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Conserved domains on  [gi|110625761|ref|NP_081406|]
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mitochondrial inner membrane m-AAA protease component AFG3L2 [Mus musculus]

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];
156-746 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 816.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 156 VMIYFVFKSSG---REITWKDFVNnYLSKGVVDRLEVVNKRfVRVTFTPGKTpvdgQYVWFNIGSVDTFERNLEtlqqel 232
Cdd:COG0465    6 VLLFNLFSSSSssvKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTLKDGTK----TRFTTYRVNDPELVDLLE------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 233 giegENRVPVVYIAESDGSF----LLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFK 307
Cdd:COG0465   74 ----EKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 387
Cdd:COG0465  143 DVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 388 VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGR 467
Cdd:COG0465  223 VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGR 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 468 FDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQA 547
Cdd:COG0465  303 FDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEA 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 548 IERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCM 626
Cdd:COG0465  379 IDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAV 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 627 TLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVR 701
Cdd:COG0465  459 LLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVR 538
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 110625761 702 ILISDAYRRTVALLTEKKADVEKVALLLLEKEVLDKNDMVQLLGP 746
Cdd:COG0465  539 RIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
156-746 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 816.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 156 VMIYFVFKSSG---REITWKDFVNnYLSKGVVDRLEVVNKRfVRVTFTPGKTpvdgQYVWFNIGSVDTFERNLEtlqqel 232
Cdd:COG0465    6 VLLFNLFSSSSssvKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTLKDGTK----TRFTTYRVNDPELVDLLE------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 233 giegENRVPVVYIAESDGSF----LLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFK 307
Cdd:COG0465   74 ----EKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 387
Cdd:COG0465  143 DVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 388 VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGR 467
Cdd:COG0465  223 VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGR 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 468 FDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQA 547
Cdd:COG0465  303 FDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEA 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 548 IERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCM 626
Cdd:COG0465  379 IDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAV 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 627 TLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVR 701
Cdd:COG0465  459 LLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVR 538
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 110625761 702 ILISDAYRRTVALLTEKKADVEKVALLLLEKEVLDKNDMVQLLGP 746
Cdd:COG0465  539 RIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
252-745 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: 743.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  252 FLLSMLPTVLIIAFLLYTIRRGPAGIGrtgrgmGGLFSVGETTAKVLKDE-IDVKFKDVAGCEEAKLEIMEFVNFLKNPK 330
Cdd:TIGR01241   5 FLFSLLPPILLLVGVWFFFRRQMQGGG------GRAFSFGKSKAKLLNEEkPKVTFKDVAGIDEAKEELMEIVDFLKNPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  331 QYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDA 410
Cdd:TIGR01241  79 KFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  411 VGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHL 490
Cdd:TIGR01241 159 VGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  491 RPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTV 570
Cdd:TIGR01241 239 KNKKLAPDVDLKAVAR----RTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  571 AYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDL 649
Cdd:TIGR01241 315 AYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  650 RKVTQSAYAQIVQFGMNEKVGQISFDlPRQGDMVL------EKPYSEATARMIDDEVRILISDAYRRTVALLTEKKADVE 723
Cdd:TIGR01241 395 KQATNIARAMVTEWGMSDKLGPVAYG-SDGGDVFLgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELE 473
                         490       500
                  ....*....|....*....|..
gi 110625761  724 KVALLLLEKEVLDKNDMVQLLG 745
Cdd:TIGR01241 474 LLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
251-756 2.82e-180

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 531.55  E-value: 2.82e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 251 SFLLsmLPtVLIIAFLLYTIRRG---PAGIGRtgrgmgGLFSVGETTAKVLKD-EIDVKFKDVAGCEEAKLEIMEFVNFL 326
Cdd:CHL00176 132 SNLL--LP-LILIGVLWFFFQRSsnfKGGPGQ------NLMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 327 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 406
Cdd:CHL00176 203 KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFID 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 407 EIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIF 486
Cdd:CHL00176 283 EIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 487 KVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEkKTQVLQPEE 566
Cdd:CHL00176 363 KVHARNKKLSPDVSLELIARR----TPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKN 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 567 KKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLP-KEQYLYTKEQLLDRMCMTLGGRVSEEIFFG--RITT 643
Cdd:CHL00176 438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTT 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 644 GAQDDLRKVTQSAYAQIVQFGMNeKVGQISFDLPRQGD------MVLEKPYSEATARMIDDEVRILISDAYRRTVALLTE 717
Cdd:CHL00176 518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 110625761 718 KKADVEKVALLLLEKEVLDKNDMVQLLGPR-PFTEKSTYE 756
Cdd:CHL00176 597 NRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
304-474 2.65e-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: 348.84  E-value: 2.65e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 304 VKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 383
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 384 GPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALL 463
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 110625761 464 RPGRFDRQIFI 474
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
561-743 2.08e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 277.17  E-value: 2.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  561 VLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYTKEQLLDRMCMTLGGRVSEEIFFG 639
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  640 RITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDlPRQG------DMVLEKPYSEATARMIDDEVRILISDAYRRTVA 713
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 110625761  714 LLTEKKADVEKVALLLLEKEVLDKNDMVQL 743
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
340-478 4.48e-20

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: 87.43  E-value: 4.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761   340 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDLFALARKNAPCI 402
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625761   403 LFIDEIDAVGRKRgrgnfggqSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPgRFDRQIFIGPPD 478
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
156-746 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 816.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 156 VMIYFVFKSSG---REITWKDFVNnYLSKGVVDRLEVVNKRfVRVTFTPGKTpvdgQYVWFNIGSVDTFERNLEtlqqel 232
Cdd:COG0465    6 VLLFNLFSSSSssvKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTLKDGTK----TRFTTYRVNDPELVDLLE------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 233 giegENRVPVVYIAESDGSF----LLSMLPTVLIIAFLLYTIRRgpagigrTGRGMGGLFSVGETTAKVL-KDEIDVKFK 307
Cdd:COG0465   74 ----EKGVEVTAKPPEESSWllslLISLLPILLLIGLWIFFMRR-------MQGGGGGAMSFGKSKAKLYdEDKPKVTFD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 387
Cdd:COG0465  143 DVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 388 VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGR 467
Cdd:COG0465  223 VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGR 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 468 FDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQA 547
Cdd:COG0465  303 FDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIAR----RTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEA 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 548 IERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCM 626
Cdd:COG0465  379 IDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAV 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 627 TLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQ-----GDMVLEKPYSEATARMIDDEVR 701
Cdd:COG0465  459 LLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgRDIGQSRNYSEETAREIDEEVR 538
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 110625761 702 ILISDAYRRTVALLTEKKADVEKVALLLLEKEVLDKNDMVQLLGP 746
Cdd:COG0465  539 RIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
252-745 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: 743.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  252 FLLSMLPTVLIIAFLLYTIRRGPAGIGrtgrgmGGLFSVGETTAKVLKDE-IDVKFKDVAGCEEAKLEIMEFVNFLKNPK 330
Cdd:TIGR01241   5 FLFSLLPPILLLVGVWFFFRRQMQGGG------GRAFSFGKSKAKLLNEEkPKVTFKDVAGIDEAKEELMEIVDFLKNPS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  331 QYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDA 410
Cdd:TIGR01241  79 KFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  411 VGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHL 490
Cdd:TIGR01241 159 VGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  491 RPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTV 570
Cdd:TIGR01241 239 KNKKLAPDVDLKAVAR----RTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  571 AYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKE-QYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDL 649
Cdd:TIGR01241 315 AYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  650 RKVTQSAYAQIVQFGMNEKVGQISFDlPRQGDMVL------EKPYSEATARMIDDEVRILISDAYRRTVALLTEKKADVE 723
Cdd:TIGR01241 395 KQATNIARAMVTEWGMSDKLGPVAYG-SDGGDVFLgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELE 473
                         490       500
                  ....*....|....*....|..
gi 110625761  724 KVALLLLEKEVLDKNDMVQLLG 745
Cdd:TIGR01241 474 LLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
251-756 2.82e-180

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 531.55  E-value: 2.82e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 251 SFLLsmLPtVLIIAFLLYTIRRG---PAGIGRtgrgmgGLFSVGETTAKVLKD-EIDVKFKDVAGCEEAKLEIMEFVNFL 326
Cdd:CHL00176 132 SNLL--LP-LILIGVLWFFFQRSsnfKGGPGQ------NLMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 327 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 406
Cdd:CHL00176 203 KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFID 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 407 EIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIF 486
Cdd:CHL00176 283 EIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 487 KVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEkKTQVLQPEE 566
Cdd:CHL00176 363 KVHARNKKLSPDVSLELIARR----TPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKN 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 567 KKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLP-KEQYLYTKEQLLDRMCMTLGGRVSEEIFFG--RITT 643
Cdd:CHL00176 438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTT 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 644 GAQDDLRKVTQSAYAQIVQFGMNeKVGQISFDLPRQGD------MVLEKPYSEATARMIDDEVRILISDAYRRTVALLTE 717
Cdd:CHL00176 518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 110625761 718 KKADVEKVALLLLEKEVLDKNDMVQLLGPR-PFTEKSTYE 756
Cdd:CHL00176 597 NRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
251-768 3.45e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 482.61  E-value: 3.45e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 251 SFLLSMLPTVLIIAFLLYTIRRGPAGIGRtgrgmgGLFSVGETTAKVL-KDEIDVKFKDVAGCEEAKLEIMEFVNFLKNP 329
Cdd:PRK10733 101 SIFISWFPMLLLIGVWIFFMRQMQGGGGK------GAMSFGKSKARMLtEDQIKTTFADVAGCDEAKEEVAELVEYLREP 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 330 KQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEID 409
Cdd:PRK10733 175 SRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEID 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 410 AVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVH 489
Cdd:PRK10733 255 AVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVH 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 490 LRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKT 569
Cdd:PRK10733 335 MRRVPLAPDIDAAIIARG----TPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 570 VAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTL-GGRVSEEIFFG--RITTGAQ 646
Cdd:PRK10733 411 TAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLyGGRLAEEIIYGpeHVSTGAS 490
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 647 DDLRKVTQSAYAQIVQFGMNEKVGQISFdLPRQGDMVL------EKPYSEATARMIDDEVRILISDAYRRTVALLTEKKA 720
Cdd:PRK10733 491 NDIKVATNLARNMVTQWGFSEKLGPLLY-AEEEGEVFLgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMD 569
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 110625761 721 DVEKVALLLLEKEVLDKNDMVQLLGPRPFTEKSTYEEfVEGTGSLDED 768
Cdd:PRK10733 570 ILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEE-PGASNNSDDN 616
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
304-474 2.65e-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: 348.84  E-value: 2.65e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 304 VKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 383
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 384 GPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALL 463
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 110625761 464 RPGRFDRQIFI 474
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
303-559 2.46e-112

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 344.68  E-value: 2.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 303 DVKFKDVAGCEEAKLEIMEFV-NFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 381
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 382 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 461
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 462 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 541
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAK----LTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307
                        250
                 ....*....|....*...
gi 110625761 542 KHFEQAIERVIGGLEKKT 559
Cdd:COG1222  308 EDLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
303-558 3.67e-95

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 302.14  E-value: 3.67e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 303 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 381
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 382 GVGpAR-VRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDP 460
Cdd:PRK03992 207 GEG-ARlVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 461 ALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAIN 540
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAE----LTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*...
gi 110625761 541 EKHFEQAIERVIGGLEKK 558
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
561-743 2.08e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 277.17  E-value: 2.08e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  561 VLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYTKEQLLDRMCMTLGGRVSEEIFFG 639
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  640 RITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDlPRQG------DMVLEKPYSEATARMIDDEVRILISDAYRRTVA 713
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 110625761  714 LLTEKKADVEKVALLLLEKEVLDKNDMVQL 743
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
303-552 7.13e-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: 261.27  E-value: 7.13e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  303 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 381
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  382 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 461
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  462 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARklasLTPGFSGADVANVCNEAALIAARHLSDAINE 541
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAK----MTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 110625761  542 KHFEQAIERVI 552
Cdd:TIGR01242 354 DDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
183-551 6.54e-79

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: 259.84  E-value: 6.54e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 183 VVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLI 262
Cdd:COG0464   31 LALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 263 IAFLLYTIRRGPAGIGRTGRGMGGLFSVGE--TTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVN-FLKNPKQYQDLGAKI 339
Cdd:COG0464  111 LLDLERALLELLRESAEALALAAPLVTYEDigGLEEELLELREAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPP 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 340 PKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGN 419
Cdd:COG0464  191 PRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 420 FGGQSEQentLNQLLVEMDGFntTTNVVILAGTNRPDILDPALLRpgRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSAL 499
Cdd:COG0464  271 DGVGRRV---VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDV 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110625761 500 EKDKLARKlaslTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERV 551
Cdd:COG0464  344 DLEELAEA----TEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
296-557 3.00e-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: 245.59  E-value: 3.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  296 KVLKDEIDVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGS 374
Cdd:TIGR01243 442 EVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  375 EFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNR 454
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNR 599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  455 PDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKlaslTPGFSGADVANVCNEAALIAARH 534
Cdd:TIGR01243 600 PDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEM----TEGYTGADIEAVCREAAMAALRE 675
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 110625761  535 LSDA------------------INEKHFEQAIERVIGGLEK 557
Cdd:TIGR01243 676 SIGSpakeklevgeeeflkdlkVEMRHFLEALKKVKPSVSK 716
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
306-472 4.08e-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: 222.60  E-value: 4.08e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 306 FKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 384
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 385 PARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLR 464
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                 ....*...
gi 110625761 465 PGRFDRQI 472
Cdd:cd19502  162 PGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
303-552 5.42e-64

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 219.63  E-value: 5.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 303 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 381
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 382 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 461
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 462 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALE-KDKLARklaslTPGFSGADVANVCNEAALIAARHLSDAIN 540
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDlEDFVSR-----PEKISAADIAAICQEAGMQAVRKNRYVIL 375
                        250
                 ....*....|..
gi 110625761 541 EKHFEQAIERVI 552
Cdd:PTZ00454 376 PKDFEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
297-552 3.93e-62

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 215.79  E-value: 3.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 297 VLKDEIDV-------------KFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAG 362
Cdd:PTZ00361 160 ILLDEVDPlvsvmkvdkapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVAN 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 363 EANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNT 442
Cdd:PTZ00361 240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDS 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 443 TTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKL--DSALE-----KDKLarklasltpgf 515
Cdd:PTZ00361 320 RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLaeDVDLEefimaKDEL----------- 388
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 110625761 516 SGADVANVCNEAALIAARHLSDAINEKHFEQAIERVI 552
Cdd:PTZ00361 389 SGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVL 425
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
306-568 3.07e-61

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 206.66  E-value: 3.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 306 FKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 385
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 386 ARVRDLFALARkNAPCILFIDEIDAVGRKRGRGNFGGqsEQENTLNQLLVEMDGFNttTNVVILAGTNRPDILDPALLRp 465
Cdd:COG1223   81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 466 gRFDRQIFIGPPDIKGRASIFKVHLRPLKldsaLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFE 545
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFP----LPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229
                        250       260
                 ....*....|....*....|...
gi 110625761 546 QAIErvigglEKKTQVLQPEEKK 568
Cdd:COG1223  230 EALK------QRKERKKEPKKEG 246
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
303-535 5.09e-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: 219.78  E-value: 5.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  303 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 381
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  382 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQEnTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPA 461
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVEKR-VVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110625761  462 LLRPGRFDRQIFIGPPDIKGRASIFKVHLRplklDSALEKDKLARKLASLTPGFSGADVANVCNEAALIAARHL 535
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTR----NMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRF 400
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
315-474 7.51e-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: 202.51  E-value: 7.51e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 315 AKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 394
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 395 ARKNAPCILFIDEIDAVGRKRGRGnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 474
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSS--GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
315-474 1.36e-59

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: 199.05  E-value: 1.36e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 315 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFA 393
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 394 LARKNAPCILFIDEIDAVGRKRGrGNFGGQSeQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 473
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRG-QSDSSGV-TDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 110625761 474 I 474
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 ...
308-474 1.14e-56

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: 191.35  E-value: 1.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 386
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 387 RVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRP 465
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 110625761 466 GRFDRQIFI 474
Cdd:cd19503  157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
315-474 7.76e-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: 7.76e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 315 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFA 393
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 394 LARKNAPCILFIDEIDAVGRKRGRGnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 473
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTT--GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 110625761 474 I 474
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 ...
316-474 1.52e-52

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: 180.01  E-value: 1.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 316 KLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 394
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 395 ARKNAPCILFIDEIDAVGRKRGrGNFGGQS-EQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 473
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARG-GNIGDAGgAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 110625761 474 I 474
Cdd:cd19528  161 I 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
344-475 1.99e-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: 178.17  E-value: 1.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  344 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfGGQ 423
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110625761  424 SEQENTLNQLLVEMDGF-NTTTNVVILAGTNRPDILDPALLrpGRFDRQIFIG 475
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 ...
308-475 9.05e-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: 172.24  E-value: 9.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 386
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 387 RVRDLFALARKNAPCILFIDEIDAVGRKRGRGNfgGQSEQEnTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPG 466
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 110625761 467 RFDRQIFIG 475
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 ...
320-474 6.06e-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: 169.98  E-value: 6.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 320 MEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNA 399
Cdd:cd19530   10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625761 400 PCILFIDEIDAVGRKRGRgnfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 474
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 ...
308-472 6.62e-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: 161.80  E-value: 6.62e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNFLKNPKQ-YQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 386
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 387 RVRDLFALARKNAPCILFIDEIDAVGRKRGrgnfGGQSEQENTL-NQLLVEMDGFN----TTTNVVILAGTNRPDILDPA 461
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE----SAQREMERRIvSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                        170
                 ....*....|.
gi 110625761 462 LLRPGRFDRQI 472
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 ...
327-473 3.65e-44

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: 156.43  E-value: 3.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 327 KNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFID 406
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625761 407 EIDAVGRKRGRGNFGgqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIF 473
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 ...
316-474 3.61e-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: 148.04  E-value: 3.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 316 KLEIMEFVNF-LKNPKQYQDlGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFAL 394
Cdd:cd19527    2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 395 ARKNAPCILFIDEIDAVGRKRGR-GNFGGQSEQenTLNQLLVEMDGFNTTT-NVVILAGTNRPDILDPALLRPGRFDRQI 472
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 110625761 473 FI 474
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 ...
309-474 2.24e-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: 137.48  E-value: 2.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 309 VAGCEEAKLEIMEFVNF-LKNPKQYQdLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 387
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 388 VRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTN--VVILAGTNRPDILDPALLR 464
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 110625761 465 pgRFDRQIFI 474
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
303-474 1.06e-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: 127.29  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 303 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 380
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 381 VGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGF-NTTTNVVILAGTNRPDIL 458
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIkTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                        170
                 ....*....|....*.
gi 110625761 459 DPALLRpgRFDRQIFI 474
Cdd:cd19521  157 DSAIRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
308-468 1.14e-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: 121.38  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLG-AKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 385
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 386 ARVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfggqSEQENTL---NQLLVEMDGFNTTTN--VVILAGTNRPDILDP 460
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDE 154
                        170
                 ....*....|
gi 110625761 461 ALLR--PGRF 468
Cdd:cd19520  155 AILRrmPKRF 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
308-473 2.92e-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: 120.31  E-value: 2.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEAN-----VPFITVSGSEFLEMFV 381
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 382 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfggQSEQENT----LNQLLVEMDGFNTTTNVVILAGTNRPDI 457
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....*.
gi 110625761 458 LDPALLRPGRFDRQIF 473
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; ...
303-474 1.11e-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: 119.32  E-value: 1.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 303 DVKFKDVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 381
Cdd:cd19525   18 PINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 382 GVGPARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfgGQSEQENTL---NQLLVEMDGFNTTTN--VVILAGTNRPD 456
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR------GEGEHESSRrikTEFLVQLDGATTSSEdrILVVGATNRPQ 170
                        170
                 ....*....|....*...
gi 110625761 457 ILDPALLRpgRFDRQIFI 474
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; ...
329-474 6.65e-30

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: 116.44  E-value: 6.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 329 PKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANV--PFItVSGSEFLEMFVGVGPARVRDLFALA-----RKNAPC 401
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAeeeqrRLGANS 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625761 402 ---ILFIDEIDAVGRKRGRGNfGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 474
Cdd:cd19504  103 glhIIIFDEIDAICKQRGSMA-GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
308-474 3.91e-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: 113.79  E-value: 3.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 386
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 387 RVRDLFALARKNAPCILFIDEIDAVGRKRGRgnfgGQSEQENTL-NQLLVEMDGFNTTTN--VVILAGTNRPDILDPALL 463
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 110625761 464 RpgRFDRQIFI 474
Cdd:cd19524  156 R--RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
308-474 5.07e-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: 5.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 385
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 386 ARVRDLFALARKNAPCILFIDEIDAVGRKRgrgnfGGQSEQENTL---NQLLVEMDGF-NTTTN------VVILAGTNRP 455
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR-----GTSEEHEASRrvkSELLVQMDGVgGASENddpskmVMVLAATNFP 153
                        170
                 ....*....|....*....
gi 110625761 456 DILDPALLRpgRFDRQIFI 474
Cdd:cd19522  154 WDIDEALRR--RLEKRIYI 170
ycf46 CHL00195
Ycf46; Provisional
303-542 1.67e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 120.12  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 303 DVKFKDVAGCEEAKleimEFVNFLKN--PKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 380
Cdd:CHL00195 224 NEKISDIGGLDNLK----DWLKKRSTsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 381 VGVGPARVRDLFALARKNAPCILFIDEID-AVGRKRGRGNFGGQSEQENTLNQLLVEmdgfnTTTNVVILAGTNRPDILD 459
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLP 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 460 PALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDklARKLASLTPGFSGADVanvcnEAALIAARHLsdAI 539
Cdd:CHL00195 375 LEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYD--IKKLSKLSNKFSGAEI-----EQSIIEAMYI--AF 445

                 ...
gi 110625761 540 NEK 542
Cdd:CHL00195 446 YEK 448
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
340-476 7.81e-27

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: 106.85  E-value: 7.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 340 PKGAILTGPPGTGKTLLAKATAGEA---NVPFITVSGSEFLEMFVG---VGPARVRDLFALARKNAPCILFIDEIDAVGR 413
Cdd:cd00009   19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625761 414 KrgrgnfggqsEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGP 476
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 ...
330-474 1.58e-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: 94.74  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 330 KQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEID 409
Cdd:cd19507   21 KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625761 410 avgrkRGRGNFGGQSEQENT---LNQLLVEMDgfNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 474
Cdd:cd19507  101 -----KGFSNADSKGDSGTSsrvLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
340-478 4.48e-20

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: 87.43  E-value: 4.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761   340 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDLFALARKNAPCI 402
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625761   403 LFIDEIDAVGRKRgrgnfggqSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPgRFDRQIFIGPPD 478
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
325-474 3.83e-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: 3.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 325 FLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEflemfVGVGPARVRDLFALARKNApcILF 404
Cdd:cd19510    8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625761 405 IDEIDA--VGRKR-GRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 474
Cdd:cd19510   81 LEDIDAafESREHnKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
335-474 3.57e-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: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 335 LGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFL--------------EMFVGVGPARVRDLFALARKNAP 400
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625761 401 CILFIDEIDAVGRKRgrgnFGGQSEQENT-----LNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFI 474
Cdd:cd19505   87 CIIWIPNIHELNVNR----STQNLEEDPKlllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
308-474 7.53e-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: 72.99  E-value: 7.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 308 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLgAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 386
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 387 RVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQentlNQLLVEMDGFNTTT--NVVILAGTNRPDILDPALLR 464
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQ----VELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
                        170
                 ....*....|
gi 110625761 465 pgRFDRQIFI 474
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 ...
507-546 2.15e-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: 62.17  E-value: 2.15e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 110625761  507 KLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQ 546
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
344-408 4.20e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 62.41  E-value: 4.20e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625761 344 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDLFALARKNA----PCILFIDEI 408
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
344-408 4.85e-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: 4.85e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625761 344 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDLFALARKNA----PCILFIDEI 408
Cdd:COG2256   53 ILWGPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
305-425 2.25e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 60.70  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 305 KFKDVAGCEEAKLEIMEFV-NFLKNpkqyqdlgaKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEF-----LE 378
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 110625761 379 MFVGVGpARVRDLFALARKnapcILFIDEIDAVgrkRGRGNFGGQSE 425
Cdd:PRK04195  83 RVAGEA-ATSGSLFGARRK----LILLDEVDGI---HGNEDRGGARA 121
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
340-409 3.63e-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: 56.43  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  340 PKGAIL-TGPPGTGKTLLAKATAGEANV---PFITVSGSEFLE-----MFVGVGPARVR-----DLFALARKNAPCILFI 405
Cdd:pfam07724   2 PIGSFLfLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                  ....
gi 110625761  406 DEID 409
Cdd:pfam07724  82 DEIE 85
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
339-468 4.52e-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: 56.62  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 339 IPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVGvgparvRDLFALARKNAPCILFIDEIDAVGRKRGR 417
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGS 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625761 418 GnfGGQSEQENTLNQLL--VEMDGFNTTTNVV-------ILAGT---NRPDILDPALlrPGRF 468
Cdd:cd19498  119 S--GPDVSREGVQRDLLpiVEGSTVSTKYGPVktdhilfIAAGAfhvAKPSDLIPEL--QGRF 177
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
344-462 6.39e-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: 55.61  E-value: 6.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 344 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMfvGV-GPARVRDLFALARK-NAPCILFIDEIDAVGRKRgrgNFG 421
Cdd:cd19512   26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR---STE 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 110625761 422 GQSE-QENTLNQLLVEMdGFNTTTNVVILAgTNRPDILDPAL 462
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 ...
145-241 4.77e-08

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: 51.45  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  145 YFLWTALFWGGVMIYFVF----KSSGREITWKDFVNnYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGS--- 217
Cdd:pfam06480   1 LLLWLLILLVLLLLFLLFllssSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFTTYFIPSlpn 79
                          90       100
                  ....*....|....*....|....
gi 110625761  218 VDTFERNLETLQQELGIEGENRVP 241
Cdd:pfam06480  80 VDSLLEKLEDALEEKGVKVSVKPP 103
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
318-551 1.88e-07

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 53.03  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 318 EIMEFVNFLKNpkqYQDLGakipkgaILTGPPGTGKTLLAKATAGE-ANVPFITVSGS----EFL-----EMFVGVGPAR 387
Cdd:COG2842   38 RFAEALDEARA---LPGIG-------VVYGESGVGKTTAAREYANRnPNVIYVTASPSwtskELLeelaeELGIPAPPGT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 388 VRDLF-ALARKNAPCI--LFIDEIDAVGRKrgrgnfggqseqenTLNQLlveMDGFNTTTNVVILAGTNRPdildPALLR 464
Cdd:COG2842  108 IADLRdRILERLAGTGrlLIIDEADHLKPK--------------ALEEL---RDIHDETGVGVVLIGMERL----PAKLK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 465 pgRFDRqifigppdIKGRASiFKVHLRPLKLDSA---------LEKDKLARKLASLTpgfSGA--DVANVCNEAALIAAR 533
Cdd:COG2842  167 --RYEQ--------LYSRIG-FWVEFKPLSLEDVralaeawgeLTDPDLLELLHRIT---RGNlrRLDRTLRLAARAAKR 232
                        250
                 ....*....|....*...
gi 110625761 534 HLSDAINEKHFEQAIERV 551
Cdd:COG2842  233 NGLTKITLDHVRAAALML 250
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
128-408 2.10e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 54.39  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 128 SRFQKGDFPWDDKDFRMYFLWTALFWGGVMIYFVFKSSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVD 207
Cdd:COG1401   15 LRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLAL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 208 GQYVWFNIGSvdtFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPtVLIIAFLLYTIRRGPAGIGRTGRGMGGL 287
Cdd:COG1401   95 SEAAVAIEEL---YELEADSEIEAVGLLLELAERSDALEALERARLLLELA-DLEERAALETEVLEALEAELEELLAAPE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 288 FSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFvnflKNPKQYQDLGA--KIPKGAILTGPPGTGKT----LLAKATA 361
Cdd:COG1401  171 DLSADALAAELSAAEELYSEDLESEDDYLKDLLRE----KFEETLEAFLAalKTKKNVILAGPPGTGKTylarRLAEALG 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625761 362 GEA--NVPFITV----SGSEFLEMFV--------GVGPARVRDLFALARKN--APCILFIDEI 408
Cdd:COG1401  247 GEDngRIEFVQFhpswSYEDFLLGYRpsldegkyEPTPGIFLRFCLKAEKNpdKPYVLIIDEI 309
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
307-413 4.08e-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: 51.02  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 307 KDVAGCEEAKLEIMEFVNFLKnpkqyqdLGAKIpKGAIL--TGPPGTGKTLLAKATAGEANVPFITVS-G--SEFLEM-- 379
Cdd:cd19500   10 ADHYGLEDVKERILEYLAVRK-------LKGSM-KGPILclVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrg 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 110625761 380 ----FVGVGPARVRDLFALARKNAPCILfIDEIDAVGR 413
Cdd:cd19500   82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
344-468 5.00e-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: 49.60  E-value: 5.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  344 ILTGPPGTGKTLLAKATAgEA--NVPFITVSGSEFLE-------MFVGVGPARVRD--LFALARKnaPCILFIDEIDavg 412
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625761  413 rkrgRGNfggqSEQENTLNQLLVE-----MDGFNTT----TNVVILAGTNRPDI----LDPALLRpgRF 468
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 ...
344-459 1.75e-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: 47.50  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 344 ILTGPPGTGKTLLAKATAGEA---NVPFITVSgseFLEMFvgvgparVRDLFALARKNAPCILFIDEIDAVGRKRGRGnf 420
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTI-------LEAIEDLIEEKKLDIIIIDSLSSLARASQGD-- 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 110625761 421 ggqsEQENTLNQLLVEMDGFNtTTNVVILAGTNRPDILD 459
Cdd:cd01120   70 ----RSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
AAA_22 pfam13401
AAA domain;
344-459 6.71e-06

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  344 ILTGPPGTGKTLLAK---ATAGEANVPFITV------SGSEFLEMFV------GVGPARVRDLFA-----LARKNAPCIL 403
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAalqqlLLALAVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110625761  404 FIDEIDAVgrkrgrgnfggqseQENTLNqLLVEMDGFNTTTNVVILAGTnrPDILD 459
Cdd:pfam13401  89 IIDEAQHL--------------SLEALE-ELRDLLNLSSKLLQLILVGT--PELRE 127
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
341-376 1.75e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.04  E-value: 1.75e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 110625761 341 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF 376
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
344-408 2.68e-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: 2.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625761  344 ILTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFA-LARKNAPCILFIDEI 408
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAieRPGDLAAiLTNLEPGDVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
345-408 3.92e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.66  E-value: 3.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625761 345 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFAL---ARKNApcILFIDEI 408
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 ...
311-472 6.43e-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: 46.38  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  311 GCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGA---ILTGPPGTGKTLLAKATA------GEANVPFIT-VSGSEFLEMF 380
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAkiycglGVLRKPLVReVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  381 VGVGPARVRDLF--ALARknapcILFIDEIDA-VGRKRGRGN-FGGQSeqentLNQLLVEMDGfNTTTNVVILAGTNrpD 456
Cdd:TIGR03922 360 IGESEAKTNEIIdsALGG-----VLFLDEAYTlVETGYGQKDpFGLEA-----IDTLLARMEN-DRDRLVVIGAGYR--K 426
                         170       180
                  ....*....|....*....|.
gi 110625761  457 ILDPAL-----LRpGRFDRQI 472
Cdd:TIGR03922 427 DLDKFLevnegLR-SRFTRVI 446
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
326-414 7.96e-05

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: 44.90  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 326 LKNPKQYQDLGAKIPKGAI-LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPARVRDLFA------LA 395
Cdd:cd19497   35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKLLQAadydveRA 114
                         90
                 ....*....|....*....
gi 110625761 396 RKNapcILFIDEIDAVGRK 414
Cdd:cd19497  115 QRG---IVYIDEIDKIARK 130
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
341-379 8.26e-05

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: 45.76  E-value: 8.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 110625761  341 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF--LEM 379
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVysLEM 93
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
338-410 8.32e-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: 43.77  E-value: 8.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 338 KIPKGAI--LTGPPGTGKTLLAKATAGEANVP--FITVSGSEFLEMFVGVGPARV----------RDLFALARK--NAPC 401
Cdd:cd00267   21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                 ....*....
gi 110625761 402 ILFIDEIDA 410
Cdd:cd00267  101 LLLLDEPTS 109
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
345-541 8.57e-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: 8.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 345 LTGPPGTGKTLLAKATAGEANVPFITVSGSE----------------FLEMFVGVGParvrdLFAlarknapCILFIDEI 408
Cdd:COG0714   36 LEGVPGVGKTTLAKALARALGLPFIRIQFTPdllpsdilgtyiydqqTGEFEFRPGP-----LFA-------NVLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 409 DAVGRKrgrgnfggqseqenTLNQLLVEMD------GFNT-----------TTNVVILAGTNR-PDildpALLRpgRFDR 470
Cdd:COG0714  104 NRAPPK--------------TQSALLEAMEerqvtiPGGTyklpepflviaTQNPIEQEGTYPlPE----AQLD--RFLL 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110625761 471 QIFIGPPDIKGRASIFKVHLRplkldsalekdklaRKLASLTPGFSGADVANVcneAALIAARHLSDAINE 541
Cdd:COG0714  164 KLYIGYPDAEEEREILRRHTG--------------RHLAEVEPVLSPEELLAL---QELVRQVHVSEAVLD 217
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
344-409 1.55e-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: 43.32  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 344 ILTGPPGTGKTLLAKATA-----GEANvpFITVSGSEFLEMF-----VGVGPARV----RDLFALA-RKNAPCILFIDEI 408
Cdd:cd19499   45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122

                 .
gi 110625761 409 D 409
Cdd:cd19499  123 E 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
345-408 4.60e-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: 4.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 345 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDLFA----LARKNapcILFIDEI 408
Cdd:COG2255   59 LYGPPGLGKTTLAHIIANEMGVNIRITS-----------GPAieKPGDLAAiltnLEEGD---VLFIDEI 114
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
336-413 5.94e-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: 42.67  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761  336 GAKIPKGAI----LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLemfvgvgpaRVRDLFA-LARKNAPCILFIDEIDA 410
Cdd:TIGR00635  22 AAKMRQEALdhllLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAiLTNLEEGDVLFIDEIHR 92

                  ...
gi 110625761  411 VGR 413
Cdd:TIGR00635  93 LSP 95
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
344-414 8.51e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.45  E-value: 8.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 344 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPARVRDLFA------LARKNapcILFIDEIDAVGRK 414
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 ...
328-458 3.37e-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: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 328 NPKQYQDLGAKIPKGAIL--TGPPGTGKTLLAKA-------TAGEANVPFITVS--GSEFLEMFVGVGPARVRdLFA--- 393
Cdd:cd03246   14 EPPVLRNVSFSIEPGESLaiIGPSGSGKSTLARLilgllrpTSGRVRLDGADISqwDPNELGDHVGYLPQDDE-LFSgsi 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 394 --------------LAR---KNaPCILFIDEIDAvgrkrgrgNFGGQSEQenTLNQLLVEMDGFNTTTnVVIlagTNRPD 456
Cdd:cd03246   93 aenilsggqrqrlgLARalyGN-PRILVLDEPNS--------HLDVEGER--ALNQAIAALKAAGATR-IVI---AHRPE 157

                 ..
gi 110625761 457 IL 458
Cdd:cd03246  158 TL 159
PRK13341 PRK13341
AAA family ATPase;
343-408 9.34e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.65  E-value: 9.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625761 343 AILTGPPGTGKTLLAKATAGEANVPFI----TVSGSEFLEMFVGVGPARvrdlfaLARKNAPCILFIDEI 408
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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