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Conserved domains on  [gi|24665814|ref|NP_730250|]
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AFG3 like matrix AAA peptidase subunit 2, isoform B [Drosophila melanogaster]

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];
39-636 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 800.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  39 AIGAVVLVGSFAFFEMGYKEISWKEFVNsYLSKGVVEKLEVVNKKwVRVRLqqnSNSGSGVLWFNIGSVDSFERNLEAAQ 118
Cdd:COG0465   2 ALLLVLLFNLFSSSSSSVKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTL---KDGTKTRFTTYRVNDPELVDLLEEKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 119 teqgtesinfVPVIYRNEVEAASLTGLL----PTLLIIGFLVYMMRKSADMMGGgrgrkggglfggVMQ---STAKLTNP 191
Cdd:COG0465  77 ----------VEVTAKPPEESSWLLSLLisllPILLLIGLWIFFMRRMQGGGGG------------AMSfgkSKAKLYDE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 192 NEIGVGFKDVAGCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM 271
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 272 FVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILD 351
Cdd:COG0465 215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 352 KALMRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKtsLDKN-ELsRKMAALTPGFTGADIANVCNEAALIAARDSKDSIV 430
Cdd:COG0465 295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDvDL-EVIARRTPGFSGADLANLVNEAALLAARRNKKAVT 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 431 LKHFEQAIERVIAGMEKKTNVLAPEEKRTVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLPK-DHYLLSKEQ 509
Cdd:COG0465 372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEeDRYLYTKEE 451
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 510 LFDRMCMTLGGRVAEELFFNRITTGAQDDLKKITDIAYSQVVRFGMNEKVGQVSFdvGQAGDPVF-------SKPYSEDT 582
Cdd:COG0465 452 LLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY--GESEGEVFlgrdigqSRNYSEET 529
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....
gi 24665814 583 AQLIDNEVRSIIKCAHEATTSLLTKHKENVQKVAERLLQNEVLSRDDMIELLGP 636
Cdd:COG0465 530 AREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
39-636 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 800.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  39 AIGAVVLVGSFAFFEMGYKEISWKEFVNsYLSKGVVEKLEVVNKKwVRVRLqqnSNSGSGVLWFNIGSVDSFERNLEAAQ 118
Cdd:COG0465   2 ALLLVLLFNLFSSSSSSVKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTL---KDGTKTRFTTYRVNDPELVDLLEEKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 119 teqgtesinfVPVIYRNEVEAASLTGLL----PTLLIIGFLVYMMRKSADMMGGgrgrkggglfggVMQ---STAKLTNP 191
Cdd:COG0465  77 ----------VEVTAKPPEESSWLLSLLisllPILLLIGLWIFFMRRMQGGGGG------------AMSfgkSKAKLYDE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 192 NEIGVGFKDVAGCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM 271
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 272 FVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILD 351
Cdd:COG0465 215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 352 KALMRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKtsLDKN-ELsRKMAALTPGFTGADIANVCNEAALIAARDSKDSIV 430
Cdd:COG0465 295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDvDL-EVIARRTPGFSGADLANLVNEAALLAARRNKKAVT 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 431 LKHFEQAIERVIAGMEKKTNVLAPEEKRTVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLPK-DHYLLSKEQ 509
Cdd:COG0465 372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEeDRYLYTKEE 451
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 510 LFDRMCMTLGGRVAEELFFNRITTGAQDDLKKITDIAYSQVVRFGMNEKVGQVSFdvGQAGDPVF-------SKPYSEDT 582
Cdd:COG0465 452 LLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY--GESEGEVFlgrdigqSRNYSEET 529
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....
gi 24665814 583 AQLIDNEVRSIIKCAHEATTSLLTKHKENVQKVAERLLQNEVLSRDDMIELLGP 636
Cdd:COG0465 530 AREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
142-635 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: 701.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   142 LTGLLPTLLIIGFLVYMMRKSADMMGGGrgrkggglfggVM---QSTAKLTNPNEIGVGFKDVAGCEEAKIEIMEFVNFL 218
Cdd:TIGR01241   6 LFSLLPPILLLVGVWFFFRRQMQGGGGR-----------AFsfgKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   219 KNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFID 298
Cdd:TIGR01241  75 KNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFID 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   299 EIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASIF 378
Cdd:TIGR01241 155 EIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEIL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   379 KVHLGNLKtsLDKNELSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQAIERVIAGMEKKTNVLAPEEKR 458
Cdd:TIGR01241 235 KVHAKNKK--LAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   459 TVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLP-KDHYLLSKEQLFDRMCMTLGGRVAEELFFNRITTGAQD 537
Cdd:TIGR01241 313 LVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   538 DLKKITDIAYSQVVRFGMNEKVGQVSFdvGQAGDPVF-------SKPYSEDTAQLIDNEVRSIIKCAHEATTSLLTKHKE 610
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAY--GSDGGDVFlgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRD 470
                         490       500
                  ....*....|....*....|....*
gi 24665814   611 NVQKVAERLLQNEVLSRDDMIELLG 635
Cdd:TIGR01241 471 ELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
145-646 5.99e-175

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 514.21  E-value: 5.99e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  145 LLPTLLIIGfLVYMMRKSADMMGGGRGRKGGglfggVMQSTAKLTNPNEIGVGFKDVAGCEEAKIEIMEFVNFLKNPQQY 224
Cdd:CHL00176 135 LLPLILIGV-LWFFFQRSSNFKGGPGQNLMN-----FGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERF 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  225 IDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFIDEIDAVG 304
Cdd:CHL00176 209 TAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVG 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  305 RKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASIFKVHLGN 384
Cdd:CHL00176 289 RQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  385 LKTSLDkneLSRK-MAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQAIERVIAGMEkKTNVLAPEEKRTVAHH 463
Cdd:CHL00176 369 KKLSPD---VSLElIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYH 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  464 EAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLP-KDHYLLSKEQLFDRMCMTLGGRVAEELFFN--RITTGAQDDLK 540
Cdd:CHL00176 445 EVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQ 524
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  541 KITDIAYSQVVRFGMNeKVGQVSFDVGQAGDPVF------SKPYSEDTAQLIDNEVRSIIKCAHEATTSLLTKHKENVQK 614
Cdd:CHL00176 525 QVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDL 603
                        490       500       510
                 ....*....|....*....|....*....|...
gi 24665814  615 VAERLLQNEVLSRDDMIELLGPR-PFKEKSTYE 646
Cdd:CHL00176 604 LVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
196-366 1.08e-117

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: 349.61  E-value: 1.08e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 196 VGFKDVAGCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 275
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 276 GPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALM 355
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                       170
                ....*....|.
gi 24665814 356 RPGRFDRQIYV 366
Cdd:cd19501 161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
451-633 8.83e-87

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 270.24  E-value: 8.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   451 VLAPEEKRTVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLP-KDHYLLSKEQLFDRMCMTLGGRVAEELFFN 529
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPeEDKLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   530 RITTGAQDDLKKITDIAYSQVVRFGMNEKVGQVSFDVGQA-----GDPVFSKPYSEDTAQLIDNEVRSIIKCAHEATTSL 604
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGnvflgRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKEI 161
                         170       180
                  ....*....|....*....|....*....
gi 24665814   605 LTKHKENVQKVAERLLQNEVLSRDDMIEL 633
Cdd:pfam01434 162 LTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
232-370 8.86e-21

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: 89.35  E-value: 8.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814    232 PKGAMLTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPSRVRDMFAMARKHAPCI 294
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24665814    295 LFIDEIDAVGRKRggktfgghSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPgRFDRQIYVPAPD 370
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
39-636 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 800.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  39 AIGAVVLVGSFAFFEMGYKEISWKEFVNsYLSKGVVEKLEVVNKKwVRVRLqqnSNSGSGVLWFNIGSVDSFERNLEAAQ 118
Cdd:COG0465   2 ALLLVLLFNLFSSSSSSVKEISYSEFLQ-LVEAGKVKSVTIQGDR-ITGTL---KDGTKTRFTTYRVNDPELVDLLEEKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 119 teqgtesinfVPVIYRNEVEAASLTGLL----PTLLIIGFLVYMMRKSADMMGGgrgrkggglfggVMQ---STAKLTNP 191
Cdd:COG0465  77 ----------VEVTAKPPEESSWLLSLLisllPILLLIGLWIFFMRRMQGGGGG------------AMSfgkSKAKLYDE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 192 NEIGVGFKDVAGCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM 271
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 272 FVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILD 351
Cdd:COG0465 215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 352 KALMRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKtsLDKN-ELsRKMAALTPGFTGADIANVCNEAALIAARDSKDSIV 430
Cdd:COG0465 295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDvDL-EVIARRTPGFSGADLANLVNEAALLAARRNKKAVT 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 431 LKHFEQAIERVIAGMEKKTNVLAPEEKRTVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLPK-DHYLLSKEQ 509
Cdd:COG0465 372 MEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEeDRYLYTKEE 451
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 510 LFDRMCMTLGGRVAEELFFNRITTGAQDDLKKITDIAYSQVVRFGMNEKVGQVSFdvGQAGDPVF-------SKPYSEDT 582
Cdd:COG0465 452 LLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY--GESEGEVFlgrdigqSRNYSEET 529
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....
gi 24665814 583 AQLIDNEVRSIIKCAHEATTSLLTKHKENVQKVAERLLQNEVLSRDDMIELLGP 636
Cdd:COG0465 530 AREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
142-635 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: 701.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   142 LTGLLPTLLIIGFLVYMMRKSADMMGGGrgrkggglfggVM---QSTAKLTNPNEIGVGFKDVAGCEEAKIEIMEFVNFL 218
Cdd:TIGR01241   6 LFSLLPPILLLVGVWFFFRRQMQGGGGR-----------AFsfgKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   219 KNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFID 298
Cdd:TIGR01241  75 KNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFID 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   299 EIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASIF 378
Cdd:TIGR01241 155 EIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEIL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   379 KVHLGNLKtsLDKNELSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQAIERVIAGMEKKTNVLAPEEKR 458
Cdd:TIGR01241 235 KVHAKNKK--LAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   459 TVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLP-KDHYLLSKEQLFDRMCMTLGGRVAEELFFNRITTGAQD 537
Cdd:TIGR01241 313 LVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   538 DLKKITDIAYSQVVRFGMNEKVGQVSFdvGQAGDPVF-------SKPYSEDTAQLIDNEVRSIIKCAHEATTSLLTKHKE 610
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAY--GSDGGDVFlgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRD 470
                         490       500
                  ....*....|....*....|....*
gi 24665814   611 NVQKVAERLLQNEVLSRDDMIELLG 635
Cdd:TIGR01241 471 ELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
145-646 5.99e-175

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 514.21  E-value: 5.99e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  145 LLPTLLIIGfLVYMMRKSADMMGGGRGRKGGglfggVMQSTAKLTNPNEIGVGFKDVAGCEEAKIEIMEFVNFLKNPQQY 224
Cdd:CHL00176 135 LLPLILIGV-LWFFFQRSSNFKGGPGQNLMN-----FGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERF 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  225 IDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFIDEIDAVG 304
Cdd:CHL00176 209 TAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVG 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  305 RKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASIFKVHLGN 384
Cdd:CHL00176 289 RQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  385 LKTSLDkneLSRK-MAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQAIERVIAGMEkKTNVLAPEEKRTVAHH 463
Cdd:CHL00176 369 KKLSPD---VSLElIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYH 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  464 EAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLP-KDHYLLSKEQLFDRMCMTLGGRVAEELFFN--RITTGAQDDLK 540
Cdd:CHL00176 445 EVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQ 524
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  541 KITDIAYSQVVRFGMNeKVGQVSFDVGQAGDPVF------SKPYSEDTAQLIDNEVRSIIKCAHEATTSLLTKHKENVQK 614
Cdd:CHL00176 525 QVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDL 603
                        490       500       510
                 ....*....|....*....|....*....|...
gi 24665814  615 VAERLLQNEVLSRDDMIELLGPR-PFKEKSTYE 646
Cdd:CHL00176 604 LVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
146-686 6.86e-151

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 452.57  E-value: 6.86e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  146 LPTLLIIGFLVYMMRKsadmmgggRGRKGGGLFGGVMQSTAKLTNPNEIGVGFKDVAGCEEAKIEIMEFVNFLKNPQQYI 225
Cdd:PRK10733 107 FPMLLLIGVWIFFMRQ--------MQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQ 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  226 DLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGR 305
Cdd:PRK10733 179 KLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGR 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  306 KRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASIFKVHLGN- 384
Cdd:PRK10733 259 QRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRv 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  385 -LKTSLDKNELSRKmaalTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQAIERVIAGMEKKTNVLAPEEKRTVAHH 463
Cdd:PRK10733 339 pLAPDIDAAIIARG----TPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYH 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  464 EAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLPK-DHYLLSKEQLFDRMCMTLGGRVAEELFF--NRITTGAQDDLK 540
Cdd:PRK10733 415 EAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEgDAISASRQKLESQISTLYGGRLAEEIIYgpEHVSTGASNDIK 494
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  541 KITDIAYSQVVRFGMNEKVGQVSFdvGQAGDPVF-------SKPYSEDTAQLIDNEVRSIIKCAHEATTSLLTKHKENVQ 613
Cdd:PRK10733 495 VATNLARNMVTQWGFSEKLGPLLY--AEEEGEVFlgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILH 572
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24665814  614 KVAERLLQNEVLSRDDMIELLGPRPFKEKSTYEEfVEGTGSFEEDTTlPEGlkswnkekerTEPLDAGSTPSS 686
Cdd:PRK10733 573 AMKDALMKYETIDAPQIDDLMARRDVRPPAGWEE-PGASNNSDDNGT-PKA----------PRPVDEPRTPNP 633
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
196-366 1.08e-117

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: 349.61  E-value: 1.08e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 196 VGFKDVAGCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 275
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 276 GPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALM 355
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                       170
                ....*....|.
gi 24665814 356 RPGRFDRQIYV 366
Cdd:cd19501 161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
195-450 1.08e-112

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 342.76  E-value: 1.08e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 195 GVGFKDVAGCEEAKIEIMEFV-NFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 273
Cdd:COG1222  74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 274 GVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKtfGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKA 353
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD--GTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 354 LMRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKtsLDKNELSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKH 433
Cdd:COG1222 232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMP--LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMED 309
                       250
                ....*....|....*..
gi 24665814 434 FEQAIERVIAGMEKKTN 450
Cdd:COG1222 310 LEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
195-448 2.50e-95

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 299.83  E-value: 2.50e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  195 GVGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 273
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  274 GVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKA 353
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  354 LMRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKTSLDKNelSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKH 433
Cdd:PRK03992 287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD--LEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMED 364
                        250
                 ....*....|....*
gi 24665814  434 FEQAIERVIAGMEKK 448
Cdd:PRK03992 365 FLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
451-633 8.83e-87

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 270.24  E-value: 8.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   451 VLAPEEKRTVAHHEAGHAVAGWFLEHADPLLKVSIIPRGKGLGYAQYLP-KDHYLLSKEQLFDRMCMTLGGRVAEELFFN 529
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPeEDKLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   530 RITTGAQDDLKKITDIAYSQVVRFGMNEKVGQVSFDVGQA-----GDPVFSKPYSEDTAQLIDNEVRSIIKCAHEATTSL 604
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGnvflgRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKEI 161
                         170       180
                  ....*....|....*....|....*....
gi 24665814   605 LTKHKENVQKVAERLLQNEVLSRDDMIEL 633
Cdd:pfam01434 162 LTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
198-441 1.62e-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: 259.07  E-value: 1.62e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 198 FKDVAGCEEAKIEIMEFVN-FLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 276
Cdd:COG0464 156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 277 PSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTfGGHSEQEntLNQLLVEMDGFntTTNVVVLAATNRVDILDKALMR 356
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG-DGVGRRV--VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 357 pgRFDRQIYVPAPDIKGRASIFKVHLGNLKtsLDKNELSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQ 436
Cdd:COG0464 311 --RFDEIIFFPLPDAEERLEIFRIHLRKRP--LDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLE 386

                ....*
gi 24665814 437 AIERV 441
Cdd:COG0464 387 ALERE 391
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
196-442 2.11e-79

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: 257.42  E-value: 2.11e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   196 VGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 274
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   275 VGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKAL 354
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   355 MRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKTSLDKNelSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHF 434
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVD--LEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDF 356

                  ....*...
gi 24665814   435 EQAIERVI 442
Cdd:TIGR01242 357 IKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
196-447 6.67e-69

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: 239.42  E-value: 6.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   196 VGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 274
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   275 VGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTfgGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKAL 354
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPAL 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   355 MRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKTSLDKNelSRKMAALTPGFTGADIANVCNEAALIAARDSKDS------ 428
Cdd:TIGR01243 608 LRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVD--LEELAEMTEGYTGADIEAVCREAAMAALRESIGSpakekl 685
                         250       260       270
                  ....*....|....*....|....*....|.
gi 24665814   429 ------------IVLKHFEQAIERVIAGMEK 447
Cdd:TIGR01243 686 evgeeeflkdlkVEMRHFLEALKKVKPSVSK 716
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
198-366 3.52e-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: 220.67  E-value: 3.52e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 198 FKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 276
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 277 PSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMR 356
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161
                       170
                ....*....|
gi 24665814 357 PGRFDRQIYV 366
Cdd:cd19502 162 PGRFDRKIEF 171
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
198-451 2.19e-65

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 222.72  E-value: 2.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  198 FKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 276
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  277 PSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMR 356
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  357 PGRFDRQIYVPAPDIKGRASIFKVHLGNLKTSLD---------KNELSrkmaaltpgftGADIANVCNEAALIAARDSKD 427
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDvdleefimaKDELS-----------GADIKAICTEAGLLALRERRM 410
                        250       260
                 ....*....|....*....|....
gi 24665814  428 SIVLKHFEQAIERVIagMEKKTNV 451
Cdd:PTZ00361 411 KVTQADFRKAKEKVL--YRKKGNI 432
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
181-442 3.20e-63

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 215.78  E-value: 3.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  181 VMQSTAKltnPNeigVGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVP 259
Cdd:PTZ00454 133 LLQMSEK---PD---VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTAT 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  260 FITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVV 339
Cdd:PTZ00454 207 FIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVK 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  340 VLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASIFKVHLG--NLKTSLDKNELsrkmAALTPGFTGADIANVCNEA 417
Cdd:PTZ00454 287 VIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSkmNLSEEVDLEDF----VSRPEKISAADIAAICQEA 362
                        250       260
                 ....*....|....*....|....*
gi 24665814  418 ALIAARDSKDSIVLKHFEQAIERVI 442
Cdd:PTZ00454 363 GMQAVRKNRYVILPKDFEKGYKTVV 387
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
207-366 1.22e-60

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: 200.20  E-value: 1.22e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 207 AKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAM 286
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 287 ARKHAPCILFIDEIDAVGRKRGGKtfGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYV 366
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDSS--GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
198-440 1.68e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 203.19  E-value: 1.68e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 198 FKDVAGCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 277
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 278 SRVRDMFAMARKhAPCILFIDEIDAVGRKRGGKTfgGHSEQENTLNQLLVEMDGFNttTNVVVLAATNRVDILDKALMRp 357
Cdd:COG1223  81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQN--DVGEVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 358 gRFDRQIYVPAPDIKGRASIFKVHLGNLKTSLDKNelSRKMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQA 437
Cdd:COG1223 155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELD--LKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231

                ...
gi 24665814 438 IER 440
Cdd:COG1223 232 LKQ 234
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
207-366 6.62e-58

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: 192.88  E-value: 6.62e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 207 AKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFA 285
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 286 MARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQenTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIY 365
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                .
gi 24665814 366 V 366
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 ...
200-366 3.75e-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: 188.65  E-value: 3.75e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPS 278
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 279 RVRDMFAMARKHAPCILFIDEIDAVGRKRGgktfGGHSEQENTL-NQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRP 357
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKRE----EDQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 24665814 358 GRFDRQIYV 366
Cdd:cd19503 157 GRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
196-423 1.35e-55

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: 202.44  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   196 VGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 274
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   275 VGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTfgGHSEQEnTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKAL 354
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVEKR-VVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665814   355 MRPGRFDRQIYVPAPDIKGRASIFKVHLGNLKTSLDKneLSRKMAALTPGFTGADIANVCNEAALIAAR 423
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDV--DLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
208-366 1.66e-53

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 181.17  E-value: 1.66e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 208 KIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAM 286
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 287 ARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYV 366
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
236-367 2.03e-53

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: 179.71  E-value: 2.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   236 MLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGktfGGH 315
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24665814   316 SEQENTLNQLLVEMDGF-NTTTNVVVLAATNRVDILDKALMrpGRFDRQIYVP 367
Cdd:pfam00004  79 SESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
207-366 1.21e-52

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: 178.84  E-value: 1.21e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 207 AKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFA 285
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 286 MARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQenTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIY 365
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                .
gi 24665814 366 V 366
Cdd:cd19529 159 I 159
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
212-366 5.27e-47

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: 163.43  E-value: 5.27e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 212 MEFVNFLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHA 291
Cdd:cd19530  10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24665814 292 PCILFIDEIDAVGRKRGGktfGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYV 366
Cdd:cd19530  90 PCVIFFDEVDALVPKRGD---GGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
200-367 6.20e-47

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: 163.76  E-value: 6.20e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPS 278
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 279 RVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTfgGHSEQEnTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPG 358
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 24665814 359 RFDRQIYVP 367
Cdd:cd19519 158 RFDREIDIG 166
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
219-365 5.95e-42

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: 149.50  E-value: 5.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 219 KNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFID 298
Cdd:cd19526  14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24665814 299 EIDAVGRKRGGKTFGghsEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIY 365
Cdd:cd19526  94 EFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
200-364 3.78e-41

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: 147.55  E-value: 3.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNFLK-NPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPS 278
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 279 RVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTfgghSEQENTL-NQLLVEMDGFN----TTTNVVVLAATNRVDILDKA 353
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQ----REMERRIvSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                       170
                ....*....|.
gi 24665814 354 LMRPGRFDRQI 364
Cdd:cd19518 157 LRRAGRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
208-366 3.39e-39

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: 141.88  E-value: 3.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 208 KIEIMEFVNF-LKNPQQYIDlGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAM 286
Cdd:cd19527   2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 287 ARKHAPCILFIDEIDAVGRKRGGKTFGGhSEQENTLNQLLVEMDGFNTTT-NVVVLAATNRVDILDKALMRPGRFDRQIY 365
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSGDSG-GVMDRVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                .
gi 24665814 366 V 366
Cdd:cd19527 160 L 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
201-366 3.50e-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: 136.33  E-value: 3.50e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 201 VAGCEEAKIEIMEFVNF-LKNPQQYiDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSR 279
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 280 VRDMFAMARKHAPCILFIDEIDAVGRKRGGktfGGHSEQENTLNQLLVEMDGFNTTTN--VVVLAATNRVDILDKALMRp 357
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155

                ....*....
gi 24665814 358 gRFDRQIYV 366
Cdd:cd19509 156 -RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
191-366 2.15e-33

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 126.13  E-value: 2.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 191 PNeigVGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIdlGAKIP-KGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEF 268
Cdd:cd19521   2 PN---VKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 269 LEMFVGVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGgktfGGHSEQENTL-NQLLVEMDGF-NTTTNVVVLAATNR 346
Cdd:cd19521  77 VSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRG----EGESEASRRIkTELLVQMNGVgNDSQGVLVLGATNI 152
                       170       180
                ....*....|....*....|
gi 24665814 347 VDILDKALMRpgRFDRQIYV 366
Cdd:cd19521 153 PWQLDSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
200-365 3.59e-32

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: 122.62  E-value: 3.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN-----VPFITVSGSEFLEMFV 273
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 274 GVGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGKTFGGHSEQENTLnqlLVEMDGFNTTTNVVVLAATNRVDILDKA 353
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTL---LALMDGLDNRGQVVVIGATNRPDALDPA 157
                       170
                ....*....|..
gi 24665814 354 LMRPGRFDRQIY 365
Cdd:cd19517 158 LRRPGRFDREFY 169
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
196-366 4.30e-32

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: 122.79  E-value: 4.30e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 196 VGFKDVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKiPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 274
Cdd:cd19525  19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 275 VGPSRVRDMFAMARKHAPCILFIDEIDAVGRKRGGktfGGHSEQENTLNQLLVEMDGFNTTTN--VVVLAATNRVDILDK 352
Cdd:cd19525  98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 174
                       170
                ....*....|....
gi 24665814 353 ALMRpgRFDRQIYV 366
Cdd:cd19525 175 AARR--RLVKRLYI 186
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
200-360 1.63e-31

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 120.61  E-value: 1.63e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNF-LKNPQQYIDLG-AKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 277
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 278 SRVRDMFAMARKHAPCILFIDEIDAVGRKRggkTFGGHSEQENTLNQLLVEMDGFNTTTN--VVVLAATNRVDILDKALM 355
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR---SSTDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAIL 157

                ....*..
gi 24665814 356 R--PGRF 360
Cdd:cd19520 158 RrmPKRF 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
200-366 2.96e-30

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: 117.01  E-value: 2.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNFLKNPQQYIDlGAKIP-KGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPS 278
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK-GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 279 RVRDMFAMARKHAPCILFIDEIDAVGRKRGGKtfGGHSEQENTLNQLLVEMDGF-NTTTN------VVVLAATNRVDILD 351
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTS--EEHEASRRVKSELLVQMDGVgGASENddpskmVMVLAATNFPWDID 157
                       170
                ....*....|....*
gi 24665814 352 KALMRpgRFDRQIYV 366
Cdd:cd19522 158 EALRR--RLEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
200-366 2.44e-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: 114.18  E-value: 2.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNF-LKNPQQYIDLGAKiPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPS 278
Cdd:cd19524   1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 279 RVRDMFAMARKHAPCILFIDEIDAVGRKRGGktfGGHSEQENTLNQLLVEMDGFNTTTN--VVVLAATNRVDILDKALMR 356
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                       170
                ....*....|
gi 24665814 357 pgRFDRQIYV 366
Cdd:cd19524 157 --RFTKRVYV 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
227-366 4.62e-28

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: 111.04  E-value: 4.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 227 LGAKIPKGAMLTGPPGTGKTLLAKATAGEANV--PFItVSGSEFLEMFVGVGPSRVRDMFAMARKHAPC--------ILF 296
Cdd:cd19504  30 LGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIII 108
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 297 IDEIDAVGRKRGGKTfGGHSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYV 366
Cdd:cd19504 109 FDEIDAICKQRGSMA-GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
232-367 1.57e-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: 108.77  E-value: 1.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 232 PKGAMLTGPPGTGKTLLAKATAGEA---NVPFITVSGSEFLEMFVG---VGPSRVRDMFAMARKHAPCILFIDEIDAVGR 305
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24665814 306 KrggktfgghsEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVP 367
Cdd:cd00009  99 G----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
222-421 2.51e-26

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 113.19  E-value: 2.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  222 QQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPSRVRDMFAMARKHAPCILFIDEID 301
Cdd:CHL00195 249 KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEID 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  302 avgrkrggKTFGG-HSEQEN-TLNQLLVEMDGF--NTTTNVVVLAATNRVDILDKALMRPGRFDRQIYVPAPDIKGRASI 377
Cdd:CHL00195 329 --------KAFSNsESKGDSgTTNRVLATFITWlsEKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKI 400
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24665814  378 FKVHLGNLKTSLDKNELSRKMAALTPGFTGADIANVCNEAALIA 421
Cdd:CHL00195 401 FKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
200-366 1.02e-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: 95.13  E-value: 1.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKiEIMEFVN--FLKNPQQYidlGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 277
Cdd:cd19507   1 DVGGLDNLK-DWLKKRKaaFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 278 SRVRDMFAMARKHAPCILFIDEIDavgrkrggKTFGG---HSEQENT---LNQLLVEMDgfNTTTNVVVLAATNRVDILD 351
Cdd:cd19507  77 SRLRQMIQTAEAIAPCVLWIDEIE--------KGFSNadsKGDSGTSsrvLGTFLTWLQ--EKKKPVFVVATANNVQSLP 146
                       170
                ....*....|....*
gi 24665814 352 KALMRPGRFDRQIYV 366
Cdd:cd19507 147 PELLRKGRFDEIFFV 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
232-370 8.86e-21

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: 89.35  E-value: 8.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814    232 PKGAMLTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPSRVRDMFAMARKHAPCI 294
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24665814    295 LFIDEIDAVGRKRggktfgghSEQENTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPgRFDRQIYVPAPD 370
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
217-366 1.63e-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: 85.87  E-value: 1.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 217 FLKNPQQYIDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEflemfVGVGPSRVRDMFAMARKHApcILF 296
Cdd:cd19510   8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24665814 297 IDEIDA--VGRKRGGKT---FGGHSEQenTLNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYV 366
Cdd:cd19510  81 LEDIDAafESREHNKKNpsaYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
200-366 4.28e-16

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: 76.46  E-value: 4.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 200 DVAGCEEAKIEIMEFVNF-LKNPQQYIDLgAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPS 278
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 279 RVRDMFAMARKHAPCILFIDEIDAVGRKRggktFGGHSEQENTLNQLLVEMDGFNTTT--NVVVLAATNRVDILDKALMR 356
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQ----DDEASPVGRLQVELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
                       170
                ....*....|
gi 24665814 357 pgRFDRQIYV 366
Cdd:cd19523 156 --YFSKRLLV 163
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
227-366 6.20e-12

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: 64.32  E-value: 6.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 227 LGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFL--------------EMFVGVGPSRVRDMFAMARKHAP 292
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665814 293 CILFIDEIDAVGRKRggktFGGHSEQENT-----LNQLLVEMDGFNTTTNVVVLAATNRVDILDKALMRPGRFDRQIYV 366
Cdd:cd19505  87 CIIWIPNIHELNVNR----STQNLEEDPKlllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
397-436 3.65e-11

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: 58.32  E-value: 3.65e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 24665814   397 KMAALTPGFTGADIANVCNEAALIAARDSKDSIVLKHFEQ 436
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
34-130 2.14e-10

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: 58.00  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814    34 WILLGAIGAVVLVGSFAFFEMGYKEISWKEFVNsYLSKGVVEKLEVVNKKWVRVRLQQNSNSGSG----VLWFNIGSVDS 109
Cdd:pfam06480   4 WLLILLVLLLLFLLFLLSSSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGSkfttYFIPSLPNVDS 82
                          90       100
                  ....*....|....*....|.
gi 24665814   110 FERNLEAAQTEQGTESINFVP 130
Cdd:pfam06480  83 LLEKLEDALEEKGVKVSVKPP 103
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
231-310 3.46e-10

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: 59.70  E-value: 3.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 231 IPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVGvgpsrvRDMFAMARKHAPCILFIDEIDAVGRKRGG 309
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGS 118

                .
gi 24665814 310 K 310
Cdd:cd19498 119 S 119
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
239-300 7.83e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.53  E-value: 7.83e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24665814 239 GPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpSRVRDMFAMARKHA----PCILFIDEI 300
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
237-300 9.62e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.17  E-value: 9.62e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24665814  237 LTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpSRVRDMFAMARKHA----PCILFIDEI 300
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
236-354 5.57e-08

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: 52.53  E-value: 5.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 236 MLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMfvGV-GPSRVRDMFAMARK-HAPCILFIDEIDAVGRKRGgkTFG 313
Cdd:cd19512  26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRS--TEK 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24665814 314 GHSEQENTLNQLLVEMdGFNTTTNVVVLaATNRVDILDKAL 354
Cdd:cd19512 102 ISEDLRAALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI 140
PRK04195 PRK04195
replication factor C large subunit; Provisional
198-301 5.94e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 55.70  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  198 FKDVAGCEEAKIEIMEFV-NFLKNpqqyidlgaKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEF-----LEM 271
Cdd:PRK04195  13 LSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 24665814  272 FVGVGpSRVRDMFAMARKhapcILFIDEID 301
Cdd:PRK04195  84 VAGEA-ATSGSLFGARRK----LILLDEVD 108
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
236-301 3.24e-07

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: 50.66  E-value: 3.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665814   236 MLTGPPGTGKTLLAKATAGEANV---PFITVSGSEFLE-----MFVGVGPSRVR-----DMFAMARKHAPCILFIDEID 301
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
236-360 5.39e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.21  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   236 MLTGPPGTGKTLLAKATAgEA--NVPFITVSGSEFLE-------MFVGVGPSRVRD---MFAMARKHapcILFIDEIDAv 303
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgplVRAAREGE---IAVLDEINR- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   304 grkrggktfgGHSEQENTLNQLLVE-----MDGFNTT----TNVVVLAATNRVDI----LDKALMRpgRF 360
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDErrlllPDGGELVkaapDGFRLIATMNPLDRglneLSPALRS--RF 135
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
204-300 1.55e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 51.31  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 204 CEEAKIEIMEFVNFLKNPQQYIdlgakipkgamLTGPPGTGKT----LLAKATAGEA--NVPFITV----SGSEFLEMFV 273
Cdd:COG1401 204 REKFEETLEAFLAALKTKKNVI-----------LAGPPGTGKTylarRLAEALGGEDngRIEFVQFhpswSYEDFLLGYR 272
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 24665814 274 GVGPS---RVRD-MF------AMARKHAPCILFIDEI 300
Cdd:COG1401 273 PSLDEgkyEPTPgIFlrfclkAEKNPDKPYVLIIDEI 309
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
199-309 1.15e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 46.40  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 199 KDVAGCEEAKIEIMEF--VNFLKNpqqyiDLGAKIpkgAMLTGPPGTGKTLLAKATAGEANVPFITVS-G--SEFLEM-- 271
Cdd:cd19500  10 ADHYGLEDVKERILEYlaVRKLKG-----SMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrg 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24665814 272 ----FVGVGPSRVRDMFAMARKHAPCILfIDEIDAVGRKRGG 309
Cdd:cd19500  82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGSSFRG 122
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
236-351 1.42e-05

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: 44.80  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 236 MLTGPPGTGKTLLAKATAGEA---NVPFITVSgseFLEMFVgvgpSRVRDmfaMARKHAPCILFIDEIDAVGRKRGGktf 312
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARASQG--- 68
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24665814 313 gghSEQENTLNQLLVEMDGFNtTTNVVVLAATNRVDILD 351
Cdd:cd01120  69 ---DRSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
233-268 1.44e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.04  E-value: 1.44e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24665814 233 KGAMLTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF 268
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
232-441 1.88e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.54  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 232 PKGAMLTGPPGTGKTLLAKA-------TAGEANVPFITV------SGSEF------LEMFV--------GVGPSRVRDMF 284
Cdd:COG1474  51 PSNVLIYGPTGTGKTAVAKYvleeleeEAEERGVDVRVVyvncrqASTRYrvlsriLEELGsgedipstGLSTDELFDRL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 285 --AMARKHAPCILFIDEIDAVGRKRGgktfgghseqENTLNQLLvEMDGFNTTTNVVVLAATNRVDILDkalmrpgRFDr 362
Cdd:COG1474 131 yeALDERDGVLVVVLDEIDYLVDDEG----------DDLLYQLL-RANEELEGARVGVIGISNDLEFLE-------NLD- 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 363 qiyvpaPDIKGRASIFKVHLgnlkTSLDKNEL-----SRKMAALTPGFTGADIANVCNE------------------AAL 419
Cdd:COG1474 192 ------PRVKSSLGEEEIVF----PPYDADELrdileDRAELAFYDGVLSDEVIPLIAAlaaqehgdarkaidllrvAGE 261
                       250       260
                ....*....|....*....|..
gi 24665814 420 IAARDSKDSIVLKHFEQAIERV 441
Cdd:COG1474 262 IAEREGSDRVTEEHVREAREKI 283
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
236-301 4.11e-05

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: 44.86  E-value: 4.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 236 MLTGPPGTGKTLLAKATA-----GEANvpFITVSGSEFLEMF-----VGVGPSRV----RDMFAMA-RKHAPCILFIDEI 300
Cdd:cd19499  45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122

                .
gi 24665814 301 D 301
Cdd:cd19499 123 E 123
AAA_22 pfam13401
AAA domain;
236-306 4.43e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 43.48  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   236 MLTGPPGTGKTLLAK---ATAGEANVPFITV------SGSEFLEMFV------GVGPSRVRDMFAM-----ARKHAPCIL 295
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAAlqqllLALAVAVVL 88
                          90
                  ....*....|.
gi 24665814   296 FIDEIDAVGRK 306
Cdd:pfam13401  89 IIDEAQHLSLE 99
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
233-271 9.48e-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: 44.99  E-value: 9.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 24665814   233 KGAMLTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF--LEM 271
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVysLEM 93
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
203-368 1.58e-04

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: 44.84  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   203 GCEEAKIEIMEFVNFLKNPQQYIDLGAKIPKGA---MLTGPPGTGKTLLAKATA------GEANVPFIT-VSGSEFLEMF 272
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAkiycglGVLRKPLVReVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   273 VGVGPSRVRDMF--AMARkhapcILFIDEIDAVGRKRGGKT--FGGHSeqentLNQLLVEMDgfNTTTNVVVLAATNRVD 348
Cdd:TIGR03922 360 IGESEAKTNEIIdsALGG-----VLFLDEAYTLVETGYGQKdpFGLEA-----IDTLLARME--NDRDRLVVIGAGYRKD 427
                         170       180
                  ....*....|....*....|....*...
gi 24665814   349 IlDKAL-MRPG---RFDRQI----YVPA 368
Cdd:TIGR03922 428 L-DKFLeVNEGlrsRFTRVIefpsYSPD 454
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
236-300 1.74e-04

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: 42.49  E-value: 1.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24665814   236 MLTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGP--SRVRDMFAMARKHAPC-ILFIDEI 300
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITS-----------GPaiERPGDLAAILTNLEPGdVLFIDEI 93
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
230-302 1.78e-04

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: 42.62  E-value: 1.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 230 KIPKGAM--LTGPPGTGKTLLAKATAGEANVP--FITVSGSEFLEMFVGVGPSRV----------RDMFAMARK--HAPC 293
Cdd:cd00267  21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                ....*....
gi 24665814 294 ILFIDEIDA 302
Cdd:cd00267 101 LLLLDEPTS 109
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
237-300 3.02e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.58  E-value: 3.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  237 LTGPPGTGKTLLAKATAGEANVPFITVSG------SEFLEMFVGVGPsrvRDmfamarkhapcILFIDEI 300
Cdd:PRK00080  56 LYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI 111
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
228-305 1.02e-03

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: 41.90  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814   228 GAKIPKGA----MLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEmfvgvgPSRVRDMFAMARKHApcILFIDEIDAV 303
Cdd:TIGR00635  22 AAKMRQEAldhlLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK------PGDLAAILTNLEEGD--VLFIDEIHRL 93

                  ..
gi 24665814   304 GR 305
Cdd:TIGR00635  94 SP 95
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
218-306 1.71e-03

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: 40.66  E-value: 1.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 218 LKNPQQYIDLGAKIPKGAM-LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVG--VGPSRVR----DMFAMARK 289
Cdd:cd19497  35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKllqaADYDVERA 114
                        90
                ....*....|....*..
gi 24665814 290 HAPcILFIDEIDAVGRK 306
Cdd:cd19497 115 QRG-IVYIDEIDKIARK 130
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
236-306 2.71e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 40.53  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  236 MLTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVGvgpsrvRDMFAMARK--HApC----------ILFIDEIDA 302
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVG------EDVENILLKllQA-AdydvekaqrgIVYIDEIDK 184

                 ....
gi 24665814  303 VGRK 306
Cdd:PRK05342 185 IARK 188
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
237-301 3.70e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 39.77  E-value: 3.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24665814 237 LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEmfvgvgPSRV--RDMFAMAR-----KHAP---CILFIDEID 301
Cdd:COG0714  36 LEGVPGVGKTTLAKALARALGLPFIRIQFTPDLL------PSDIlgTYIYDQQTgefefRPGPlfaNVLLADEIN 104
44 PHA02544
clamp loader, small subunit; Provisional
222-304 5.25e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.59  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814  222 QQYIDLGaKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVSGSEflemfVGVGPSRVR-DMFA--MARKHAPCILFID 298
Cdd:PHA02544  34 KSIVKKG-RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD-----CRIDFVRNRlTRFAstVSLTGGGKVIIID 107

                 ....*.
gi 24665814  299 EIDAVG 304
Cdd:PHA02544 108 EFDRLG 113
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
210-301 5.48e-03

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 39.16  E-value: 5.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665814 210 EIMEFVNFLknpQQYIDLGakipkgaMLTGPPGTGKTLLAKATAGE-ANVPFITVSGS----EFL-----EMFVGVGPSR 279
Cdd:COG2842  38 RFAEALDEA---RALPGIG-------VVYGESGVGKTTAAREYANRnPNVIYVTASPSwtskELLeelaeELGIPAPPGT 107
                        90       100
                ....*....|....*....|....*
gi 24665814 280 VRDMFAMARKH-APCI--LFIDEID 301
Cdd:COG2842 108 IADLRDRILERlAGTGrlLIIDEAD 132
 
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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