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Conserved domains on  [gi|19075270|ref|NP_587770|]
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AAA family ATPase Pex1 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 614-771 5.19e-103

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: 317.06  E-value: 5.19e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 614 AKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFS 693
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270 694 RAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFC 771
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVYC 158
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 373-915 5.22e-86

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.


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 291.43  E-value: 5.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   373 QNIYINGPKGCGKSNLVHSLFDYYSLNSIyfqmIVSCSEIDRSSFAKFQSFWNNVFIQAERYEPSIIYLDDVHCLISSSN 452
Cdd:TIGR01243 213 KGVLLYGPPGTGKTLLAKAVANEAGAYFI----SINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   453 EngELGFVEEREIAFLQHQIINLKRKRKIIFIGFGEEFLTFSENLVLPLLFQIKIALPSLAVTRRKEILTtIFQENFSDI 532
Cdd:TIGR01243 289 E--VTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILK-VHTRNMPLA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   533 TMDSIEFISVKTEGYLMTDLVLFVK--------RLLSEAFVE-KIQNGPKHLMNKglIEKTLKDFV-------PLQLRKA 596
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKeaamaalrRFIREGKINfEAEEIPAEVLKE--LKVTMKDFMealkmvePSAIREV 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   597 KFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPEL 676
Cdd:TIGR01243 444 LVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEI 523

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   677 LDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQD-STGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMI 755
Cdd:TIGR01243 524 LSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   756 DPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSIN 835
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   836 AVDpsqttssftnltteskrnasmlalppesrynqnMQSMSDSKSVVIEDYMLMEALKKNSPSLNSEEFEHLSNLYRDFR 915
Cdd:TIGR01243 684 KLE---------------------------------VGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
 90-164 6.08e-23

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi beta-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


:

Pssm-ID: 462729  Cd Length: 77  Bit Score: 93.33  E-value: 6.08e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075270    90 EQLEIEPVTSNDWEIAERNAAWLEENLLVQYRVATT-ERFIIYLPSGTFIQFQPLKLIPSSL-CGRLLRTTEVLITP 164
Cdd:pfam09262   1 TTVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPgQILPVWVSGTTVARFRVTSIEPANSpFARLSPDTEVIVAP 77
 
Name Accession Description Interval E-value
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 614-771 5.19e-103

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: 317.06  E-value: 5.19e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 614 AKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFS 693
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270 694 RAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFC 771
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVYC 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 373-915 5.22e-86

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: 291.43  E-value: 5.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   373 QNIYINGPKGCGKSNLVHSLFDYYSLNSIyfqmIVSCSEIDRSSFAKFQSFWNNVFIQAERYEPSIIYLDDVHCLISSSN 452
Cdd:TIGR01243 213 KGVLLYGPPGTGKTLLAKAVANEAGAYFI----SINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   453 EngELGFVEEREIAFLQHQIINLKRKRKIIFIGFGEEFLTFSENLVLPLLFQIKIALPSLAVTRRKEILTtIFQENFSDI 532
Cdd:TIGR01243 289 E--VTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILK-VHTRNMPLA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   533 TMDSIEFISVKTEGYLMTDLVLFVK--------RLLSEAFVE-KIQNGPKHLMNKglIEKTLKDFV-------PLQLRKA 596
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKeaamaalrRFIREGKINfEAEEIPAEVLKE--LKVTMKDFMealkmvePSAIREV 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   597 KFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPEL 676
Cdd:TIGR01243 444 LVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEI 523

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   677 LDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQD-STGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMI 755
Cdd:TIGR01243 524 LSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   756 DPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSIN 835
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   836 AVDpsqttssftnltteskrnasmlalppesrynqnMQSMSDSKSVVIEDYMLMEALKKNSPSLNSEEFEHLSNLYRDFR 915
Cdd:TIGR01243 684 KLE---------------------------------VGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 596-835 3.72e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 268.41  E-value: 3.72e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 596 AKFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPE 675
Cdd:COG1222  68 VPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 676 LLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDST-GVTDRVVNQILTQMDGAESLDGVYIVAATTRPDM 754
Cdd:COG1222 148 LVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTsGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDL 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 755 IDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSI 834
Cdd:COG1222 228 LDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307


                .
gi 19075270 835 N 835
Cdd:COG1222 308 E 308
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 603-835 6.28e-57

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: 209.76  E-value: 6.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   603 IRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIG 682
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   683 KSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRP 762
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRP 334

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075270   763 GRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSIN 835
Cdd:TIGR01243 335 GRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKIN 407
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 600-825 1.33e-52

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 188.89  E-value: 1.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  600 KSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDK 679
Cdd:PRK03992 125 SPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  680 YIGKSEQGVRDLFsraQMAK---PCVLFFDEFDSVAPRRGQDSTGvTDRVVN----QILTQMDGAESLDGVYIVAATTRP 752
Cdd:PRK03992 205 FIGEGARLVRELF---ELARekaPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRI 280

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075270  753 DMIDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAV 825
Cdd:PRK03992 281 DILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 643-773 3.95e-46

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: 161.22  E-value: 3.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   643 ILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGV 722
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19075270   723 TDRVVNQILTQMDGAESLDG-VYIVAATTRPDMIDPALLrpGRLDKLIFCDL 773
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
 90-164 6.08e-23

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi beta-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


Pssm-ID: 462729  Cd Length: 77  Bit Score: 93.33  E-value: 6.08e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075270    90 EQLEIEPVTSNDWEIAERNAAWLEENLLVQYRVATT-ERFIIYLPSGTFIQFQPLKLIPSSL-CGRLLRTTEVLITP 164
Cdd:pfam09262   1 TTVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPgQILPVWVSGTTVARFRVTSIEPANSpFARLSPDTEVIVAP 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 640-770 1.05e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 66.63  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270    640 PTGILLFGYPGCGKTYLASAISSTFPVQ---FISIKGPELL--------------DKYIGKSEQGVRDLFSRAQMAKPCV 702
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270    703 LFFDEFDSVAPRRGQDstgvtDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPgRLDKLIF 770
Cdd:smart00382  82 LILDEITSLLDAEQEA-----LLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIV 143
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 375-510 3.33e-11

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: 61.46  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   375 IYINGPKGCGKSNLVHSLFDYYSLNsiyFqMIVSCSEIDRSSFAKFQSFWNNVFIQAERYEPSIIYLDDVHCLISSSNEN 454
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAP---F-IEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270   455 GElgFVEEREIAFLQHQIINLKRK-RKIIFIGFGEEFLTFSEnlvlPLL--FQIKIALP 510
Cdd:pfam00004  77 GD--SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDP----ALLgrFDRIIEFP 129
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 360-485 1.02e-04

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: 43.67  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 360 HEFAQVRNAVFLHQ--NIYINGPKGCGKSNLVHSLFDYYSLNSIYFqMIVSCSEI---DRSSFAKFQSFWNNVFIQAERY 434
Cdd:cd00009   5 EAIEALREALELPPpkNLLLYGPPGTGKTTLARAIANELFRPGAPF-LYLNASDLlegLVVAELFGHFLVRLLFELAEKA 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19075270 435 EPSIIYLDDVHCLISSSNENGELgfveereiaFLQHQIINLKRKRKIIFIG 485
Cdd:cd00009  84 KPGVLFIDEIDSLSRGAQNALLR---------VLETLNDLRIDRENVRVIG 125
 
Name Accession Description Interval E-value
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 614-771 5.19e-103

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: 317.06  E-value: 5.19e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 614 AKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFS 693
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270 694 RAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFC 771
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVYC 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 614-771 4.21e-91

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: 285.72  E-value: 4.21e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 614 AKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFS 693
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270 694 RAQMAKPCVLFFDEFDSVAPRRGQ-DSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFC 771
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQsDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 373-915 5.22e-86

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: 291.43  E-value: 5.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   373 QNIYINGPKGCGKSNLVHSLFDYYSLNSIyfqmIVSCSEIDRSSFAKFQSFWNNVFIQAERYEPSIIYLDDVHCLISSSN 452
Cdd:TIGR01243 213 KGVLLYGPPGTGKTLLAKAVANEAGAYFI----SINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   453 EngELGFVEEREIAFLQHQIINLKRKRKIIFIGFGEEFLTFSENLVLPLLFQIKIALPSLAVTRRKEILTtIFQENFSDI 532
Cdd:TIGR01243 289 E--VTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILK-VHTRNMPLA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   533 TMDSIEFISVKTEGYLMTDLVLFVK--------RLLSEAFVE-KIQNGPKHLMNKglIEKTLKDFV-------PLQLRKA 596
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKeaamaalrRFIREGKINfEAEEIPAEVLKE--LKVTMKDFMealkmvePSAIREV 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   597 KFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPEL 676
Cdd:TIGR01243 444 LVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEI 523

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   677 LDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQD-STGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMI 755
Cdd:TIGR01243 524 LSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   756 DPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSIN 835
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   836 AVDpsqttssftnltteskrnasmlalppesrynqnMQSMSDSKSVVIEDYMLMEALKKNSPSLNSEEFEHLSNLYRDFR 915
Cdd:TIGR01243 684 KLE---------------------------------VGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 596-835 3.72e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 268.41  E-value: 3.72e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 596 AKFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPE 675
Cdd:COG1222  68 VPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 676 LLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDST-GVTDRVVNQILTQMDGAESLDGVYIVAATTRPDM 754
Cdd:COG1222 148 LVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTsGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDL 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 755 IDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSI 834
Cdd:COG1222 228 LDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307


                .
gi 19075270 835 N 835
Cdd:COG1222 308 E 308
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 593-833 1.84e-73

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: 247.52  E-value: 1.84e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 593 LRKAKFVKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIK 672
Cdd:COG0464 144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 673 GPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAEslDGVYIVAATTRP 752
Cdd:COG0464 224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR--SDVVVIAATNRP 301

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 753 DMIDPALLRpgRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRV 832
Cdd:COG0464 302 DLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPV 379


                .
gi 19075270 833 S 833
Cdd:COG0464 380 T 380
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 614-770 4.07e-64

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: 213.13  E-value: 4.07e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 614 AKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFS 693
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270 694 RAQMAKPCVLFFDEFDSVAPRRGQDS-TGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIF 770
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGdSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 611-770 1.14e-62

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: 208.88  E-value: 1.14e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 611 MQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRD 690
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 691 LFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIF 770
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 607-769 4.54e-60

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: 202.14  E-value: 4.54e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLD 766
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160


                ...
gi 19075270 767 KLI 769
Cdd:cd19503 161 REV 163
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 615-770 1.64e-58

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: 197.35  E-value: 1.64e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 615 KEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSR 694
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270 695 AQMAKPCVLFFDEFDSVAPRRG---QDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIF 770
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 603-835 6.28e-57

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: 209.76  E-value: 6.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   603 IRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIG 682
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   683 KSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRP 762
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRP 334

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075270   763 GRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSIN 835
Cdd:TIGR01243 335 GRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKIN 407
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 615-770 2.75e-56

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: 191.19  E-value: 2.75e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 615 KEAVRDIIESPVKYSLIYKQcRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSR 694
Cdd:cd19527   2 KKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270 695 AQMAKPCVLFFDEFDSVAPRRGQ--DSTGVTDRVVNQILTQMDG-AESLDGVYIVAATTRPDMIDPALLRPGRLDKLIF 770
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNsgDSGGVMDRVVSQLLAELDGmSSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 595-838 1.16e-54

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: 197.89  E-value: 1.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   595 KAKFV---KSSIRWIDIAGMQEAKEAVRDIIE---SPVKYSliykQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQF 668
Cdd:TIGR01241  41 KAKLLneeKPKVTFKDVAGIDEAKEELMEIVDflkNPSKFT----KLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   669 ISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTD---RVVNQILTQMDGAESLDGVYI 745
Cdd:TIGR01241 117 FSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDereQTLNQLLVEMDGFGTNTGVIV 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   746 VAATTRPDMIDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAV 825
Cdd:TIGR01241 197 IAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAA 276

                         250
                  ....*....|...
gi 19075270   826 HKLLKRVSINAVD 838
Cdd:TIGR01241 277 RKNKTEITMNDIE 289
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 600-825 1.33e-52

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 188.89  E-value: 1.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  600 KSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDK 679
Cdd:PRK03992 125 SPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  680 YIGKSEQGVRDLFsraQMAK---PCVLFFDEFDSVAPRRGQDSTGvTDRVVN----QILTQMDGAESLDGVYIVAATTRP 752
Cdd:PRK03992 205 FIGEGARLVRELF---ELARekaPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRI 280

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075270  753 DMIDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAV 825
Cdd:PRK03992 281 DILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
607-825 4.87e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.00  E-value: 4.87e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESpVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:COG1223   3 DVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAqMAKPCVLFFDEFDSVAPRRG-QDSTGVTDRVVNQILTQMDGAESldGVYIVAATTRPDMIDPALLRpgRL 765
Cdd:COG1223  82 NLRKLFDFA-RRAPCVIFFDEFDAIAKDRGdQNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RF 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 766 DKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAV 825
Cdd:COG1223 157 DEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAI 216
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 607-769 6.39e-49

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: 170.98  E-value: 6.39e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19502   4 DIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEGAR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGvTDRVVN----QILTQMDGAESLDGVYIVAATTRPDMIDPALLRP 762
Cdd:cd19502  84 LVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTG-GDREVQrtmlELLNQLDGFDPRGNIKVIMATNRPDILDPALLRP 162


                ....*..
gi 19075270 763 GRLDKLI 769
Cdd:cd19502 163 GRFDRKI 169
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 607-769 2.17e-48

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: 169.15  E-value: 2.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRgQDSTG-VTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRL 765
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGeVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRF 159


                ....
gi 19075270 766 DKLI 769
Cdd:cd19519 160 DREI 163
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 614-771 3.60e-48

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: 168.23  E-value: 3.60e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 614 AKEAVRDIIESPVKYSLIYKQcRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFS 693
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270 694 RAQMAKPCVLFFDEFDSVAPRRG-QDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFC 771
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 603-770 4.58e-48

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: 168.56  E-value: 4.58e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 603 IRWIDIAGMQEAKEAVRDIIE---SPVKYSLIykqcRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDK 679
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEflkNPEKFTKL----GAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 680 YIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTD---RVVNQILTQMDGAESLDGVYIVAATTRPDMID 756
Cdd:cd19501  77 FVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLD 156

                       170
                ....*....|....
gi 19075270 757 PALLRPGRLDKLIF 770
Cdd:cd19501 157 PALLRPGRFDRQVY 170
ftsH CHL00176
cell division protein; Validated
 577-840 2.22e-47

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 179.86  E-value: 2.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  577 NKGLIEKTLKDFVPLQLRKAKFVKSSIRWIDIAGMQEAKEAVRDII---ESPVKYSLIYKqcrlRLPTGILLFGYPGCGK 653
Cdd:CHL00176 154 FKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVsflKKPERFTAVGA----KIPKGVLLVGPPGTGK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  654 TYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGqdsTGV------TDRVV 727
Cdd:CHL00176 230 TLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRG---AGIgggndeREQTL 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  728 NQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFCDLPNEEERLEVLqklanRFHIENAAMLKKLSTL--- 804
Cdd:CHL00176 307 NQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDIL-----KVHARNKKLSPDVSLElia 381

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 19075270  805 --TDGYTYADLSSLLYDAHLIAVHKLLKRVSINAVDPS 840
Cdd:CHL00176 382 rrTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 603-785 3.25e-47

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 176.82  E-value: 3.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   603 IRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTF----------PVQFISIK 672
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLaarigaegggKSYFLNIK 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   673 GPELLDKYIGKSEQGVRDLFSRAQMA----KPCVLFFDEFDSVAPRRGQD-STGVTDRVVNQILTQMDGAESLDGVYIVA 747
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGSGvSSDVETTVVPQLLAEIDGVESLDNVIVIG 338

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 19075270   748 ATTRPDMIDPALLRPGRLDKLIFCDLPNEEERLEVLQK 785
Cdd:TIGR03689 339 ASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAK 376
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 643-773 3.95e-46

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: 161.22  E-value: 3.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   643 ILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGV 722
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19075270   723 TDRVVNQILTQMDGAESLDG-VYIVAATTRPDMIDPALLrpGRLDKLIFCDL 773
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
595-827 3.59e-43

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 166.37  E-value: 3.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 595 KAKFV---KSSIRWIDIAGMQEAKEAVRDIIE---SPVKYSliykqcRL--RLPTGILLFGYPGCGKTYLASAISSTFPV 666
Cdd:COG0465 128 KAKLYdedKPKVTFDDVAGVDEAKEELQEIVDflkDPEKFT------RLgaKIPKGVLLVGPPGTGKTLLAKAVAGEAGV 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 667 QFISIKGPELLDKYIGkseQG---VRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTD---RVVNQILTQMDGAESL 740
Cdd:COG0465 202 PFFSISGSDFVEMFVG---VGasrVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDereQTLNQLLVEMDGFEGN 278

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 741 DGVYIVAATTRPDMIDPALLRPGRLDKLIFCDLPNEEERLEVLqklanRFHIENAAM-----LKKLSTLTDGYTYADLSS 815
Cdd:COG0465 279 EGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAIL-----KVHARKKPLapdvdLEVIARRTPGFSGADLAN 353

                       250
                ....*....|..
gi 19075270 816 LLYDAHLIAVHK 827
Cdd:COG0465 354 LVNEAALLAARR 365
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 600-827 5.55e-43

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 161.47  E-value: 5.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  600 KSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDK 679
Cdd:PTZ00454 139 KPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQK 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  680 YIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGvTDRVVNQI----LTQMDGAESLDGVYIVAATTRPDMI 755
Cdd:PTZ00454 219 YLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTG-ADREVQRIllelLNQMDGFDQTTNVKVIMATNRADTL 297

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075270  756 DPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHK 827
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
607-834 7.64e-43

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 166.36  E-value: 7.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  607 DIAGMQEAKEAVRDIIESpVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTD---RVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPG 763
Cdd:PRK10733 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPG 311

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075270  764 RLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVSI 834
Cdd:PRK10733 312 RFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSM 382
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 607-769 2.94e-41

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 149.09  E-value: 2.94e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMD--GAESLDG--VYIVAATTRPDMIDPALLRP 762
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDelNNEKTAGgpVLVIGATNRPDSLDPALRRA 160


                ....*..
gi 19075270 763 GRLDKLI 769
Cdd:cd19518 161 GRFDREI 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 608-770 5.09e-41

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: 148.27  E-value: 5.09e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 608 IAGMQEAKEAVRDIIESPVKYSLIYKQCRlRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQG 687
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLR-GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 688 VRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAE--SLDGVYIVAATTRPDMIDPALLRpgRL 765
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR--RF 157


                ....*
gi 19075270 766 DKLIF 770
Cdd:cd19509 158 EKRIY 162
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 642-766 1.11e-36

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: 136.08  E-value: 1.11e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 642 GILLFGYPGCGKTYLASAISSTFPVQFISI-KGPELLDKYIGKSEQGVRDLFSRAQMA-KPC-------VLFFDEFDSVA 712
Cdd:cd19504  37 GILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEqRRLgansglhIIIFDEIDAIC 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075270 713 PRRG--QDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLD 766
Cdd:cd19504 117 KQRGsmAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 600-770 2.92e-33

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 126.13  E-value: 2.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 600 KSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRlRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDK 679
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNR-KPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 680 YIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDG-AESLDGVYIVAATTRPDMIDPA 758
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGvGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|..
gi 19075270 759 LLRpgRLDKLIF 770
Cdd:cd19521 160 IRR--RFEKRIY 169
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 607-767 1.78e-31

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 121.08  E-value: 1.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFP-----VQFISIKGPELLDKYI 681
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 682 GKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLR 761
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160


                ....*.
gi 19075270 762 PGRLDK 767
Cdd:cd19517 161 PGRFDR 166
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 599-770 1.82e-31

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: 121.63  E-value: 1.82e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 599 VKSSIRWIDIAGMQEAKEAVRDIIESPVKYSLIYKQCRLRlPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLD 678
Cdd:cd19525  15 HGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 679 KYIGKSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGA--ESLDGVYIVAATTRPDMID 756
Cdd:cd19525  94 KWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEID 173

                       170
                ....*....|....
gi 19075270 757 PALLRpgRLDKLIF 770
Cdd:cd19525 174 EAARR--RLVKRLY 185
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 607-838 2.00e-31

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 128.35  E-value: 2.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  607 DIAGM----QEAKEAVrdiiESPVKYSLIYKQCRLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIG 682
Cdd:PTZ00361 184 DIGGLeqqiQEIKEAV----ELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  683 KSEQGVRDLFSRAQMAKPCVLFFDEFDSVAPRR-GQDSTGVTD--RVVNQILTQMDGAESLDGVYIVAATTRPDMIDPAL 759
Cdd:PTZ00361 260 DGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRyDATSGGEKEiqRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270  760 LRPGRLDKLIFCDLPNEEERLEVLQKLANRFHIENAAMLKKLSTLTDGYTYADLSSLLYDAHLIAVHKllKRVSINAVD 838
Cdd:PTZ00361 340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRE--RRMKVTQAD 416
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 607-765 8.51e-28

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: 110.21  E-value: 8.51e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRL-RLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSE 685
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 686 QGVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAES--LDGVYIVAATTRPDMIDPALLR-- 761
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDEAILRrm 160


                ....
gi 19075270 762 PGRL 765
Cdd:cd19520 161 PKRF 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 607-770 5.97e-27

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: 108.15  E-value: 5.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRlRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTG-VTDRVVNQILTQMDGA-------ESLDGVYIVAATTRPDMIDPA 758
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHeASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEA 159

                       170
                ....*....|..
gi 19075270 759 LLRpgRLDKLIF 770
Cdd:cd19522 160 LRR--RLEKRIY 169
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 607-770 8.81e-27

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: 107.24  E-value: 8.81e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCRlRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTDRVVNQILTQMDGAES--LDGVYIVAATTRPDMIDPALLRpgR 764
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSngDDRVLVMGATNRPQELDDAVLR--R 157


                ....*.
gi 19075270 765 LDKLIF 770
Cdd:cd19524 158 FTKRVY 163
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
 90-164 6.08e-23

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi beta-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


Pssm-ID: 462729  Cd Length: 77  Bit Score: 93.33  E-value: 6.08e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075270    90 EQLEIEPVTSNDWEIAERNAAWLEENLLVQYRVATT-ERFIIYLPSGTFIQFQPLKLIPSSL-CGRLLRTTEVLITP 164
Cdd:pfam09262   1 TTVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPgQILPVWVSGTTVARFRVTSIEPANSpFARLSPDTEVIVAP 77
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 609-773 8.62e-23

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: 95.68  E-value: 8.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 609 AGMQEAKEAVRDIIESPVkysliykqcrlrlPTGILLFGYPGCGKTYLASAI---SSTFPVQFISIKGPELLDKYIGKSE 685
Cdd:cd00009   1 VGQEEAIEALREALELPP-------------PKNLLLYGPPGTGKTTLARAIaneLFRPGAPFLYLNASDLLEGLVVAEL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 686 QG---VRDLFSRAQMAKPCVLFFDEFDSVAPRrgqdstgVTDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRP 762
Cdd:cd00009  68 FGhflVRLLFELAEKAKPGVLFIDEIDSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140

                       170
                ....*....|.
gi 19075270 763 GRLDKLIFCDL 773
Cdd:cd00009 141 DRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 607-761 1.72e-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: 86.48  E-value: 1.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 607 DIAGMQEAKEAVRDIIESPVKYSLIYKQCrLRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQ 686
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075270 687 GVRDLFSRAQMAKPCVLFFDEFDSVAPRRGQDSTGVTdRVVNQILTQMDG--AESLDGVYIVAATTRPDMIDPALLR 761
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGvlGSGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 637-770 2.52e-19

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: 85.88  E-value: 2.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 637 LRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFD---SVAP 713
Cdd:cd19507  28 LPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkgfSNAD 107

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19075270 714 RRGqDStGVTDRVVNQILTQMdgAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIF 770
Cdd:cd19507 108 SKG-DS-GTSSRVLGTFLTWL--QEKKKPVFVVATANNVQSLPPELLRKGRFDEIFF 160
ycf46 CHL00195
Ycf46; Provisional
 637-824 1.31e-16

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 83.92  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  637 LRLPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLDKYIGKSEQGVRDLFSRAQMAKPCVLFFDEFD-SVAPRR 715
Cdd:CHL00195 256 LPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSE 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270  716 GQDSTGVTDRVVNQILTQMdgAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIFCDLPNEEERLEVLQKLANRF---HI 792
Cdd:CHL00195 336 SKGDSGTTNRVLATFITWL--SEKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpkSW 413

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075270  793 ENAAmLKKLSTLTDGYTYADLSSLLYDAHLIA 824
Cdd:CHL00195 414 KKYD-IKKLSKLSNKFSGAEIEQSIIEAMYIA 444
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 640-770 1.05e-12

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 66.63  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270    640 PTGILLFGYPGCGKTYLASAISSTFPVQ---FISIKGPELL--------------DKYIGKSEQGVRDLFSRAQMAKPCV 702
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270    703 LFFDEFDSVAPRRGQDstgvtDRVVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPgRLDKLIF 770
Cdd:smart00382  82 LILDEITSLLDAEQEA-----LLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIV 143
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 375-510 3.33e-11

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: 61.46  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   375 IYINGPKGCGKSNLVHSLFDYYSLNsiyFqMIVSCSEIDRSSFAKFQSFWNNVFIQAERYEPSIIYLDDVHCLISSSNEN 454
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAP---F-IEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270   455 GElgFVEEREIAFLQHQIINLKRK-RKIIFIGFGEEFLTFSEnlvlPLL--FQIKIALP 510
Cdd:pfam00004  77 GD--SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDP----ALLgrFDRIIEFP 129
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 642-770 1.84e-08

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: 54.28  E-value: 1.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 642 GILLFGYPGCGKTYLASAISSTFPVQFISIkgpELLDKyiGKSEQGVRDLFSRAqmAKPCVLFFDEFDS---------VA 712
Cdd:cd19510  25 GYLLYGPPGTGKSSFIAALAGELDYDICDL---NLSEV--VLTDDRLNHLLNTA--PKQSIILLEDIDAafesrehnkKN 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270 713 PRRGQDSTGVTdrvVNQILTQMDGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLIF 770
Cdd:cd19510  98 PSAYGGLSRVT---FSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIY 152
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 643-759 2.87e-07

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: 52.06  E-value: 2.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 643 ILLFGYPGCGKTYLASAISSTFPV---------QFISIKGPELLDKYIGKSEQGVRDLFSRAQ-MAKP-----CVLFfDE 707
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIQeLIDDkdalvFVLI-DE 133

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075270 708 FDSVAPRRGQDSTGV--TD--RVVNQILTQMDGAESLDGVYIVAATTRPDMIDPAL 759
Cdd:cd19508 134 VESLAAARSASSSGTepSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
643-802 9.71e-06

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 49.80  E-value: 9.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 643 ILLFGYPGCGKT----YLASAISST-------FPVqFISIKG-------PELLDKYIGKSEQGVRDLFSRAQMAKPCVLF 704
Cdd:COG5635 183 LLILGEPGSGKTtllrYLALELAERyldaedpIPI-LIELRDlaeeaslEDLLAEALEKRGGEPEDALERLLRNGRLLLL 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 705 FDEFDSVAPRRGQdstgvtDRVVNQILTQmdgAESLDGVYIVaATTRPDMIDPALLRpgRLDKLIFCDLpNEEERLEVLQ 784
Cdd:COG5635 262 LDGLDEVPDEADR------DEVLNQLRRF---LERYPKARVI-ITSRPEGYDSSELE--GFEVLELAPL-SDEQIEEFLK 328

                       170
                ....*....|....*...
gi 19075270 785 KLANRFHIENAAMLKKLS 802
Cdd:COG5635 329 KWFEATERKAERLLEALE 346
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 798-833 2.80e-05

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: 42.14  E-value: 2.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 19075270   798 LKKLSTLTDGYTYADLSSLLYDAHLIAVHKLLKRVS 833
Cdd:pfam17862   4 LEELAERTEGFSGADLEALCREAALAALRRGLEAVT 39
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 642-761 8.89e-05

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: 43.44  E-value: 8.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270   642 GILLFGYPGCGKTYLASAIS------STFPVQFIS------IKGPELLDKYIGKSEQGVrdlFSRAqMAKPCVLFFDEFD 709
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrPVFYVQLTRdtteedLFGRRNIDPGGASWVDGP---LVRA-AREGEIAVLDEIN 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075270   710 SVAPrrgqDSTGVTDRVVN-QILTQMDGAE----SLDGVYIVAATTRPDM----IDPALLR 761
Cdd:pfam07728  77 RANP----DVLNSLLSLLDeRRLLLPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS 133
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 360-485 1.02e-04

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: 43.67  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 360 HEFAQVRNAVFLHQ--NIYINGPKGCGKSNLVHSLFDYYSLNSIYFqMIVSCSEI---DRSSFAKFQSFWNNVFIQAERY 434
Cdd:cd00009   5 EAIEALREALELPPpkNLLLYGPPGTGKTTLARAIANELFRPGAPF-LYLNASDLlegLVVAELFGHFLVRLLFELAEKA 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19075270 435 EPSIIYLDDVHCLISSSNENGELgfveereiaFLQHQIINLKRKRKIIFIG 485
Cdd:cd00009  84 KPGVLFIDEIDSLSRGAQNALLR---------VLETLNDLRIDRENVRVIG 125
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 608-713 4.66e-04

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.16  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 608 IAGMQEAKEAVRDIIespvkysliyKQCRLRL-----PTGILLF-GYPGCGKTYLASAISSTF---PVQFISIKGPELLD 678
Cdd:cd19499  13 VVGQDEAVKAVSDAI----------RRARAGLsdpnrPIGSFLFlGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYME 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 19075270 679 K------------YIGKSEqgvRDLFSRAQMAKP-CVLFFDEFDSVAP 713
Cdd:cd19499  83 KhsvsrligappgYVGYTE---GGQLTEAVRRKPySVVLLDEIEKAHP 127
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 643-707 4.84e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 43.51  E-value: 4.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270 643 ILLFGYPGCGKTYLASAISSTFPVQFISIKGpeLLDkyiGKSEqgVRDLFSRAQMA----KPCVLFFDE 707
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA--VTS---GVKD--IREVIEEARERraygRRTILFVDE 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 608-723 7.83e-04

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: 41.60  E-value: 7.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 608 IAGMQEAKEAVRDIIESPVKYSLIYKQCRLR-LPTGILLFGYPGCGKTYLASAISSTFPVQFISIKGPELLD-KYIGKS- 684
Cdd:cd19498  13 IIGQDEAKRAVAIALRNRWRRMQLPEELRDEvTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGRDv 92

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19075270 685 EQGVRDLFSRaqmakpcVLFFDEFDSVAPRRGQDSTGVT 723
Cdd:cd19498  93 ESIIRDLVEG-------IVFIDEIDKIAKRGGSSGPDVS 124
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 379-485 8.64e-04

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: 40.73  E-value: 8.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 379 GPKGCGKSNLVHSLFDYYSLNSIYfqmiVSCSEIdrssFAKFQSFW----NNVFIQAERYEPSIIYLDDVHCLISSSNEN 454
Cdd:cd19481  33 GPPGTGKTLLAKALAGELGLPLIV----VKLSSL----LSKYVGESeknlRKIFERARRLAPCILFIDEIDAIGRKRDSS 104

                        90       100       110
                ....*....|....*....|....*....|.
gi 19075270 455 GELGFVEEREIAFLQhQIINLKRKRKIIFIG 485
Cdd:cd19481 105 GESGELRRVLNQLLT-ELDGVNSRSKVLVIA 134
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 643-707 1.09e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.38  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075270  643 ILLFGYPGCGKTYLASAISSTFPVQFISIKGPELldkyiGKSEqgVRDLFSRA----QMAKPCVLFFDE 707
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-----GVKD--LREVIEEArqrrSAGRRTILFIDE 100
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 634-769 3.32e-03

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: 39.28  E-value: 3.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075270 634 QCRLRLPTGILLFGYPGCGKTYLAS--AISSTFPVQFISIKgpELLDK-----------YIGKSEQGVRDL---FSRAQM 697
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKslAANSYVPLIRISLN--KLLYNkpdfgnddwidGMLILKESLHRLnlqFELAKA 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075270 698 AKPCVLFF-DEFDSVAPRRGQDSTGVTDRVVNQILTQM---DGAESLDGVYIVAATTRPDMIDPALLRPGRLDKLI 769
Cdd:cd19505  84 MSPCIIWIpNIHELNVNRSTQNLEEDPKLLLGLLLNYLsrdFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCI 159
PRK04195 PRK04195
replication factor C large subunit; Provisional
 607-664 3.56e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.06  E-value: 3.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075270  607 DIAGMQEAKEAVRDIIESpvkysliYKQCRLRLPtgILLFGYPGCGKTYLASAISSTF 664
Cdd:PRK04195  15 DVVGNEKAKEQLREWIES-------WLKGKPKKA--LLLYGPPGVGKTSLAHALANDY 63
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
642-708 4.53e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 4.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075270 642 GILLFGYPGCGKTYLASAISST-----FPVQFISIkgPELLDK-YIGKSEQGVRDLFsrAQMAKPCVLFFDEF 708
Cdd:COG1484 101 NLILLGPPGTGKTHLAIALGHEacragYRVRFTTA--PDLVNElKEARADGRLERLL--KRLAKVDLLILDEL 169
 
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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