COG1222   232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAK----LTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307
                         250
                  ....*....|....*...
gi 1958742965 464 KHFEQAIERVIGGLEKKT 481
Cdd:COG1222   308 EDLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
225-480 1.37e-94

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 298.67  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 303
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGpAR-VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDP 382
Cdd:PRK03992  207 GEG-ARlVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 383 ALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAIN 462
Cdd:PRK03992  286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAE----LTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                         250
                  ....*....|....*...
gi 1958742965 463 EKHFEQAIERVIGGLEKK 480
Cdd:PRK03992  362 MEDFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
483-665 3.03e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 274.86  E-value: 3.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 483 VLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYTKEQLLDRMCMTLGGRVSEEIFFG 561
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 562 RITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDlPRQG------DMVLEKPYSEATARMIDDEVRILISEAYKRTVA 635
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958742965 636 LLTEKKADVEKVALLLLEKEVLDKNDMVEL 665
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
225-474 8.65e-80

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 259.35  E-value: 8.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 303
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 383
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 384 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 463
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAK----MTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 1958742965 464 KHFEQAIERVI 474
Cdd:TIGR01242 354 DDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
105-473 1.39e-78

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: 257.15  E-value: 1.39e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 105 VVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLI 184
Cdd:COG0464    31 LALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 185 IAFLLYTIRRGPAGIGRTGRGMGGLFSVGE--TTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVN-FLKNPKQYQDLGAKI 261
Cdd:COG0464   111 LLDLERALLELLRESAEALALAAPLVTYEDigGLEEELLELREAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPP 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 262 PKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGN 341
Cdd:COG0464   191 PRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 342 FGGQSEQentLNQLLVEMDGFntTTNVVILAGTNRPDILDPALLRpgRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSAL 421
Cdd:COG0464   271 DGVGRRV---VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDV 343
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958742965 422 EKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERV 473
Cdd:COG0464   344 DLEELAEA----TEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
218-479 3.72e-70

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: 243.66  E-value: 3.72e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 218 KVLKDEIDVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGS 296
Cdd:TIGR01243 442 EVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 297 EFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNR 376
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNR 599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 377 PDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARH 456
Cdd:TIGR01243 600 PDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEM----TEGYTGADIEAVCREAAMAALRE 675
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958742965 457 LSDA------------------INEKHFEQAIERVIGGLEK 479
Cdd:TIGR01243 676 SIGSpakeklevgeeeflkdlkVEMRHFLEALKKVKPSVSK 716
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
228-394 2.78e-68

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: 221.83  E-value: 2.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 228 FKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 306
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 307 PARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLR 386
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                  ....*...
gi 1958742965 387 PGRFDRQI 394
Cdd:cd19502   162 PGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
225-474 4.66e-64

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 218.48  E-value: 4.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 303
Cdd:PTZ00454  141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 383
Cdd:PTZ00454  221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 384 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALE-KDKLARklaslTPGFSGADVANVCNEAALIAARHLSDAIN 462
Cdd:PTZ00454  301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDlEDFVSR-----PEKISAADIAAICQEAGMQAVRKNRYVIL 375
                         250
                  ....*....|..
gi 1958742965 463 EKHFEQAIERVI 474
Cdd:PTZ00454  376 PKDFEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
219-474 6.32e-62

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 213.86  E-value: 6.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 219 VLKDEIDV-------------KFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAG 284
Cdd:PTZ00361  160 ILLDEVDPlvsvmkvdkapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVAN 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 285 EANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNT 364
Cdd:PTZ00361  240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDS 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 365 TTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKL--DSALE-----KDKLarklasltpgf 437
Cdd:PTZ00361  320 RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLaeDVDLEefimaKDEL----------- 388
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958742965 438 SGADVANVCNEAALIAARHLSDAINEKHFEQAIERVI 474
Cdd:PTZ00361  389 SGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVL 425
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
237-396 5.34e-61

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: 201.74  E-value: 5.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 237 AKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 316
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 317 ARKNAPCILFIDEIDAVGRKRGRGnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 396
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSS--GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
225-457 6.53e-61

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: 217.85  E-value: 6.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 303
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQEnTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 383
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVEKR-VVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958742965 384 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRplklDSALEKDKLARKLASLTPGFSGADVANVCNEAALIAARHL 457
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTR----NMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRF 400
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
228-472 1.13e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 203.96  E-value: 1.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 228 FKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 307
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 308 ARVRDLFALARkNAPCILFIDEIDAVGRKRGRGNFGGqsEQENTLNQLLVEMDGFNttTNVVILAGTNRPDILDPALLRp 387
Cdd:COG1223    81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 388 gRFDRQIFIGPPDIKGRASIFKVHLRPLKldsaLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFE 467
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFP----LPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229

                  ....*
gi 1958742965 468 QAIER 472
Cdd:COG1223   230 EALKQ 234
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
237-396 3.62e-60

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 199.43  E-value: 3.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 237 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFA 315
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 316 LARKNAPCILFIDEIDAVGRKRGrGNFGGQSeQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 395
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRG-QSDSSGV-TDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                  .
gi 1958742965 396 I 396
Cdd:cd19511   159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
230-396 2.85e-57

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: 192.12  E-value: 2.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 308
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 309 RVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRP 387
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                  ....*....
gi 1958742965 388 GRFDRQIFI 396
Cdd:cd19503   157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
237-396 3.78e-54

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 183.47  E-value: 3.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 237 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFA 315
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 316 LARKNAPCILFIDEIDAVGRKRGRGnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 395
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGTT--GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                  .
gi 1958742965 396 I 396
Cdd:cd19529   159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
238-396 8.96e-53

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 179.63  E-value: 8.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 238 KLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 316
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 317 ARKNAPCILFIDEIDAVGRKRGrGNFGGQS-EQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 395
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARG-GNIGDAGgAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                  .
gi 1958742965 396 I 396
Cdd:cd19528   161 I 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
266-397 3.74e-52

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: 176.63  E-value: 3.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfGGQ 345
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958742965 346 SEQENTLNQLLVEMDGF-NTTTNVVILAGTNRPDILDPALLrpGRFDRQIFIG 397
Cdd:pfam00004  79 SESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
230-397 6.87e-50

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: 171.85  E-value: 6.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 308
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 309 RVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQEnTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPG 388
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                  ....*....
gi 1958742965 389 RFDRQIFIG 397
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
242-396 1.64e-49

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 170.75  E-value: 1.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 242 MEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNA 321
Cdd:cd19530    10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958742965 322 PCILFIDEIDAVGRKRGRgnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 396
Cdd:cd19530    90 PCVIFFDEVDALVPKRGD---GGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
230-394 2.28e-46

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: 162.57  E-value: 2.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNFLKNPKQ-YQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 308
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 309 RVRDLFALARKNAPCILFIDEIDAVGRKRGrgnfGGQSEQENTL-NQLLVEMDGFN----TTTNVVILAGTNRPDILDPA 383
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRE----SAQREMERRIvSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                         170
                  ....*....|.
gi 1958742965 384 LLRPGRFDRQI 394
Cdd:cd19518   157 LRRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
249-395 7.65e-45

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 157.98  E-value: 7.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 249 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 328
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958742965 329 EIDAVGRKRGRGNFGgqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 395
Cdd:cd19526    94 EFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
238-396 2.03e-41

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 148.43  E-value: 2.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 238 KLEIMEFVNF-LKNPKQYQDlGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 316
Cdd:cd19527     2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 317 ARKNAPCILFIDEIDAVGRKRGR-GNFGGQSEQenTLNQLLVEMDGFNTTT-NVVILAGTNRPDILDPALLRPGRFDRQI 394
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                  ..
gi 1958742965 395 FI 396
Cdd:cd19527   159 YL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
231-396 2.41e-37

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: 137.10  E-value: 2.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 231 VAGCEEAKLEIMEFVNF-LKNPKQYQdLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 309
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 310 VRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTN--VVILAGTNRPDILDPALLR 386
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155
                         170
                  ....*....|
gi 1958742965 387 pgRFDRQIFI 396
Cdd:cd19509   156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
225-396 1.45e-33

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: 126.52  E-value: 1.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 302
Cdd:cd19521     3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 303 VGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGF-NTTTNVVILAGTNRPDIL 380
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIkTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                         170
                  ....*....|....*.
gi 1958742965 381 DPALLRpgRFDRQIFI 396
Cdd:cd19521   157 DSAIRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
230-390 1.56e-31

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: 120.61  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLG-AKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 307
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 308 ARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfggqSEQENTL---NQLLVEMDGFNTTTN--VVILAGTNRPDILDP 382
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDE 154
                         170
                  ....*....|
gi 1958742965 383 ALLR--PGRF 390
Cdd:cd19520   155 AILRrmPKRF 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
230-395 1.64e-31

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: 120.69  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEAN-----VPFITVSGSEFLEMFV 303
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfggQSEQENT----LNQLLVEMDGFNTTTNVVILAGTNRPDI 379
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                         170
                  ....*....|....*.
gi 1958742965 380 LDPALLRPGRFDRQIF 395
Cdd:cd19517   154 LDPALRRPGRFDREFY 169
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
225-396 1.08e-30

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: 118.94  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 303
Cdd:cd19525    18 PINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 304 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfgGQSEQENTL---NQLLVEMDGFNTTTN--VVILAGTNRPD 378
Cdd:cd19525    97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR------GEGEHESSRrikTEFLVQLDGATTSSEdrILVVGATNRPQ 170
                         170
                  ....*....|....*...
gi 1958742965 379 ILDPALLRpgRFDRQIFI 396
Cdd:cd19525   171 EIDEAARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
251-396 1.13e-29

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 115.66  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 251 PKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANV--PFItVSGSEFLEMFVGVGPARVRDLFALA-----RKNAPC 323
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAeeeqrRLGANS 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958742965 324 ---ILFIDEIDAVGRKRGRGNfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 396
Cdd:cd19504   103 glhIIIFDEIDAICKQRGSMA-GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
230-396 4.44e-29

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: 113.93  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 307
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 308 ARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfGGQSEQENTL---NQLLVEMDGF-NTTTN------VVILAGTNRP 377
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR-----GTSEEHEASRrvkSELLVQMDGVgGASENddpskmVMVLAATNFP 153
                         170
                  ....*....|....*....
gi 1958742965 378 DILDPALLRpgRFDRQIFI 396
Cdd:cd19522   154 WDIDEALRR--RLEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
230-396 4.67e-29

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: 113.41  E-value: 4.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 308
Cdd:cd19524     1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 309 RVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTN--VVILAGTNRPDILDPALL 385
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155
                         170
                  ....*....|.
gi 1958742965 386 RpgRFDRQIFI 396
Cdd:cd19524   156 R--RFTKRVYV 164
ycf46 CHL00195
Ycf46; Provisional
225-464 4.50e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 118.58  E-value: 4.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 225 DVKFKDVAGCEEAKleimEFVNFLKN--PKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 302
Cdd:CHL00195  224 NEKISDIGGLDNLK----DWLKKRSTsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 303 VGVGPARVRDLFALARKNAPCILFIDEID-AVGRKRGRGNFGGQSEQENTLNQLLVEmdgfnTTTNVVILAGTNRPDILD 381
Cdd:CHL00195  300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLP 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 382 PALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDklARKLASLTPGFSGADVanvcnEAALIAARHLsdAI 461
Cdd:CHL00195  375 LEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYD--IKKLSKLSNKFSGAEI-----EQSIIEAMYI--AF 445

                  ...
gi 1958742965 462 NEK 464
Cdd:CHL00195  446 YEK 448
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
262-398 2.93e-26

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: 104.92  E-value: 2.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 262 PKGAILTGPPGTGKTLLAKATAGEA---NVPFITVSGSEFLEMFVG---VGPARVRDLFALARKNAPCILFIDEIDAVGR 335
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958742965 336 KrgrgnfggqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGP 398
Cdd:cd00009    99 G----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
252-396 2.05e-22

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: 94.36  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 252 KQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEID 331
Cdd:cd19507    21 KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958742965 332 avgrkRGRGNFGGQSEQENT---LNQLLVEMDgfNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 396
Cdd:cd19507   101 -----KGFSNADSKGDSGTSsrvLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
262-400 1.56e-19

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: 85.89  E-value: 1.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  262 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDLFALARKNAPCI 324
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958742965  325 LFIDEIDAVGRKRgrgnfggqSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPgRFDRQIFIGPPD 400
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
247-396 3.41e-19

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. 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: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 84.71  E-value: 3.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 247 FLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEflemfVGVGPARVRDLFALARKNApcILF 326
Cdd:cd19510     8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958742965 327 IDEIDA--VGRKR-GRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 396
Cdd:cd19510    81 LEDIDAafESREHnKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
257-396 3.18e-15

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. 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: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 73.56  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 257 LGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFL--------------EMFVGVGPARVRDLFALARKNAP 322
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958742965 323 CILFIDEIDAVGRKRgrgnFGGQSEQENT-----LNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 396
Cdd:cd19505    87 CIIWIPNIHELNVNR----STQNLEEDPKlllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
230-396 3.35e-15

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent 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: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 73.77  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 230 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLgAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 308
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 309 RVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQentlNQLLVEMDGFNTTT--NVVILAGTNRPDILDPALLR 386
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQ----VELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
                         170
                  ....*....|
gi 1958742965 387 pgRFDRQIFI 396
Cdd:cd19523   156 --YFSKRLLV 163
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
429-468 3.39e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 61.40  E-value: 3.39e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958742965 429 KLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQ 468
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
266-330 3.63e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 62.41  E-value: 3.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDLFALARKNA----PCILFIDEI 330
Cdd:PRK13342   40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
266-330 4.30e-10

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 62.38  E-value: 4.30e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDLFALARKNA----PCILFIDEI 330
Cdd:COG2256    53 ILWGPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
227-347 4.51e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.55  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 227 KFKDVAGCEEAKLEIMEFV-NFLKNpkqyqdlgaKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEF-----LE 300
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958742965 301 MFVGVGpARVRDLFALARKnapcILFIDEIDAVgrkRGRGNFGGQSE 347
Cdd:PRK04195   83 RVAGEA-ATSGSLFGARRK----LILLDEVDGI---HGNEDRGGARA 121
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
261-390 5.54e-09

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: 56.23  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 261 IPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVGvgparvRDLFALARKNAPCILFIDEIDAVGRKRGR 339
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGS 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958742965 340 GnfGGQSEQENTLNQLL--VEMDGFNTTTNVV-------ILAGT---NRPDILDPALlrPGRF 390
Cdd:cd19498   119 S--GPDVSREGVQRDLLpiVEGSTVSTKYGPVktdhilfIAAGAfhvAKPSDLIPEL--QGRF 177
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
262-331 7.27e-09

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: 55.66  E-value: 7.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 262 PKGAIL-TGPPGTGKTLLAKATAGEANV---PFITVSGSEFLE-----MFVGVGPARVR-----DLFALARKNAPCILFI 327
Cdd:pfam07724   2 PIGSFLfLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                  ....
gi 1958742965 328 DEID 331
Cdd:pfam07724  82 DEIE 85
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
266-384 8.28e-09

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 54.84  E-value: 8.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMfvGV-GPARVRDLFALARK-NAPCILFIDEIDAVGRKRgrgNFG 343
Cdd:cd19512    26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR---STE 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958742965 344 GQSE-QENTLNQLLVEMdGFNTTTNVVILAgTNRPDILDPAL 384
Cdd:cd19512   101 KISEdLRAALNAFLYRT-GEQSNKFMLVLA-SNQPEQFDWAI 140
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
67-163 1.70e-07

FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes. It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress, and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear.


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 49.91  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  67 YFLWTALFWSGVMIYFLF----KSSGREITWKDFVNnYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGS--- 139
Cdd:pfam06480   1 LLLWLLILLVLLLLFLLFllssSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFTTYFIPSlpn 79
                          90       100
                  ....*....|....*....|....
gi 1958742965 140 VDTFERNLETLQQELGIEGENRVP 163
Cdd:pfam06480  80 VDSLLEKLEDALEEKGVKVSVKPP 103
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
240-473 3.57e-07

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 52.26  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 240 EIMEFVNFLKNpkqYQDLGakipkgaILTGPPGTGKTLLAKATAGE-ANVPFITVSGS----EFL-----EMFVGVGPAR 309
Cdd:COG2842    38 RFAEALDEARA---LPGIG-------VVYGESGVGKTTAAREYANRnPNVIYVTASPSwtskELLeelaeELGIPAPPGT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 310 VRDLF-ALARKNAPCI--LFIDEIDAVGRKrgrgnfggqseqenTLNQLlveMDGFNTTTNVVILAGTNRPdildPALLR 386
Cdd:COG2842   108 IADLRdRILERLAGTGrlLIIDEADHLKPK--------------ALEEL---RDIHDETGVGVVLIGMERL----PAKLK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 387 pgRFDRqifigppdIKGRASiFKVHLRPLKLDSA---------LEKDKLARKLASLTpgfSGA--DVANVCNEAALIAAR 455
Cdd:COG2842   167 --RYEQ--------LYSRIG-FWVEFKPLSLEDVralaeawgeLTDPDLLELLHRIT---RGNlrRLDRTLRLAARAAKR 232
                         250
                  ....*....|....*...
gi 1958742965 456 HLSDAINEKHFEQAIERV 473
Cdd:COG2842   233 NGLTKITLDHVRAAALML 250
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
229-335 4.22e-07

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: 50.63  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 229 KDVAGCEEAKLEIMEFVNFLKnpkqyqdLGAKIpKGAIL--TGPPGTGKTLLAKATAGEANVPFITVS-G--SEFLEM-- 301
Cdd:cd19500    10 ADHYGLEDVKERILEYLAVRK-------LKGSM-KGPILclVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrg 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958742965 302 ----FVGVGPARVRDLFALARKNAPCILfIDEIDAVGR 335
Cdd:cd19500    82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
50-330 4.43e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 53.23  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965  50 SRFQKGDFPWDDKDFRMYFLWTALFWSGVMIYFLFKSSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVD 129
Cdd:COG1401    15 LRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLAL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 130 GQYVWFNIGSvdtFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPtVLIIAFLLYTIRRGPAGIGRTGRGMGGL 209
Cdd:COG1401    95 SEAAVAIEEL---YELEADSEIEAVGLLLELAERSDALEALERARLLLELA-DLEERAALETEVLEALEAELEELLAAPE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 210 FSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFvnflKNPKQYQDLGA--KIPKGAILTGPPGTGKTLLAKATA---- 283
Cdd:COG1401   171 DLSADALAAELSAAEELYSEDLESEDDYLKDLLRE----KFEETLEAFLAalKTKKNVILAGPPGTGKTYLARRLAealg 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958742965 284 --GEANVPFITV----SGSEFLEMFV--------GVGPARVRDLFALARKN--APCILFIDEI 330
Cdd:COG1401   247 geDNGRIEFVQFhpswSYEDFLLGYRpsldegkyEPTPGIFLRFCLKAEKNpdKPYVLIIDEI 309
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
266-390 5.20e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.21  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAKATAgEA--NVPFITVSGSEFLE-------MFVGVGPARVRD--LFALARKnaPCILFIDEIDavg 334
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958742965 335 rkrgRGNfggqSEQENTLNQLLVE-----MDGFNTT----TNVVILAGTNRPDI----LDPALLRpgRF 390
Cdd:pfam07728  77 ----RAN----PDVLNSLLSLLDErrlllPDGGELVkaapDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
266-381 4.05e-06

RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 46.34  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEA---NVPFITVSgseFLEMFvgvgparVRDLFALARKNAPCILFIDEIDAVGRKRGRGnf 342
Cdd:cd01120     2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTI-------LEAIEDLIEEKKLDIIIIDSLSSLARASQGD-- 69
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958742965 343 ggqsEQENTLNQLLVEMDGFNtTTNVVILAGTNRPDILD 381
Cdd:cd01120    70 ----RSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
AAA_22 pfam13401
AAA domain;
266-381 9.80e-06

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 45.41  E-value: 9.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAK---ATAGEANVPFITV------SGSEFLEMFV------GVGPARVRDLFA-----LARKNAPCIL 325
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAalqqlLLALAVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958742965 326 FIDEIDAVgrkrgrgnfggqseQENTLNqLLVEMDGFNTTTNVVILAGTnrPDILD 381
Cdd:pfam13401  89 IIDEAQHL--------------SLEALE-ELRDLLNLSSKLLQLILVGT--PELRE 127
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
263-298 2.34e-05

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.27  E-value: 2.34e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958742965 263 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF 298
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
266-330 2.44e-05

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 45.18  E-value: 2.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFA-LARKNAPCILFIDEI 330
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAieRPGDLAAiLTNLEPGDVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
267-330 4.26e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.28  E-value: 4.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958742965 267 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFAL---ARKNApcILFIDEI 330
Cdd:PRK00080   56 LYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAleKPGDLAAIltnLEEGD--VLFIDEI 111
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
233-394 7.74e-05

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 45.99  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 233 GCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGA---ILTGPPGTGKTLLAKATA------GEANVPFIT-VSGSEFLEMF 302
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAkiycglGVLRKPLVReVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 303 VGVGPARVRDLF--ALARknapcILFIDEIDA-VGRKRGRGN-FGGQSeqentLNQLLVEMDGfNTTTNVVILAGTNrpD 378
Cdd:TIGR03922 360 IGESEAKTNEIIdsALGG-----VLFLDEAYTlVETGYGQKDpFGLEA-----IDTLLARMEN-DRDRLVVIGAGYR--K 426
                         170       180
                  ....*....|....*....|.
gi 1958742965 379 ILDPAL-----LRpGRFDRQI 394
Cdd:TIGR03922 427 DLDKFLevnegLR-SRFTRVI 446
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
267-463 8.70e-05

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 45.16  E-value: 8.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 267 LTGPPGTGKTLLAKATAGEANVPFITVSGSE----------------FLEMFVGVGParvrdLFAlarknapCILFIDEI 330
Cdd:COG0714    36 LEGVPGVGKTTLAKALARALGLPFIRIQFTPdllpsdilgtyiydqqTGEFEFRPGP-----LFA-------NVLLADEI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 331 DAVGRKrgrgnfggqseqenTLNQLLVEMD------GFNT-----------TTNVVILAGTNR-PDildpALLRpgRFDR 392
Cdd:COG0714   104 NRAPPK--------------TQSALLEAMEerqvtiPGGTyklpepflviaTQNPIEQEGTYPlPE----AQLD--RFLL 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958742965 393 QIFIGPPDIKGRASIFKVHLRplkldsalekdklaRKLASLTPGFSGADVANVcneAALIAARHLSDAINE 463
Cdd:COG0714   164 KLYIGYPDAEEEREILRRHTG--------------RHLAEVEPVLSPEELLAL---QELVRQVHVSEAVLD 217
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
260-332 9.67e-05

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 43.39  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 260 KIPKGAI--LTGPPGTGKTLLAKATAGEANVP--FITVSGSEFLEMFVGVGPARV----------RDLFALARK--NAPC 323
Cdd:cd00267    21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                  ....*....
gi 1958742965 324 ILFIDEIDA 332
Cdd:cd00267   101 LLLLDEPTS 109
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
248-336 1.08e-04

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: 44.51  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 248 LKNPKQYQDLGAKIPKGAI-LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPARVRDLFA------LA 317
Cdd:cd19497    35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKLLQAadydveRA 114
                          90
                  ....*....|....*....
gi 1958742965 318 RKNapcILFIDEIDAVGRK 336
Cdd:cd19497   115 QRG---IVYIDEIDKIARK 130
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
263-301 1.10e-04

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 44.99  E-value: 1.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958742965 263 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF--LEM 301
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVysLEM 93
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
266-331 2.04e-04

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.55  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAKATA-----GEANvpFITVSGSEFLEMF-----VGVGPARV----RDLFALA-RKNAPCILFIDEI 330
Cdd:cd19499    45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122

                  .
gi 1958742965 331 D 331
Cdd:cd19499   123 E 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
267-330 4.20e-04

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 43.15  E-value: 4.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 267 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFA----LARKNapcILFIDEI 330
Cdd:COG2255    59 LYGPPGLGKTTLAHIIANEMGVNIRITS-----------GPAieKPGDLAAiltnLEEGD---VLFIDEI 114
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
258-335 6.59e-04

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 42.29  E-value: 6.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 258 GAKIPKGAI----LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLemfvgvgpaRVRDLFA-LARKNAPCILFIDEIDA 332
Cdd:TIGR00635  22 AAKMRQEALdhllLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAiLTNLEEGDVLFIDEIHR 92

                  ...
gi 1958742965 333 VGR 335
Cdd:TIGR00635  93 LSP 95
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
266-336 1.12e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.07  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 266 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPARVRDLFA------LARKNapcILFIDEIDAVGRK 336
Cdd:PRK05342  112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVGedVENILLKLLQAadydveKAQRG---IVYIDEIDKIARK 188
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
250-380 2.95e-03

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 39.12  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 250 NPKQYQDLGAKIPKGAIL--TGPPGTGKTLLAKA-------TAGEANVPFITVS--GSEFLEMFVGVGPARVRdLFA--- 315
Cdd:cd03246    14 EPPVLRNVSFSIEPGESLaiIGPSGSGKSTLARLilgllrpTSGRVRLDGADISqwDPNELGDHVGYLPQDDE-LFSgsi 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 316 --------------LAR---KNaPCILFIDEIDAvgrkrgrgNFGGQSEQenTLNQLLVEMDGFNTTTnVVIlagTNRPD 378
Cdd:cd03246    93 aenilsggqrqrlgLARalyGN-PRILVLDEPNS--------HLDVEGER--ALNQAIAALKAAGATR-IVI---AHRPE 157

                  ..
gi 1958742965 379 IL 380
Cdd:cd03246   158 TL 159
PRK13341 PRK13341
AAA family ATPase;
265-330 8.30e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.65  E-value: 8.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742965 265 AILTGPPGTGKTLLAKATAGEANVPFI----TVSGSEFLEMFVGVGPARvrdlfaLARKNAPCILFIDEI 330
Cdd:PRK13341   55 LILYGPPGVGKTTLARIIANHTRAHFSslnaVLAGVKDLRAEVDRAKER------LERHGKRTILFIDEV 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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