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Conserved domains on  [gi|685370626|ref|XP_009119063|]
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ATP-dependent zinc metalloprotease FTSH 8, chloroplastic [Brassica rapa]

Protein Classification

ATP-dependent zinc metalloprotease FtsH family protein( domain architecture ID 11414130)

ATP-dependent zinc metalloprotease FtsH family protein similar to Arabidopsis thaliana FTSH 8, part of a complex that functions as an ATP-dependent zinc metallopeptidase, and which is involved in the thylakoid formation and in the removal of damaged D1 in the photosystem II, preventing cell death under high-intensity light conditions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ftsH CHL00176
cell division protein; Validated
85-676 0e+00

cell division protein; Validated


:

Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 910.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  85 QGVSSSRMSYSRFLEYLDKGRVDKVDLYENGTIAIVEAVSPELGNRIQRVRVQLPGLSQELLQKLRAKNIDFAAHTTQED 164
Cdd:CHL00176  45 QNKASSRMTYGRFLEYLDMGWIKKVDLYDNGRTAIVEASSPELGNRPQRIRVELPVGASELIQKLKEANIDFDAHPPVLK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 165 qgSPLLNLIGNLAFPLILIGGLFLLSRRSSGGMGGPGGPGfpLQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVE 244
Cdd:CHL00176 125 --SNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQNL--MNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVS 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 245 FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVF 324
Cdd:CHL00176 201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVF 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 325 VDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTE 404
Cdd:CHL00176 281 IDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLD 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 405 ILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSIDRIVAGMEGTVMTDGKSKSL 484
Cdd:CHL00176 361 ILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKRL 440
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 485 VAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIFGEPEVTTGAV 564
Cdd:CHL00176 441 IAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEVTTGAS 520
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 565 GDLQQITGLAKQMVTTFGMSEIGPWSLMDSSAQSDVIMRMMARNS-MSEKLANDIDSAVKTLSDRAYEIALGHIRNNREA 643
Cdd:CHL00176 521 NDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRFMQRNSeYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVL 600
                        570       580       590
                 ....*....|....*....|....*....|...
gi 685370626 644 MDKIVEVLLEKETMSGDEFRAILSEFTEIPPEN 676
Cdd:CHL00176 601 IDLLVELLLQKETIDGDEFREIVNSYTILPPKK 633
 
Name Accession Description Interval E-value
ftsH CHL00176
cell division protein; Validated
85-676 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 910.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  85 QGVSSSRMSYSRFLEYLDKGRVDKVDLYENGTIAIVEAVSPELGNRIQRVRVQLPGLSQELLQKLRAKNIDFAAHTTQED 164
Cdd:CHL00176  45 QNKASSRMTYGRFLEYLDMGWIKKVDLYDNGRTAIVEASSPELGNRPQRIRVELPVGASELIQKLKEANIDFDAHPPVLK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 165 qgSPLLNLIGNLAFPLILIGGLFLLSRRSSGGMGGPGGPGfpLQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVE 244
Cdd:CHL00176 125 --SNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQNL--MNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVS 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 245 FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVF 324
Cdd:CHL00176 201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVF 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 325 VDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTE 404
Cdd:CHL00176 281 IDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLD 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 405 ILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSIDRIVAGMEGTVMTDGKSKSL 484
Cdd:CHL00176 361 ILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKRL 440
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 485 VAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIFGEPEVTTGAV 564
Cdd:CHL00176 441 IAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEVTTGAS 520
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 565 GDLQQITGLAKQMVTTFGMSEIGPWSLMDSSAQSDVIMRMMARNS-MSEKLANDIDSAVKTLSDRAYEIALGHIRNNREA 643
Cdd:CHL00176 521 NDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRFMQRNSeYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVL 600
                        570       580       590
                 ....*....|....*....|....*....|...
gi 685370626 644 MDKIVEVLLEKETMSGDEFRAILSEFTEIPPEN 676
Cdd:CHL00176 601 IDLLVELLLQKETIDGDEFREIVNSYTILPPKK 633
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
85-668 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 848.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  85 QGVSSSRMSYSRFLEYLDKGRVDKVDLyeNGTIAIVEAVSPELgnriQRVRVQLPGlSQELLQKLRAKNIDFAAhtTQED 164
Cdd:COG0465   15 SSSSVKEISYSEFLQLVEAGKVKSVTI--QGDRITGTLKDGTK----TRFTTYRVN-DPELVDLLEEKGVEVTA--KPPE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 165 QGSPLLNLIGNLAFPLILIGGLFLLSRRSSGGMGGPggpgfpLQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVE 244
Cdd:COG0465   86 ESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGA------MSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 245 FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVF 324
Cdd:COG0465  160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 325 VDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTE 404
Cdd:COG0465  240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 405 ILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSIDRIVAGMEGT--VMTDgKSK 482
Cdd:COG0465  320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKsrVISE-KEK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 483 SLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIFGepEVTTG 562
Cdd:COG0465  399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTG 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 563 AVGDLQQITGLAKQMVTTFGMSE-IGPWSLMDSSAQSDVIMRMMARNSMSEKLANDIDSAVKTLSDRAYEIALGHIRNNR 641
Cdd:COG0465  477 ASNDLERATKIARAMVTEYGMSEkLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENR 556
                        570       580
                 ....*....|....*....|....*..
gi 685370626 642 EAMDKIVEVLLEKETMSGDEFRAILSE 668
Cdd:COG0465  557 DKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
209-667 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 729.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  209 IGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPF 288
Cdd:TIGR01241  37 FGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPF 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  289 FSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIV 368
Cdd:TIGR01241 117 FSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  369 VAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAG 448
Cdd:TIGR01241 197 IAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  449 RRGKTAISSKEIDDSIDRIVAGMEGT--VMTDgKSKSLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSD 526
Cdd:TIGR01241 277 RKNKTEITMNDIEEAIDRVIAGPEKKsrVISE-KEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEE 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  527 DPTLISKQQLFARIVGGLGGRAAEEVIFGepEVTTGAVGDLQQITGLAKQMVTTFGMSE-IGPWSLMDSSAQSDVIMRMM 605
Cdd:TIGR01241 356 DKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDkLGPVAYGSDGGDVFLGRGFA 433
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685370626  606 ARNSMSEKLANDIDSAVKTLSDRAYEIALGHIRNNREAMDKIVEVLLEKETMSGDEFRAILS 667
Cdd:TIGR01241 434 KAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
224-394 6.50e-125

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: 368.10  E-value: 6.50e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 224 VTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGV 303
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 304 GASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALL 383
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 685370626 384 RPGRFDRQVSV 394
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
475-665 1.28e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 274.86  E-value: 1.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  475 VMTDgKSKSLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIF 554
Cdd:pfam01434   2 VISE-EEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  555 GepEVTTGAVGDLQQITGLAKQMVTTFGMSE-IGPWSLMDSSAQSDVIMRMMARNSMSEKLANDIDSAVKTLSDRAYEIA 633
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDkLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 685370626  634 LGHIRNNREAMDKIVEVLLEKETMSGDEFRAI 665
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
260-398 8.20e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.58  E-value: 8.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626   260 PKGVLLVGPPGTGKTLLAKAIAGEA---GVPFFSISGSEFVE--------------MFVGVGASRVRDLFKKAKENAPCI 322
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685370626   323 VFVDEIDAVGRQRGtgigggndEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPgRFDRQVSVDVPD 398
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
263-284 3.13e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.76  E-value: 3.13e-03
                         10        20
                 ....*....|....*....|..
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEA 284
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAA 114
 
Name Accession Description Interval E-value
ftsH CHL00176
cell division protein; Validated
85-676 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 910.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  85 QGVSSSRMSYSRFLEYLDKGRVDKVDLYENGTIAIVEAVSPELGNRIQRVRVQLPGLSQELLQKLRAKNIDFAAHTTQED 164
Cdd:CHL00176  45 QNKASSRMTYGRFLEYLDMGWIKKVDLYDNGRTAIVEASSPELGNRPQRIRVELPVGASELIQKLKEANIDFDAHPPVLK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 165 qgSPLLNLIGNLAFPLILIGGLFLLSRRSSGGMGGPGGPGfpLQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVE 244
Cdd:CHL00176 125 --SNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQNL--MNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVS 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 245 FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVF 324
Cdd:CHL00176 201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVF 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 325 VDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTE 404
Cdd:CHL00176 281 IDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLD 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 405 ILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSIDRIVAGMEGTVMTDGKSKSL 484
Cdd:CHL00176 361 ILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKRL 440
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 485 VAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIFGEPEVTTGAV 564
Cdd:CHL00176 441 IAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEVTTGAS 520
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 565 GDLQQITGLAKQMVTTFGMSEIGPWSLMDSSAQSDVIMRMMARNS-MSEKLANDIDSAVKTLSDRAYEIALGHIRNNREA 643
Cdd:CHL00176 521 NDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRFMQRNSeYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVL 600
                        570       580       590
                 ....*....|....*....|....*....|...
gi 685370626 644 MDKIVEVLLEKETMSGDEFRAILSEFTEIPPEN 676
Cdd:CHL00176 601 IDLLVELLLQKETIDGDEFREIVNSYTILPPKK 633
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
85-668 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 848.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  85 QGVSSSRMSYSRFLEYLDKGRVDKVDLyeNGTIAIVEAVSPELgnriQRVRVQLPGlSQELLQKLRAKNIDFAAhtTQED 164
Cdd:COG0465   15 SSSSVKEISYSEFLQLVEAGKVKSVTI--QGDRITGTLKDGTK----TRFTTYRVN-DPELVDLLEEKGVEVTA--KPPE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 165 QGSPLLNLIGNLAFPLILIGGLFLLSRRSSGGMGGPggpgfpLQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVE 244
Cdd:COG0465   86 ESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGA------MSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 245 FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVF 324
Cdd:COG0465  160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 325 VDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTE 404
Cdd:COG0465  240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 405 ILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSIDRIVAGMEGT--VMTDgKSK 482
Cdd:COG0465  320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKsrVISE-KEK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 483 SLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIFGepEVTTG 562
Cdd:COG0465  399 KITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTG 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 563 AVGDLQQITGLAKQMVTTFGMSE-IGPWSLMDSSAQSDVIMRMMARNSMSEKLANDIDSAVKTLSDRAYEIALGHIRNNR 641
Cdd:COG0465  477 ASNDLERATKIARAMVTEYGMSEkLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENR 556
                        570       580
                 ....*....|....*....|....*..
gi 685370626 642 EAMDKIVEVLLEKETMSGDEFRAILSE 668
Cdd:COG0465  557 DKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
209-667 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 729.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  209 IGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPF 288
Cdd:TIGR01241  37 FGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPF 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  289 FSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIV 368
Cdd:TIGR01241 117 FSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  369 VAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAG 448
Cdd:TIGR01241 197 IAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  449 RRGKTAISSKEIDDSIDRIVAGMEGT--VMTDgKSKSLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSD 526
Cdd:TIGR01241 277 RKNKTEITMNDIEEAIDRVIAGPEKKsrVISE-KEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEE 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  527 DPTLISKQQLFARIVGGLGGRAAEEVIFGepEVTTGAVGDLQQITGLAKQMVTTFGMSE-IGPWSLMDSSAQSDVIMRMM 605
Cdd:TIGR01241 356 DKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDkLGPVAYGSDGGDVFLGRGFA 433
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685370626  606 ARNSMSEKLANDIDSAVKTLSDRAYEIALGHIRNNREAMDKIVEVLLEKETMSGDEFRAILS 667
Cdd:TIGR01241 434 KAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
207-691 5.91e-176

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 516.89  E-value: 5.91e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 207 LQIGQSKAKFQMEPNTGVTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGV 286
Cdd:PRK10733 132 MSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 287 PFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGV 366
Cdd:PRK10733 212 PFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGI 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 367 IVVAATNRADILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAIL 446
Cdd:PRK10733 292 IVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALF 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 447 AGRRGKTAISSKEIDDSIDRIVAGME--GTVMTDGKSKSlVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIP 524
Cdd:PRK10733 372 AARGNKRVVSMVEFEKAKDKIMMGAErrSMVMTEAQKES-TAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLP 450
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 525 SDDPTLISKQQLFARIVGGLGGRAAEEVIFGEPEVTTGAVGDLQQITGLAKQMVTTFGMSE-IGPwsLMDSSAQSDVIM- 602
Cdd:PRK10733 451 EGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEkLGP--LLYAEEEGEVFLg 528
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 603 RMMAR-NSMSEKLANDIDSAVKTLSDRAYEIALGHIRNNREAMDKIVEVLLEKETMSGDEFRAILSEFTEIPP---ENRV 678
Cdd:PRK10733 529 RSVAKaKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPagwEEPG 608
                        490
                 ....*....|...
gi 685370626 679 ASATSTSTPTPAS 691
Cdd:PRK10733 609 ASNNSDDNGTPKA 621
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
224-394 6.50e-125

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: 368.10  E-value: 6.50e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 224 VTFDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGV 303
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 304 GASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALL 383
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 685370626 384 RPGRFDRQVSV 394
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
223-467 5.95e-111

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 338.13  E-value: 5.95e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 223 GVTFDDVAGVDEAKQDFMEVVE-FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFV 301
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 302 GVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGndEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSA 381
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 382 LLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEID 461
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLE 311

                 ....*.
gi 685370626 462 DSIDRI 467
Cdd:COG1222  312 KAIEKV 317
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
218-478 7.31e-97

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 303.68  E-value: 7.31e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 218 ME----PNtgVTFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSIS 292
Cdd:PRK03992 120 MEviesPN--VTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVV 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 293 GSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAAT 372
Cdd:PRK03992 198 GSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAAT 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 373 NRADILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGK 452
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDR 357
                        250       260
                 ....*....|....*....|....*.
gi 685370626 453 TAISSKEIDDSIDRIVAGMEGTVMTD 478
Cdd:PRK03992 358 TEVTMEDFLKAIEKVMGKEEKDSMEE 383
Peptidase_M41 pfam01434
Peptidase family M41;
475-665 1.28e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 274.86  E-value: 1.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  475 VMTDgKSKSLVAYHEVGHAVCGTLTPGHDAVQKVTLIPRGQARGLTWFIPSDDPTLISKQQLFARIVGGLGGRAAEEVIF 554
Cdd:pfam01434   2 VISE-EEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  555 GepEVTTGAVGDLQQITGLAKQMVTTFGMSE-IGPWSLMDSSAQSDVIMRMMARNSMSEKLANDIDSAVKTLSDRAYEIA 633
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDkLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 685370626  634 LGHIRNNREAMDKIVEVLLEKETMSGDEFRAI 665
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
216-467 1.63e-82

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: 265.51  E-value: 1.63e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  216 FQMEPNTGVTFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGS 294
Cdd:TIGR01242 111 MEVEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  295 EFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNR 374
Cdd:TIGR01242 191 ELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNR 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  375 ADILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTA 454
Cdd:TIGR01242 271 PDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY 350
                         250
                  ....*....|...
gi 685370626  455 ISSKEIDDSIDRI 467
Cdd:TIGR01242 351 VTMDDFIKAVEKV 363
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
226-467 4.71e-77

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: 252.52  E-value: 4.71e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 226 FDDVAGVDEAKQDFMEVVE-FLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVG 304
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 305 ASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGtGIGGGNDEREqtLNQLLTEMDGFEGNtgVIVVAATNRADILDSALLR 384
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELRSD--VVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 385 pgRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDDSI 464
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ...
gi 685370626 465 DRI 467
Cdd:COG0464  389 ERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
220-461 1.83e-72

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: 249.05  E-value: 1.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  220 PNtgVTFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVE 298
Cdd:TIGR01243 448 PN--VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  299 MFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEReqTLNQLLTEMDGFEGNTGVIVVAATNRADIL 378
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDIL 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  379 DSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSK 458
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683

                  ...
gi 685370626  459 EID 461
Cdd:TIGR01243 684 KLE 686
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
225-394 5.39e-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: 220.29  E-value: 5.39e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 225 TFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGV 303
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 304 GASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALL 383
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 685370626 384 RPGRFDRQVSV 394
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
224-460 7.04e-68

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: 236.73  E-value: 7.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  224 VTFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVG 302
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  303 VGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGggnDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSAL 382
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  383 LRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRR----GKTAISSK 458
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfireGKINFEAE 411

                  ..
gi 685370626  459 EI 460
Cdd:TIGR01243 412 EI 413
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
217-468 2.37e-64

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 218.48  E-value: 2.37e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 217 QMEPNTGVTFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSE 295
Cdd:PTZ00454 135 QMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 296 FVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRA 375
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRA 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 376 DILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAI 455
Cdd:PTZ00454 295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVI 374
                        250
                 ....*....|...
gi 685370626 456 SSKEIDDSIDRIV 468
Cdd:PTZ00454 375 LPKDFEKGYKTVV 387
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
235-394 3.20e-63

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: 207.14  E-value: 3.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 235 AKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKK 314
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 315 AKENAPCIVFVDEIDAVGRQRGTgiGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSV 394
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
235-394 9.47e-63

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: 205.98  E-value: 9.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 235 AKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFK 313
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 314 KAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEReqTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVS 393
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 685370626 394 V 394
Cdd:cd19511  159 V 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
225-449 1.12e-61

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 212.71  E-value: 1.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 225 TFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGV 303
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 304 GASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALL 383
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685370626 384 RPGRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEAAILAGR 449
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALR 406
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
226-467 4.68e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 202.04  E-value: 4.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 226 FDDVAGVDEAKQDFMEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGA 305
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 306 SRVRDLFKKAKEnAPCIVFVDEIDAVGRQRgtgiGGGNDERE--QTLNQLLTEMDGFegNTGVIVVAATNRADILDSALL 383
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDR----GDQNDVGEvkRVVNALLQELDGL--PSGSVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 384 RpgRFDRQVSVDVPDVKGRTEILKVHSGNKKFEDGVSLEVIAMRTPGFSGADLANLLNEA---AILAGRRgktAISSKEI 460
Cdd:COG1223  154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTAlkkAILEDRE---KVTKEDL 228

                 ....*..
gi 685370626 461 DDSIDRI 467
Cdd:COG1223  229 EEALKQR 235
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
235-394 4.36e-59

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: 196.18  E-value: 4.36e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 235 AKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFK 313
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 314 KAKENAPCIVFVDEIDAVGRQRGTGIGGGNDEReqTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVS 393
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 685370626 394 V 394
Cdd:cd19529  159 I 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 ...
228-392 6.52e-58

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: 193.28  E-value: 6.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGAS 306
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 307 RVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGiGGGNDEReqTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPG 386
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*.
gi 685370626 387 RFDRQV 392
Cdd:cd19503  158 RFDREV 163
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
236-394 9.27e-55

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: 184.64  E-value: 9.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 236 KQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKK 314
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 315 AKENAPCIVFVDEIDAVGRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSV 394
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
263-392 1.51e-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: 180.10  E-value: 1.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgigGG 342
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 685370626  343 NDEREQTLNQLLTEMDGFEGNTG-VIVVAATNRADILDSALLrpGRFDRQV 392
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRII 126
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
228-394 9.87e-52

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: 176.47  E-value: 9.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGAS 306
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 307 RVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgiGGGNDEReQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPG 386
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK--THGEVER-RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*...
gi 685370626 387 RFDRQVSV 394
Cdd:cd19519  158 RFDREIDI 165
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
240-394 2.69e-51

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: 175.37  E-value: 2.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 240 MEVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKKAKENA 319
Cdd:cd19530   10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685370626 320 PCIVFVDEIDAVGRQRGtgiGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSV 394
Cdd:cd19530   90 PCVIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
235-392 1.63e-48

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: 167.61  E-value: 1.63e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 235 AKQDFMEVVEFLKK-PERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFK 313
Cdd:cd19526    1 VKKALEETIEWPSKyPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685370626 314 KAKENAPCIVFVDEIDAVGRQRGTGIGGGNDereQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQV 392
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
228-394 4.48e-48

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: 166.81  E-value: 4.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFMEVVEFLKKPERFTA-VGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGAS 306
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQhLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 307 RVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgigGGNDEREQTLNQLLTEMD--GFEGNTG--VIVVAATNRADILDSAL 382
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRES---AQREMERRIVSQLLTCMDelNNEKTAGgpVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|..
gi 685370626 383 LRPGRFDRQVSV 394
Cdd:cd19518  158 RRAGRFDREICL 169
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
236-394 3.82e-43

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: 153.05  E-value: 3.82e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 236 KQDFMEVVEF-LKKPERFtAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFKK 314
Cdd:cd19527    2 KKEILDTIQLpLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 315 AKENAPCIVFVDEIDAVGRQRG-TGIGGGNDEReqTLNQLLTEMDGFE-GNTGVIVVAATNRADILDSALLRPGRFDRQV 392
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGnSGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 685370626 393 SV 394
Cdd:cd19527  159 YL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
229-394 2.30e-40

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: 145.19  E-value: 2.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 229 VAGVDEAKQDFMEVVEF-LKKPERFTAvGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASR 307
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFPG-LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 308 VRDLFKKAKENAPCIVFVDEIDAVGRQRGTgiggGNDEREQTL-NQLLTEMDGFEG--NTGVIVVAATNRADILDSALLR 384
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNkpEDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 685370626 385 pgRFDRQVSV 394
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
219-392 5.33e-37

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: 136.15  E-value: 5.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 219 EPNtgVTFDDVAGVDEAKQDFMEVVEF-LKKPERFTavGARIP-KGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEF 296
Cdd:cd19521    1 KPN--VKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 297 VEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgigGGNDEREQTLNQLLTEMDGFEGNT-GVIVVAATNRA 375
Cdd:cd19521   77 VSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDSqGVLVLGATNIP 153
                        170
                 ....*....|....*..
gi 685370626 376 DILDSALLRpgRFDRQV 392
Cdd:cd19521  154 WQLDSAIRR--RFEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
228-394 4.91e-33

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: 124.96  E-value: 4.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFMEVVEF-LKKPERFTAVGARiPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGAS 306
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 307 RVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgigGGNDEREQTLNQLLTEMDGFEGNTG--VIVVAATNRADILDSALLR 384
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 685370626 385 pgRFDRQVSV 394
Cdd:cd19524  157 --RFTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
228-391 6.52e-33

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: 124.54  E-value: 6.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFMEVVEF-LKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAG-----VPFFSISGSEFVEMFV 301
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 302 GVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgigggndEREQT----LNQLLTEMDGFEGNTGVIVVAATNRADI 377
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....
gi 685370626 378 LDSALLRPGRFDRQ 391
Cdd:cd19517  154 LDPALRRPGRFDRE 167
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
218-394 3.55e-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: 123.17  E-value: 3.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 218 MEPNTGVTFDDVAGVDEAKQDFMEVVEF-LKKPERFTAVGARiPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEF 296
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 297 VEMFVGVGASRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgigGGNDEREQTLNQLLTEMDGfeGNTG----VIVVAAT 372
Cdd:cd19525   92 TSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDG--ATTSsedrILVVGAT 166
                        170       180
                 ....*....|....*....|..
gi 685370626 373 NRADILDSALLRpgRFDRQVSV 394
Cdd:cd19525  167 NRPQEIDEAARR--RLVKRLYI 186
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
228-388 5.24e-32

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 121.76  E-value: 5.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFMEVVEF-LKKPERFTAVG-ARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGA 305
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 306 SRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGigggndEREQTL---NQLLTEMDGF--EGNTGVIVVAATNRADILDS 380
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDE 154
                        170
                 ....*....|
gi 685370626 381 ALLR--PGRF 388
Cdd:cd19520  155 AILRrmPKRF 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
228-394 6.36e-32

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: 122.02  E-value: 6.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFME-VVEFLKKPERFTavGARIP-KGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGA 305
Cdd:cd19522    1 DIADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 306 SRVRDLFKKAKENAPCIVFVDEIDAVGRQRGTgiGGGNDEREQTLNQLLTEMDGFEGNTG-------VIVVAATNRADIL 378
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGASEnddpskmVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 685370626 379 DSALLRpgRFDRQVSV 394
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
249-394 2.37e-30

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 117.59  E-value: 2.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 249 PERFTAVGARIPKGVLLVGPPGTGKTLLAKAI-----AGEAGVpffsISGSEFVEMFVGVGASRVRDLFKKAKENAPC-- 321
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685370626 322 ------IVFVDEIDAVGRQRGTGiGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSV 394
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
238-395 1.73e-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: 108.39  E-value: 1.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 238 DFMEVVEFLKKperftAVGARIPKGVLLVGPPGTGKTLLAKAIAGEA---GVPFFSISGSEFVEMFVG---VGASRVRDL 311
Cdd:cd00009    2 GQEEAIEALRE-----ALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 312 FKKAKENAPCIVFVDEIDAVGRqrgtgigggnDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQ 391
Cdd:cd00009   77 FELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146

                 ....
gi 685370626 392 VSVD 395
Cdd:cd00009  147 IVIP 150
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
228-390 3.22e-25

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: 102.45  E-value: 3.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKqdfmevvEFLKKPER-FT----AVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVG 302
Cdd:cd19507    1 DVGGLDNLK-------DWLKKRKAaFSkqasAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 303 VGASRVRDLFKKAKENAPCIVFVDEID-AVGRQRGTGIGGGNderEQTLNQLLTEMDgfEGNTGVIVVAATNRADILDSA 381
Cdd:cd19507   74 ESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTS---SRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPE 148

                 ....*....
gi 685370626 382 LLRPGRFDR 390
Cdd:cd19507  149 LLRKGRFDE 157
ycf46 CHL00195
Ycf46; Provisional
221-443 3.85e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 109.72  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 221 NTGVTFDDVAGVDEAKQdfmevveFLKK-----PERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSE 295
Cdd:CHL00195 222 SVNEKISDIGGLDNLKD-------WLKKrstsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGK 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 296 FVEMFVGVGASRVRDLFKKAKENAPCIVFVDEID-AVGRQRGTGIGGgndereqTLNQLLTEMDGF--EGNTGVIVVAAT 372
Cdd:CHL00195 295 LFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLATFITWlsEKKSPVFVVATA 367
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685370626 373 NRADILDSALLRPGRFDRQVSVDVPDVKGRTEILKVHSGN------KKFEdgvsLEVIAMRTPGFSGADLANLLNEA 443
Cdd:CHL00195 368 NNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKfrpkswKKYD----IKKLSKLSNKFSGAEIEQSIIEA 440
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
228-384 2.19e-19

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: 85.71  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 228 DVAGVDEAKQDFM-EVVEFLKKPERFTAVgARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGAS 306
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 307 RVRDLFKKAKENAPCIVFVDEIDAVGRQRGTGIGGGNdeREQTlnQLLTEMDGF--EGNTGVIVVAATNRADILDSALLR 384
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
260-398 8.20e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.58  E-value: 8.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626   260 PKGVLLVGPPGTGKTLLAKAIAGEA---GVPFFSISGSEFVE--------------MFVGVGASRVRDLFKKAKENAPCI 322
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685370626   323 VFVDEIDAVGRQRGtgigggndEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPgRFDRQVSVDVPD 398
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
241-394 9.36e-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: 83.55  E-value: 9.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 241 EVVEFLKKPERFTAVGARIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEfvemfVGVGASRVRDLFKKAKENAp 320
Cdd:cd19510    4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685370626 321 cIVFVDEIDAV---GRQRGTGIGGGNDEREQTLNQLLTEMDGFEGNTGVIVVAATNRADILDSALLRPGRFDRQVSV 394
Cdd:cd19510   78 -IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
261-392 3.27e-11

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: 61.77  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 261 KGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGvGASRVRDLFKKA-KENAPCIVFVDEIDAVGRQRGTgi 339
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRST-- 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685370626 340 GGGNDEREQTLNQLLTEMDgfEGNTGVIVVAATNRADILDSALlrPGRFDRQV 392
Cdd:cd19512  100 EKISEDLRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
PRK04195 PRK04195
replication factor C large subunit; Provisional
225-344 6.96e-11

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 64.94  E-value: 6.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 225 TFDDVAGVDEAKQDFMEVVE-FLKKperftavgaRIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEF-----VE 298
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIEsWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 685370626 299 MFVGvGASRVRDLFKKAKEnapcIVFVDEIDavgrqrgtGIGGGND 344
Cdd:PRK04195  83 RVAG-EAATSGSLFGARRK----LILLDEVD--------GIHGNED 115
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
419-462 9.27e-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: 57.16  E-value: 9.27e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 685370626  419 VSLEVIAMRTPGFSGADLANLLNEAAILAGRRGKTAISSKEIDD 462
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
260-394 1.61e-10

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: 60.08  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 260 PKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFV--------------EMFVGVGASRVRDLFKKAKENAPCIVFV 325
Cdd:cd19505   12 SKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSPCIIWI 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685370626 326 DEIDAVGRQRGTGIGGGNdeREQTLNQLLTEM-DGFEGNT--GVIVVAATNRADILDSALLRPGRFDRQVSV 394
Cdd:cd19505   92 PNIHELNVNRSTQNLEED--PKLLLGLLLNYLsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
259-364 2.78e-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: 60.09  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 259 IPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEM-FVGVGA-SRVRDLFKKakenapcIVFVDEIDAVGRQrg 336
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIAKR-- 115
                         90       100
                 ....*....|....*....|....*...
gi 685370626 337 TGIGGGNDEREQTLNQLLTEMDGFEGNT 364
Cdd:cd19498  116 GGSSGPDVSREGVQRDLLPIVEGSTVST 143
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
263-328 2.91e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 62.77  E-value: 2.91e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISGsefvemfVGVGASRVRDLFKKAKENA----PCIVFVDEI 328
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
263-328 4.84e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 62.02  E-value: 4.84e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSefvemFVGVgaSRVRDLFKKAKENA----PCIVFVDEI 328
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
261-296 3.47e-09

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 59.60  E-value: 3.47e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 685370626 261 KGVLLVGPPGTGKTLLAKAIAGEAG--VPFFSISGSEF 296
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
262-388 4.22e-09

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: 55.38  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  262 GVLLVGPPGTGKTLLAKAIAgEA--GVPFFSISGSEF---------VEMFVGVGASRVRDLFKKAKEnaPCIVFVDEIDA 330
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAARE--GEIAVLDEINR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685370626  331 vgrqrgtgiggGNDEREQTLNQLLTE-----MDGFE----GNTGVIVVAATNRADI----LDSALLRpgRF 388
Cdd:pfam07728  78 -----------ANPDVLNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
212-333 2.93e-08

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: 54.10  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 212 SKAKFQMEpntgvtfDDVAGVDEAKQdfmEVVEFLkkperftAVGARIPKG----VLLVGPPGTGKTLLAKAIAGEAGVP 287
Cdd:cd19500    2 KKARKVLD-------ADHYGLEDVKE---RILEYL-------AVRKLKGSMkgpiLCLVGPPGVGKTSLGKSIARALGRK 64
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 685370626 288 FFSIS-G--SEFVEM------FVGVGASRVRDLFKKAKENAPCIVfVDEIDAVGR 333
Cdd:cd19500   65 FVRISlGgvRDEAEIrghrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
263-382 4.27e-08

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. 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: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 53.99  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPF-FSISGSEFVEM--------FVGVGASRVRDLFKKAKE---NAPCIVFV--DEI 328
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQElidDKDALVFVliDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685370626 329 DAVGRQRgTGIGGGNDERE--QTLNQLLTEMDGFEGNTGVIVVAATNRADILDSAL 382
Cdd:cd19508  135 ESLAAAR-SASSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
261-296 8.62e-08

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: 54.62  E-value: 8.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 685370626  261 KGVLLVGPPGTGKTLLAKAIAGEAG--VPFFSISGSEF 296
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
71-158 7.49e-07

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 47.98  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626   71 GVGLLGTGKANADEQGVSSSRMSYSRFLEYLDKGRVDKVDLYEN-----GTIAIVEAVSPELGNRIQRVRVQLPGLSQEL 145
Cdd:pfam06480   8 LLVLLLLFLLFLLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDeilptGVVEGTLKDGSKFTTYFIPSLPNVDSLLEKL 87
                          90
                  ....*....|...
gi 685370626  146 LQKLRAKNIDFAA 158
Cdd:pfam06480  88 EDALEEKGVKVSV 100
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
263-379 8.68e-07

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: 48.27  E-value: 8.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEA---GVPFFSISgseFVEMFVgvgaSRVRDLfkkAKENAPCIVFVDEIDAVGRQRgtgi 339
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDL---IEEKKLDIIIIDSLSSLARAS---- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685370626 340 ggGNDEREQTLNQLLTEMDGFeGNTGVIVVAATNRADILD 379
Cdd:cd01120   67 --QGDRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI 103
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
263-411 1.67e-06

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: 50.17  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPFF----------------SISGSEFVEMFVGVGAsrvrdLFKkakenapCIVFVD 326
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGP-----LFA-------NVLLAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 327 EIDavgrqRGTgigggnderEQTLNQLLTEMDGFE----GNT-----GVIVVAATNRADI-----LDSALLRpgRFDRQV 392
Cdd:COG0714  102 EIN-----RAP---------PKTQSALLEAMEERQvtipGGTyklpePFLVIATQNPIEQegtypLPEAQLD--RFLLKL 165
                        170
                 ....*....|....*....
gi 685370626 393 SVDVPDVKGRTEILKVHSG 411
Cdd:COG0714  166 YIGYPDAEEEREILRRHTG 184
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
246-336 2.13e-06

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 51.17  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 246 LKKP-ER---FTAVGARIPKG----VLLVGPPGTGKTLLAKAIAgEAgvpffsiSGSEFVEMFVGvGasrVRD------- 310
Cdd:COG0466  330 LEKVkERileYLAVRKLKKKLkgpiLCLVGPPGVGKTSLGKSIA-RA-------LGRKFVRISLG-G---VRDeaeirgh 397
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685370626 311 --------------LFKKAKENAPciVFV-DEIDAVGR-QRG 336
Cdd:COG0466  398 rrtyigampgriiqGLKKAGTKNP--VFLlDEIDKMGSdFRG 437
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
260-467 5.53e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 260 PKGVLLVGPPGTGKTLLAKAI-------AGEAGVPF-------------FSISgSEFVEMFV--------GVGASRVRDL 311
Cdd:COG1474   51 PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVrvvyvncrqastrYRVL-SRILEELGsgedipstGLSTDELFDR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 312 FKKA--KENAPCIVFVDEIDAVGRqrgtgigggnDEREQTLNQLLTEMDGFEG-NTGVIVVaaTNRADILDsallrpgRF 388
Cdd:COG1474  130 LYEAldERDGVLVVVLDEIDYLVD----------DEGDDLLYQLLRANEELEGaRVGVIGI--SNDLEFLE-------NL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 389 DRQV-SV-----------DVPDVKgrtEILKVHSgNKKFEDGV-SLEVIAMrtpgfsGADLA-----------NLLNEAA 444
Cdd:COG1474  191 DPRVkSSlgeeeivfppyDADELR---DILEDRA-ELAFYDGVlSDEVIPL------IAALAaqehgdarkaiDLLRVAG 260
                        250       260
                 ....*....|....*....|...
gi 685370626 445 ILAGRRGKTAISSKEIDDSIDRI 467
Cdd:COG1474  261 EIAEREGSDRVTEEHVREAREKI 283
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
258-328 7.91e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.00  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 258 RIPKGVLLVGPPGTGKTLLAKAIAGEAG---------VPFF-SISGSEFVEMFVGVGAS---RVRD-LFK----KAKEN- 318
Cdd:COG1401  219 KTKKNVILAGPPGTGKTYLARRLAEALGgedngriefVQFHpSWSYEDFLLGYRPSLDEgkyEPTPgIFLrfclKAEKNp 298
                         90
                 ....*....|.
gi 685370626 319 -APCIVFVDEI 328
Cdd:COG1401  299 dKPYVLIIDEI 309
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
260-329 2.27e-05

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: 45.26  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  260 PKGV-LLVGPPGTGKTLLAKAIAGEAGV---PFFSISGSEFVE-----MFVG-----VGASRVRDLFKKAKENAPCIVFV 325
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 685370626  326 DEID 329
Cdd:pfam07724  82 DEIE 85
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
263-293 3.86e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 44.41  E-value: 3.86e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 685370626  263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISG 293
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
263-293 5.14e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.89  E-value: 5.14e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISG 293
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 84
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
218-281 2.22e-04

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 44.03  E-value: 2.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685370626 218 MEPNTGVTFDDVAGvdeakQDfmEVVEFLKKperftAVGA-RIPKGVLLVGPPGTGKTLLAKAIA 281
Cdd:COG2812    1 MSYQVPQTFDDVVG-----QE--HVVRTLKN-----ALASgRLAHAYLFTGPRGVGKTTLARILA 53
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
241-367 2.25e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 44.80  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 241 EVVEFLKKPERFTAVGARIPKgVLLVGPPGTGKTLLAKAIA---------GEAGVPFF--------SISGSEFVEMFVGV 303
Cdd:COG5635  162 NLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdlaeEASLEDLLAEALEK 240
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685370626 304 GASRVRDLFKKAKENAPCIVFVDEIDAVGRQrgtgigggnDEREQTLNQLLTEMDGFEGNTGVI 367
Cdd:COG5635  241 RGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII 295
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
263-293 2.36e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 43.92  E-value: 2.36e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISG 293
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
263-288 2.80e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 43.88  E-value: 2.80e-04
                         10        20
                 ....*....|....*....|....*.
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPF 288
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVPF 137
44 PHA02544
clamp loader, small subunit; Provisional
258-332 3.46e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.44  E-value: 3.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685370626 258 RIPKGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGS----EFVEMFVGVGASRVrDLFKKAKenapcIVFVDEIDAVG 332
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-SLTGGGK-----VIIIDEFDRLG 113
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
263-288 5.22e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.84  E-value: 5.22e-04
                         10        20
                 ....*....|....*....|....*.
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPF 288
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF 136
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
263-282 6.00e-04

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.11  E-value: 6.00e-04
                         10        20
                 ....*....|....*....|
gi 685370626 263 VLLVGPPGTGKTLLAKAIAG 282
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
264-329 6.23e-04

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 41.39  E-value: 6.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685370626 264 LLVGPPGTGKTLLAKAIAGE---AGVPFFSISGSEFVEMFVG----------VGASRVRDLFKKAKENAPCIVFVDEID 329
Cdd:cd19499   45 LFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
261-284 8.14e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 41.69  E-value: 8.14e-04
                         10        20
                 ....*....|....*....|....
gi 685370626 261 KGVLLVGPPGTGKTLLAKAIAGEA 284
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEA 123
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
263-288 8.70e-04

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 41.43  E-value: 8.70e-04
                         10        20
                 ....*....|....*....|....*.
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEAGVPF 288
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPF 78
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
263-282 1.68e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.21  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|
gi 685370626  263 VLLVGPPGTGKTLLAKAIAG 282
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
263-335 1.77e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 40.38  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 263 VLLVGPPGTGKT-LLAKAIAGEA----------GVPFFSISGSEFVEMFVGV-GASRVRD-LFKKAKENAPCIVFVdeID 329
Cdd:cd04105    3 VLLLGPSDSGKTaLFTKLTTGKVrstvtsiepnVASFYSNSSKGKKLTLVDVpGHEKLRDkLLEYLKASLKAIVFV--VD 80

                 ....*.
gi 685370626 330 AVGRQR 335
Cdd:cd04105   81 SATFQK 86
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
258-281 1.85e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 40.73  E-value: 1.85e-03
                         10        20
                 ....*....|....*....|....
gi 685370626 258 RIPKGVLLVGPPGTGKTLLAKAIA 281
Cdd:COG0470   16 RLPHALLLHGPPGIGKTTLALALA 39
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
261-327 1.86e-03

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. 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: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 39.43  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685370626 261 KGVLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVEMFVGVGASR--VRDLFKKAKENAPCIVFVDE 327
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGD 95
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
231-395 2.07e-03

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: 41.37  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  231 GVDEAKQDfmevVEFLK--------KPERFTAVGARiPKGVLLVGPPGTGKTLLAKAIAGE-AGVPFFS------ISGSE 295
Cdd:TIGR03922 280 GLERVKRQ----VAALKsstamalaRAERGLPVAQT-SNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRAD 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626  296 FVEMFVGVGASRVRDLFKKAKENapcIVFVDEIDAVGRqrgTGIGGGNDEREQTLNQLLTEMdgfEGNTGVIVVAATNRA 375
Cdd:TIGR03922 355 LIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVE---TGYGQKDPFGLEAIDTLLARM---ENDRDRLVVIGAGYR 425
                         170       180
                  ....*....|....*....|....*
gi 685370626  376 DILDSAL-----LRpGRFDRQVSVD 395
Cdd:TIGR03922 426 KDLDKFLevnegLR-SRFTRVIEFP 449
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
263-334 2.53e-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: 40.36  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685370626  263 VLLVGPPGTGKTLLAKAIAGEAGVPFFSISGSEFVemfvgvgasRVRDLFK-----KAKEnapcIVFVDEIDAVGRQ 334
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAiltnlEEGD----VLFIDEIHRLSPA 96
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
263-284 3.13e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.76  E-value: 3.13e-03
                         10        20
                 ....*....|....*....|..
gi 685370626 263 VLLVGPPGTGKTLLAKAIAGEA 284
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAA 114
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
248-381 3.74e-03

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 38.74  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 248 KPERFTAVGARIPKG--VLLVGPPGTGKTLLAKAIAGEA----------GVPFFSISGSEF----------VEMFVGV-- 303
Cdd:cd03246   14 EPPVLRNVSFSIEPGesLAIIGPSGSGKSTLARLILGLLrptsgrvrldGADISQWDPNELgdhvgylpqdDELFSGSia 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 304 -----GASRVRDLFKKAKENAPCIVFVDEIDAvgrqrgtgigGGNDEREQTLNQLLTEMDGfegnTGVIVVAATNRADIL 378
Cdd:cd03246   94 enilsGGQRQRLGLARALYGNPRILVLDEPNS----------HLDVEGERALNQAIAALKA----AGATRIVIAHRPETL 159

                 ...
gi 685370626 379 DSA 381
Cdd:cd03246  160 ASA 162
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
265-355 3.90e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 38.31  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 265 LVGPPGTGKTLLAKAIAGEAGVPFFSiSGSEFVEMFvgvGASrVRDLFKKAKENApcivF----VDEIDAVGRQRGTGI- 339
Cdd:cd00464    4 LIGMMGAGKTTVGRLLAKALGLPFVD-LDELIEQRA---GMS-IPEIFAEEGEEG----FreleREVLLLLLTKENAVIa 74
                         90
                 ....*....|....*..
gi 685370626 340 -GGGNDEREQTLNQLLT 355
Cdd:cd00464   75 tGGGAVLREENRRLLLE 91
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
225-280 7.42e-03

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 39.37  E-value: 7.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685370626 225 TFDDVAGVDEAkqdFMEVVEFLKKperftavGARIPKGVLLVGPPGTGKTLLAKAI 280
Cdd:COG3829  136 TFDDIIGKSPA---MKELLELAKR-------VAKSDSTVLILGESGTGKELFARAI 181
PRK13341 PRK13341
AAA family ATPase;
264-328 8.77e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 8.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685370626 264 LLVGPPGTGKTLLAKAIAGEAGVPFFSISGsefvemfVGVGASRVRDLFKKAKE-----NAPCIVFVDEI 328
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDEV 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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