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Conserved domains on  [gi|1039009527|gb|ANM59564|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

AAA family ATPase( domain architecture ID 14291541)

AAA family ATPase containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATP-dependent endonuclease or the ATPase component of an ABC-type transporter

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  15037234|18208389|17897320|18466635|16072036|11916378|15037233
SCOP:  2000039

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 715-881 3.45e-83

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19520:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 166  Bit Score: 265.83  E-value: 3.45e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19520      1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIRR 874
Cdd:cd19520     81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRR 159


                   ....*..
gi 1039009527  875 LPRRIYV 881
Cdd:cd19520    160 MPKRFHI 166
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 905-941 5.21e-09

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: 52.54  E-value: 5.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039009527  905 DFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQE 941
Cdd:pfam17862    1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 546-770 4.79e-05

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


The actual alignment was detected with superfamily member COG1401:

Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.07  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  546 KGLTEGFTGRGKSEENEIYKLFTNVMRLHPPKEEDTLRLFKKQLGEDRRIVISRSNINELLKALEEHELLCTDLYQVNTD 625
Cdd:COG1401      9 KFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  626 GVILTKQKAEKAIGWAKNHYLASCPVPLVKGGRLSLPRESLEISIARLRKLEDNSLKPSQNLKNIAKDEYERNFVSAVVA 705
Cdd:COG1401     89 NEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAA 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527  706 PGEIGVKFEDIGALEDVKKALNELVILPMRRPELFARGN---------LLRPCKGILLFGPPGTGKTLLAKALA 770
Cdd:COG1401    169 PEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFeetleaflaALKTKKNVILAGPPGTGKTYLARRLA 242
 
Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 715-881 3.45e-83

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: 265.83  E-value: 3.45e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19520      1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIRR 874
Cdd:cd19520     81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRR 159


                   ....*..
gi 1039009527  875 LPRRIYV 881
Cdd:cd19520    160 MPKRFHI 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 690-972 1.74e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 270.34  E-value: 1.74e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  690 IAKDEYERNFVSAVVAPGeigVKFEDIGALEDVKKALNELVILPMRRPELFAR-GnlLRPCKGILLFGPPGTGKTLLAKA 768
Cdd:COG1222     57 QKRLGTPRGTAVPAESPD---VTFDDIGGLDEQIEEIREAVELPLKNPELFRKyG--IEPPKGVLLYGPPGTGKTLLAKA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  769 LATEAGANFISITGSTLTSKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLR 848
Cdd:COG1222    132 VAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFE 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  849 SKDSqrILILGATNRPFDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNL 926
Cdd:COG1222    212 SRGD--VLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAI 289

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039009527  927 CIAAAYRPVQEllqeeqkgaraeaspGLRSLSLDDFIQSKAKVSPS 972
Cdd:COG1222    290 VTEAGMFAIRE---------------GRDTVTMEDLEKAIEKVKKK 320
cell_div_CdvC NF041006
cell division protein CdvC;
711-990 1.19e-68

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 233.86  E-value: 1.19e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGnllRPcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:NF041006   100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFPLG---WP-RGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLA-----PVIIFVDEIDSLLGARGGSSEHEAtrRMRNEFMAAWDGLRSKDSQ-RILILGATNRP 864
Cdd:NF041006   176 GEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGEV--RVRNQFLKEMDGLQDKSENyHVYVIGATNKP 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  865 FDLDDAVIRRLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQeeqk 944
Cdd:NF041006   254 WRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFE---- 329

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039009527  945 gaRAEASPglRSLSLDDFIQSKAKVSPSV------AYDAttmnelrkWNEQY 990
Cdd:NF041006   330 --KGLGEP--RPITMEDFKEVLKIRKPSVnqemlkAYEA--------WHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 711-991 5.38e-61

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 222.09  E-value: 5.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:TIGR01243  450 VRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGI-RPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDA 870
Cdd:TIGR01243  529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGI--QELSNVVVIAATNRPDILDPA 606

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  871 VIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQ---EEQKG 945
Cdd:TIGR01243  607 LLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGspaKEKLE 686

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039009527  946 ARAEASPGLRSLSLDDFIQSKAKVSPSVA-YDattMNELRKWNEQYG 991
Cdd:TIGR01243  687 VGEEEFLKDLKVEMRHFLEALKKVKPSVSkED---MLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 710-932 1.65e-58

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 206.22  E-value: 1.65e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  710 GVKFEDIGALEDVKKALNELVILPMRRPELFAR-GnlLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSK 788
Cdd:PRK03992   127 NVTYEDIGGLEEQIREVREAVELPLKKPELFEEvG--IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  789 WFGDAEKLTKALFSFATKLAPVIIFVDEIDSlLGAR----GGSSEHEATRRMRnEFMAAWDGLRSKDsqRILILGATNRP 864
Cdd:PRK03992   205 FIGEGARLVRELFELAREKAPSIIFIDEIDA-IAAKrtdsGTSGDREVQRTLM-QLLAEMDGFDPRG--NVKIIAATNRI 280

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  865 FDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAY 932
Cdd:PRK03992   281 DILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGM 350
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 752-883 4.23e-48

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: 167.00  E-value: 4.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHE 831
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039009527  832 ATRRMRNEFMAAWDGLRSKDSqRILILGATNRPFDLDDAVIRRLPRRIYVDL 883
Cdd:pfam00004   80 ESRRVVNQLLTELDGFTSSNS-KVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 750-885 2.64e-17

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: 79.72  E-value: 2.64e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527   750 KGILLFGPPGTGKTLLAKALATEAGAN---FISITGSTLTS--------------KWFGDAEKLTKALFSFATKLAPVII 812
Cdd:smart00382    3 EVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDVL 82

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527   813 FVDEIDSLLGARggsseheaTRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIR-RLPRRIYVDLPD 885
Cdd:smart00382   83 ILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 905-941 5.21e-09

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: 52.54  E-value: 5.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039009527  905 DFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQE 941
Cdd:pfam17862    1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 546-770 4.79e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.07  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  546 KGLTEGFTGRGKSEENEIYKLFTNVMRLHPPKEEDTLRLFKKQLGEDRRIVISRSNINELLKALEEHELLCTDLYQVNTD 625
Cdd:COG1401      9 KFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  626 GVILTKQKAEKAIGWAKNHYLASCPVPLVKGGRLSLPRESLEISIARLRKLEDNSLKPSQNLKNIAKDEYERNFVSAVVA 705
Cdd:COG1401     89 NEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAA 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527  706 PGEIGVKFEDIGALEDVKKALNELVILPMRRPELFARGN---------LLRPCKGILLFGPPGTGKTLLAKALA 770
Cdd:COG1401    169 PEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFeetleaflaALKTKKNVILAGPPGTGKTYLARRLA 242
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 741-773 8.41e-04

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 42.07  E-value: 8.41e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039009527  741 ARGNLLRPCKGILLFGPPGTGKTLLAKALATEA 773
Cdd:NF038214    82 ATLDFIERAENVLLLGPPGTGKTHLAIALGYAA 114
 
Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 715-881 3.45e-83

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: 265.83  E-value: 3.45e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19520      1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIRR 874
Cdd:cd19520     81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRR 159


                   ....*..
gi 1039009527  875 LPRRIYV 881
Cdd:cd19520    160 MPKRFHI 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 690-972 1.74e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 270.34  E-value: 1.74e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  690 IAKDEYERNFVSAVVAPGeigVKFEDIGALEDVKKALNELVILPMRRPELFAR-GnlLRPCKGILLFGPPGTGKTLLAKA 768
Cdd:COG1222     57 QKRLGTPRGTAVPAESPD---VTFDDIGGLDEQIEEIREAVELPLKNPELFRKyG--IEPPKGVLLYGPPGTGKTLLAKA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  769 LATEAGANFISITGSTLTSKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLR 848
Cdd:COG1222    132 VAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFE 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  849 SKDSqrILILGATNRPFDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNL 926
Cdd:COG1222    212 SRGD--VLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAI 289

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039009527  927 CIAAAYRPVQEllqeeqkgaraeaspGLRSLSLDDFIQSKAKVSPS 972
Cdd:COG1222    290 VTEAGMFAIRE---------------GRDTVTMEDLEKAIEKVKKK 320
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 716-881 1.01e-75

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: 245.72  E-value: 1.01e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  716 IGALEDVKKALNELVILPMRRPELFArgNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEK 795
Cdd:cd19509      1 IAGLDDAKEALKEAVILPSLRPDLFP--GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  796 LTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIRRL 875
Cdd:cd19509     79 IVRALFALARELQPSIIFIDEIDSLLSER-GSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRF 157


                   ....*.
gi 1039009527  876 PRRIYV 881
Cdd:cd19509    158 EKRIYI 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 713-933 5.36e-74

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: 249.83  E-value: 5.36e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  713 FEDIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGD 792
Cdd:COG0464    156 LDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  793 AEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHeATRRMRNEFMAAWDGLRSkdsqRILILGATNRPFDLDDAVI 872
Cdd:COG0464    235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEELRS----DVVVIAATNRPDLLDPALL 309

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039009527  873 RRLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYR 933
Cdd:COG0464    310 RRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ 370
cell_div_CdvC NF041006
cell division protein CdvC;
711-990 1.19e-68

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 233.86  E-value: 1.19e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGnllRPcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:NF041006   100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFPLG---WP-RGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLA-----PVIIFVDEIDSLLGARGGSSEHEAtrRMRNEFMAAWDGLRSKDSQ-RILILGATNRP 864
Cdd:NF041006   176 GEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGEV--RVRNQFLKEMDGLQDKSENyHVYVIGATNKP 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  865 FDLDDAVIRRLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQeeqk 944
Cdd:NF041006   254 WRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFE---- 329

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039009527  945 gaRAEASPglRSLSLDDFIQSKAKVSPSV------AYDAttmnelrkWNEQY 990
Cdd:NF041006   330 --KGLGEP--RPITMEDFKEVLKIRKPSVnqemlkAYEA--------WHEKF 369
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 715-881 1.84e-63

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: 212.02  E-value: 1.84e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFArgNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19524      1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIRR 874
Cdd:cd19524     79 KLVRALFAVARELQPSIIFIDEVDSLLSER-SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRR 157


                   ....*..
gi 1039009527  875 LPRRIYV 881
Cdd:cd19524    158 FTKRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 711-991 5.38e-61

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 222.09  E-value: 5.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:TIGR01243  450 VRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGI-RPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDA 870
Cdd:TIGR01243  529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGI--QELSNVVVIAATNRPDILDPA 606

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  871 VIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQ---EEQKG 945
Cdd:TIGR01243  607 LLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGspaKEKLE 686

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039009527  946 ARAEASPGLRSLSLDDFIQSKAKVSPSVA-YDattMNELRKWNEQYG 991
Cdd:TIGR01243  687 VGEEEFLKDLKVEMRHFLEALKKVKPSVSkED---MLRYERLAKELK 730
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 711-881 3.57e-60

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: 203.68  E-value: 3.57e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFArgNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:cd19525     19 INWADIAGLEFAKKTIKEIVVWPMLRPDIFT--GLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDA 870
Cdd:cd19525     97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR-GEGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEA 175

                          170
                   ....*....|.
gi 1039009527  871 VIRRLPRRIYV 881
Cdd:cd19525    176 ARRRLVKRLYI 186
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 710-932 1.65e-58

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 206.22  E-value: 1.65e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  710 GVKFEDIGALEDVKKALNELVILPMRRPELFAR-GnlLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSK 788
Cdd:PRK03992   127 NVTYEDIGGLEEQIREVREAVELPLKKPELFEEvG--IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  789 WFGDAEKLTKALFSFATKLAPVIIFVDEIDSlLGAR----GGSSEHEATRRMRnEFMAAWDGLRSKDsqRILILGATNRP 864
Cdd:PRK03992   205 FIGEGARLVRELFELAREKAPSIIFIDEIDA-IAAKrtdsGTSGDREVQRTLM-QLLAEMDGFDPRG--NVKIIAATNRI 280

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  865 FDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAY 932
Cdd:PRK03992   281 DILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGM 350
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 715-881 7.64e-58

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: 196.36  E-value: 7.64e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFArgNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19522      1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGL-----RSKDSQRILILGATNRPFDLDD 869
Cdd:cd19522     79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVggaseNDDPSKMVMVLAATNFPWDIDE 158

                          170
                   ....*....|..
gi 1039009527  870 AVIRRLPRRIYV 881
Cdd:cd19522    159 ALRRRLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 711-881 4.43e-57

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: 194.31  E-value: 4.43e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGNllRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:cd19521      4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNR--KPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLrSKDSQRILILGATNRPFDLDDA 870
Cdd:cd19521     82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR-GEGESEASRRIKTELLVQMNGV-GNDSQGVLVLGATNIPWQLDSA 159

                          170
                   ....*....|.
gi 1039009527  871 VIRRLPRRIYV 881
Cdd:cd19521    160 IRRRFEKRIYI 170
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 722-881 3.75e-53

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: 182.48  E-value: 3.75e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  722 VKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALF 801
Cdd:cd19511      1 VKRELKEAVEWPLKHPDAFKRLGI-RPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  802 SFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLRSKdsQRILILGATNRPFDLDDAVIR--RLPRRI 879
Cdd:cd19511     80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESL--KGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                   ..
gi 1039009527  880 YV 881
Cdd:cd19511    158 YV 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 711-972 4.33e-53

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: 198.98  E-value: 4.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:TIGR01243  175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGI-EPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSeHEATRRMRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDA 870
Cdd:TIGR01243  254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT-GEVEKRVVAQLLTLMDGL--KGRGRVIVIGATNRPDALDPA 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  871 VIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQEEQKGARA 948
Cdd:TIGR01243  331 LRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKINFEA 410

                          250       260
                   ....*....|....*....|....*...
gi 1039009527  949 EASPG--LRSL--SLDDFIQSKAKVSPS 972
Cdd:TIGR01243  411 EEIPAevLKELkvTMKDFMEALKMVEPS 438
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 722-881 6.70e-49

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: 170.75  E-value: 6.70e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  722 VKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALF 801
Cdd:cd19529      1 VKQELKEAVEWPLLKPEVFKRLGI-RPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  802 SFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDAVIR--RLPRRI 879
Cdd:cd19529     80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL--EEMNGVVVIAATNRPDIIDPALLRagRFDRLI 157


                   ..
gi 1039009527  880 YV 881
Cdd:cd19529    158 YI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 752-883 4.23e-48

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: 167.00  E-value: 4.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHE 831
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039009527  832 ATRRMRNEFMAAWDGLRSKDSqRILILGATNRPFDLDDAVIRRLPRRIYVDL 883
Cdd:pfam00004   80 ESRRVVNQLLTELDGFTSSNS-KVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 722-881 2.22e-47

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: 166.30  E-value: 2.22e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  722 VKKALNELVILPMRRPELFARGNLLRpcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALF 801
Cdd:cd19481      1 LKASLREAVEAPRRGSRLRRYGLGLP--KGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  802 SFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLRSKDsqRILILGATNRPFDLDDAVIR--RLPRRI 879
Cdd:cd19481     79 ERARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRS--KVLVIAATNRPDLLDPALLRpgRFDEVI 156


                   ..
gi 1039009527  880 YV 881
Cdd:cd19481    157 EF 158
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 715-881 8.01e-47

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: 164.77  E-value: 8.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19503      1 DIGGLDEQIASLKELIELPLKYPELFRALGL-KPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLRSKDsqRILILGATNRPFDLDDAVIR- 873
Cdd:cd19503     80 KNLREIFEEARSHAPSIIFIDEIDALAPKR-EEDQREVERRVVAQLLTLMDGMSSRG--KVVVIAATNRPDAIDPALRRp 156


                   ....*....
gi 1039009527  874 -RLPRRIYV 881
Cdd:cd19503    157 gRFDREVEI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
713-930 1.71e-46

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 166.98  E-value: 1.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  713 FEDIGALEDVKKALNELVILPMRRPELfaRGNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGD 792
Cdd:COG1223      1 LDDVVGQEEAKKKLKLIIKELRRRENL--RKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  793 AEKLTKALFSFAtKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFMAAWDGLRSKdsqrILILGATNRPFDLDDAVI 872
Cdd:COG1223     79 TARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSG----SVVIAATNHPELLDSALW 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039009527  873 RRLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAA 930
Cdd:COG1223    154 RRFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
ftsH CHL00176
cell division protein; Validated
 673-931 1.85e-46

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 177.55  E-value: 1.85e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  673 LRKLEDNSLKPSQNLKNIAKDEyernfvSAVVAPGEIGVKFEDIGALEDVKKALNELVILpMRRPELF-ARGNllRPCKG 751
Cdd:CHL00176   148 FQRSSNFKGGPGQNLMNFGKSK------ARFQMEADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFtAVGA--KIPKG 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSL-----LGARGG 826
Cdd:CHL00176   219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVgrqrgAGIGGG 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  827 SSEHEATrrmRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLES 904
Cdd:CHL00176   299 NDEREQT---LNQLLTEMDGF--KGNKGVIVIAATNRVDILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSP 373

                          250       260
                   ....*....|....*....|....*..
gi 1039009527  905 DFQFEKLAKETEGYSGSDLKNLCIAAA 931
Cdd:CHL00176   374 DVSLELIARRTPGFSGADLANLLNEAA 400
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 722-881 1.30e-45

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: 161.14  E-value: 1.30e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  722 VKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALF 801
Cdd:cd19528      1 VKRELQELVQYPVEHPDKFLKFGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  802 SFATKLAPVIIFVDEIDSLLGARGGSSEHE--ATRRMRNEFMAAWDGLRSKdsQRILILGATNRPFDLDDAVIR--RLPR 877
Cdd:cd19528     80 DKARAAAPCVLFFDELDSIAKARGGNIGDAggAADRVINQILTEMDGMNTK--KNVFIIGATNRPDIIDPAILRpgRLDQ 157


                   ....
gi 1039009527  878 RIYV 881
Cdd:cd19528    158 LIYI 161
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 713-881 8.59e-43

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: 153.65  E-value: 8.59e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  713 FEDIGALEDVKKALNELVILPMRRPELFARGNLLRPcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGD 792
Cdd:cd19502      2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  793 AEKLTKALFSFATKLAPVIIFVDEIDSLLGAR---GGSSEHEATRRMRnEFMAAWDGLRSKDsqRILILGATNRPFDLDD 869
Cdd:cd19502     81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTML-ELLNQLDGFDPRG--NIKVIMATNRPDILDP 157

                          170
                   ....*....|....
gi 1039009527  870 AVIR--RLPRRIYV 881
Cdd:cd19502    158 ALLRpgRFDRKIEF 171
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 711-881 4.80e-41

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: 148.53  E-value: 4.80e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILpMRRPELFAR-GNllRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKW 789
Cdd:cd19501      1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKlGA--KIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  790 FGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARG-----GSSEHEATrrmRNEFMAAWDGLRSKDSqrILILGATNRP 864
Cdd:cd19501     78 VGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGaglggGHDEREQT---LNQLLVEMDGFESNTG--VIVIAATNRP 152

                          170
                   ....*....|....*....
gi 1039009527  865 FDLDDAVIR--RLPRRIYV 881
Cdd:cd19501    153 DVLDPALLRpgRFDRQVYV 171
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 715-881 2.49e-40

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: 146.18  E-value: 2.49e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFArgNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19523      1 DIAGLGALKAAIKEEVLWPLLRPDAFS--GLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARggSSEHEATRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIRR 874
Cdd:cd19523     79 KILQASFLAARCRQPSVLFISDLDALLSSQ--DDEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRY 156


                   ....*..
gi 1039009527  875 LPRRIYV 881
Cdd:cd19523    157 FSKRLLV 163
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
703-931 1.15e-39

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 155.97  E-value: 1.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  703 VVAPGEIGVKFEDIGALEDVKKALNELV-ILpmRRPELFARgnlL--RPCKGILLFGPPGTGKTLLAKALATEAGANFIS 779
Cdd:COG0465    131 LYDEDKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTR---LgaKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  780 ITGSTLTSKWFG-------DaekltkaLFSFATKLAPVIIFVDEIDSLLGAR-----GGSSEHEATrrmRNEFMAAWDGL 847
Cdd:COG0465    206 ISGSDFVEMFVGvgasrvrD-------LFEQAKKNAPCIIFIDEIDAVGRQRgaglgGGHDEREQT---LNQLLVEMDGF 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  848 RSKDSqrILILGATNRPFDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKN 925
Cdd:COG0465    276 EGNEG--VIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLAN 353


                   ....*.
gi 1039009527  926 LCIAAA 931
Cdd:COG0465    354 LVNEAA 359
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 715-879 3.51e-39

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: 142.96  E-value: 3.51e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19519      1 DIGGCRKQLAQIREMVELPLRHPELFKAIGI-KPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARgGSSEHEATRRMRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDAVIR- 873
Cdd:cd19519     80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGEVERRIVSQLLTLMDGL--KQRAHVIVMAATNRPNSIDPALRRf 156


                   ....*..
gi 1039009527  874 -RLPRRI 879
Cdd:cd19519    157 gRFDREI 163
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 719-881 4.63e-39

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: 142.63  E-value: 4.63e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  719 LEDVKKALNELVILPMRRPELFARGNLLRPcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTK 798
Cdd:cd19530      1 LDHVREELTMSILRPIKRPDIYKALGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  799 ALFSFATKLAPVIIFVDEIDSLLGARGGsSEHEATRRMRNEFMAAWDGLrsKDSQRILILGATNRPFDLDDAVIR--RLP 876
Cdd:cd19530     80 QVFQRARASAPCVIFFDEVDALVPKRGD-GGSWASERVVNQLLTEMDGL--EERSNVFVIAATNRPDIIDPAMLRpgRLD 156


                   ....*
gi 1039009527  877 RRIYV 881
Cdd:cd19530    157 KTLYV 161
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 705-930 9.65e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 150.31  E-value: 9.65e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  705 APGEigvKFEDIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGST 784
Cdd:PTZ00361   177 APLE---SYADIGGLEQQIQEIKEAVELPLTHPELYDDIGI-KPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  785 LTSKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGAR-----GGssEHEATRRMRnEFMAAWDGLRSKDSQRILIlg 859
Cdd:PTZ00361   253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydatsGG--EKEIQRTML-ELLNQLDGFDSRGDVKVIM-- 327

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039009527  860 ATNRPFDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAA 930
Cdd:PTZ00361   328 ATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEA 400
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
708-994 1.13e-38

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 154.04  E-value: 1.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  708 EIGVKFEDIGALEDVKKALNELVILpMRRPELFARGNLLRPcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTS 787
Cdd:PRK10733   146 QIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVE 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  788 KWFGDAEKLTKALFSFATKLAPVIIFVDEIDSL-----LGARGGSSEHEATrrmRNEFMAAWDGLRSKDSqrILILGATN 862
Cdd:PRK10733   224 MFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVgrqrgAGLGGGHDEREQT---LNQMLVEMDGFEGNEG--IIVIAATN 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  863 RPFDLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLciaaayrpVQELLQ 940
Cdd:PRK10733   299 RPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANL--------VNEAAL 370

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039009527  941 EEQKGARaeaspglRSLSLDDFIQSKAKVSPSVAYDATTMNELRKWNEQYGEGG 994
Cdd:PRK10733   371 FAARGNK-------RVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAG 417
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 722-881 2.53e-35

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: 131.87  E-value: 2.53e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  722 VKKALNELVILPMRRPELFARGnlLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALF 801
Cdd:cd19527      1 VKKEILDTIQLPLEHPELFSSG--LRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  802 SFATKLAPVIIFVDEIDSLLGARGGSSEHEATR-RMRNEFMAAWDGLrSKDSQRILILGATNRPFDLDDAVIR--RLPRR 878
Cdd:cd19527     79 QKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMdRVVSQLLAELDGM-SSSGQDVFVIGATNRPDLLDPALLRpgRFDKL 157


                   ...
gi 1039009527  879 IYV 881
Cdd:cd19527    158 LYL 160
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 715-877 2.55e-34

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: 129.45  E-value: 2.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLLrPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAE 794
Cdd:cd19518      1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  795 KLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEhEATRRMRNEFMAAWDGL--RSKDSQRILILGATNRPFDLDDAvI 872
Cdd:cd19518     80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQR-EMERRIVSQLLTCMDELnnEKTAGGPVLVIGATNRPDSLDPA-L 157


                   ....*
gi 1039009527  873 RRLPR 877
Cdd:cd19518    158 RRAGR 162
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 722-880 5.03e-34

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: 127.93  E-value: 5.03e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  722 VKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDAEKLTKALF 801
Cdd:cd19526      1 VKKALEETIEWPSKYPKIFASSPL-RLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  802 SFATKLAPVIIFVDEIDSLLGARGGSSEHeATRRMRNEFMAAWDGLRSKDSqrILILGATNRPFDLDDAVIR--RLPRRI 879
Cdd:cd19526     80 SRAQSAKPCILFFDEFDSIAPKRGHDSTG-VTDRVVNQLLTQLDGVEGLDG--VYVLAATSRPDLIDPALLRpgRLDKLV 156


                   .
gi 1039009527  880 Y 880
Cdd:cd19526    157 Y 157
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 711-936 1.36e-32

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 131.42  E-value: 1.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWF 790
Cdd:PTZ00454   142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGI-DPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  791 GDAEKLTKALFSFATKLAPVIIFVDEIDSLLGAR-----GGSSEheaTRRMRNEFMAAWDGLRSKDSQRILIlgATNRPF 865
Cdd:PTZ00454   221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaqtGADRE---VQRILLELLNQMDGFDQTTNVKVIM--ATNRAD 295

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039009527  866 DLDDAVIR--RLPRRIYVDLPDAENRLKILKIFLTPENLESDFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQ 936
Cdd:PTZ00454   296 TLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVR 368
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 715-880 4.35e-32

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 123.00  E-value: 4.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALNELVILPMRRPELFARGNLlRPCKGILLFGPPGTGKTLLAKALATEA--GANFISI---TGSTLTSKW 789
Cdd:cd19517      1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKI-TPPRGVLFHGPPGTGKTLMARALAAECskGGQKVSFfmrKGADCLSKW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  790 FGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARggSSEHEATR-RMRNEFMAAWDGLRSKDsqRILILGATNRPFDLD 868
Cdd:cd19517     80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR--SSKQEQIHaSIVSTLLALMDGLDNRG--QVVVIGATNRPDALD 155

                          170
                   ....*....|....
gi 1039009527  869 DAVIR--RLPRRIY 880
Cdd:cd19517    156 PALRRpgRFDREFY 169
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 750-883 3.27e-21

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: 91.05  E-value: 3.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  750 KGILLFGPPGTGKTLLAKALATEA---GANFISITGSTLTSKWFGDAEK---LTKALFSFATKLAPVIIFVDEIDSLlga 823
Cdd:cd00009     20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDSL--- 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039009527  824 rgGSSEHEATRRMRNEFMaawdgLRSKDSQRILILGATNRPF--DLDDAVIRRLPRRIYVDL 883
Cdd:cd00009     97 --SRGAQNALLRVLETLN-----DLRIDRENVRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 750-885 2.64e-17

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: 79.72  E-value: 2.64e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527   750 KGILLFGPPGTGKTLLAKALATEAGAN---FISITGSTLTS--------------KWFGDAEKLTKALFSFATKLAPVII 812
Cdd:smart00382    3 EVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDVL 82

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527   813 FVDEIDSLLGARggsseheaTRRMRNEFMAAWDGLRSKDSQRILILGATNRPFDLDDAVIR-RLPRRIYVDLPD 885
Cdd:smart00382   83 ILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 715-841 2.61e-16

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: 77.41  E-value: 2.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  715 DIGALEDVKKALnelvilpMRRPELF---ARGNLLRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFG 791
Cdd:cd19507      1 DVGGLDNLKDWL-------KKRKAAFskqASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039009527  792 DAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFM 841
Cdd:cd19507     74 ESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFL 123
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 749-881 5.95e-16

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: 76.76  E-value: 5.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  749 CKGILLFGPPGTGKTLLAKALATEAGANFISI-TGSTLTSKWFGDAEKLTKALFSFAT----KLAP-----VIIFvDEID 818
Cdd:cd19504     35 VKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEeeqrRLGAnsglhIIIF-DEID 113

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039009527  819 SLLGARG----GSSEHEAtrrMRNEFMAAWDGLRSKDSqrILILGATNRPFDLDDAVIRrlPRRIYV 881
Cdd:cd19504    114 AICKQRGsmagSTGVHDT---VVNQLLSKIDGVEQLNN--ILVIGMTNRKDLIDEALLR--PGRLEV 173
ycf46 CHL00195
Ycf46; Provisional
 711-932 3.90e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.21  E-value: 3.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  711 VKFEDIGALEDVKKALNelvilpmRRPELFARG----NLLRPcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLT 786
Cdd:CHL00195   225 EKISDIGGLDNLKDWLK-------KRSTSFSKQasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  787 SKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEATRRMRNEFmAAWdgLRSKDSQRILILGATNrpFD 866
Cdd:CHL00195   297 GGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVLATF-ITW--LSEKKSPVFVVATANN--ID 371

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039009527  867 -LDDAVIR--RLPRRIYVDLPDAENRLKILKIFLT---PENLESdFQFEKLAKETEGYSGSDLKNLCIAAAY 932
Cdd:CHL00195   372 lLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQkfrPKSWKK-YDIKKLSKLSNKFSGAEIEQSIIEAMY 442
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 748-875 6.34e-14

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 70.25  E-value: 6.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  748 PCKGILLFGPPGTGKTLLAKALATEAGANFISITGstltskwfGD-----AEKLTK--ALFSFA-TKLAPVIIFVDEIDS 819
Cdd:cd19512     21 LYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTG--------GDvapmgREGVTAihKVFDWAnTSRRGLLLFVDEADA 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039009527  820 LLGARGGSSEHEATRRMRNEFMaawdgLRSKD-SQRILILGATNRPFDLDDAVIRRL 875
Cdd:cd19512     93 FLRKRSTEKISEDLRAALNAFL-----YRTGEqSNKFMLVLASNQPEQFDWAINDRI 144
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 744-881 5.47e-13

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: 68.63  E-value: 5.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  744 NLLRPCKGILLFGPPGTGKTLLAKALA---------TEAGANFISITGSTLTSKWFGDAEKLTKALFSFATKL-----AP 809
Cdd:cd19508     47 NLITWNRLVLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddkdAL 126

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039009527  810 VIIFVDEIDSLLGARGG-SSEHEATRRMR--NEFMAAWDGLRSKDSqrILILGATNRPFDLDDAVIRRLPRRIYV 881
Cdd:cd19508    127 VFVLIDEVESLAAARSAsSSGTEPSDAIRvvNAVLTQIDRIKRYHN--NVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 721-868 2.62e-12

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 65.63  E-value: 2.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  721 DVKKALNELVILPMRRPELFARGNLLrpcKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFGDA--EKLTK 798
Cdd:cd19506      1 DVRQLLTLYGILPLGSQAVHEKAPLV---KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLH 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039009527  799 ALFSFATKLAPVIIFVDEIDSLLGARGGSSEHEAT-RRMRNEFMAAWDGLRSKDsqRILILGATNRPFDLD 868
Cdd:cd19506     78 LVLKVARQLQPSVIWIGDAEKTFYKKVPKTEKQLDpKRLKKDLPKILKSLKPED--RVLIVGTTSRPFEAD 146
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 750-881 2.16e-09

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: 56.98  E-value: 2.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  750 KGILLFGPPGTGKTLLAKALATEAGANF--ISITGSTLTSkwfgdaeKLTKALFSFATKLApvIIFVDEIDSLLGARggs 827
Cdd:cd19510     24 RGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVLTD-------DRLNHLLNTAPKQS--IILLEDIDAAFESR--- 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039009527  828 sEHEATRRMRNEFMA---------AWDGLRSKDsQRILILgATNRPFDLDDAVIR--RLPRRIYV 881
Cdd:cd19510     92 -EHNKKNPSAYGGLSrvtfsgllnALDGVASSE-ERIVFM-TTNHIERLDPALIRpgRVDMKIYM 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 905-941 5.21e-09

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: 52.54  E-value: 5.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039009527  905 DFQFEKLAKETEGYSGSDLKNLCIAAAYRPVQELLQE 941
Cdd:pfam17862    1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 739-894 2.66e-08

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 56.33  E-value: 2.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  739 LFARGNLLrpckgilLFGPPGTGKTLLAKALATEAGANFI-----------SITGSTLTSKWFGDaekltkalFSFatKL 807
Cdd:COG0714     28 LLAGGHLL-------LEGVPGVGKTTLAKALARALGLPFIriqftpdllpsDILGTYIYDQQTGE--------FEF--RP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  808 APV---IIFVDEID--------SLLGARggsSEHE-----ATRRMRNEFMaawdglrskdsqrilILGATNRP-----FD 866
Cdd:COG0714     91 GPLfanVLLADEINrappktqsALLEAM---EERQvtipgGTYKLPEPFL---------------VIATQNPIeqegtYP 152

                          170       180
                   ....*....|....*....|....*...
gi 1039009527  867 LDDAVIRRLPRRIYVDLPDAENRLKILK 894
Cdd:COG0714    153 LPEAQLDRFLLKLYIGYPDAEEEREILR 180
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 752-821 7.49e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 55.86  E-value: 7.49e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKwfgDAEKLTKALFSFATKLAPVIIFVDEI--------DSLL 821
Cdd:PRK13342    39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTSGVK---DLREVIEEARQRRSAGRRTILFIDEIhrfnkaqqDALL 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 750-834 4.82e-07

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: 51.23  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  750 KGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFgdaekLTKALFSFATKLAPVIIFVDEIDSlLGARGGSSE 829
Cdd:cd19498     47 KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGY-----VGRDVESIIRDLVEGIVFIDEIDK-IAKRGGSSG 120


                   ....*
gi 1039009527  830 HEATR 834
Cdd:cd19498    121 PDVSR 125
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 752-823 9.53e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 52.37  E-value: 9.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISItgSTLTSkwfGDAE-----KLTKALFSFATKlapVIIFVDEI--------D 818
Cdd:COG2256     52 MILWGPPGTGKTTLARLIANATDAEFVAL--SAVTS---GVKDireviEEARERRAYGRR---TILFVDEIhrfnkaqqD 123


                   ....*
gi 1039009527  819 SLLGA 823
Cdd:COG2256    124 ALLPH 128
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
750-800 1.14e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 52.28  E-value: 1.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039009527  750 KGILLFGPPGTGKTLLAKALATEAGAN--FISITGSTLTSKWFGDAEKLTKAL 800
Cdd:COG1224     65 KGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEFLMQAL 117
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 752-846 2.43e-06

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 47.50  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGAN-----FISItgstltskwfgdAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGG 826
Cdd:cd01120      1 ILITGPPGSGKTTLLLQFAEQALLSdepviFISF------------LDTILEAIEDLIEEKKLDIIIIDSLSSLARASQG 68

                           90       100
                   ....*....|....*....|
gi 1039009527  827 SSEHEATRRMRNEFMAAWDG 846
Cdd:cd01120     69 DRSSELLEDLAKLLRAARNT 88
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 752-817 3.38e-06

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 47.88  E-value: 3.38e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKwfGDaekltkaLFSFATKLAPV-IIFVDEI 817
Cdd:pfam05496   36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP--GD-------LAAILTNLEPGdVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
752-820 6.26e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.36  E-value: 6.26e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKwfGDaekltkaLFSFATKLAPV-IIFVDEIDSL 820
Cdd:PRK00080    54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GD-------LAAILTNLEEGdVLFIDEIHRL 114
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 750-800 1.11e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 48.84  E-value: 1.11e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039009527  750 KGILLFGPPGTGKTLLAKALATEAGAN--FISITGSTLTSKWFGDAEKLTKAL 800
Cdd:pfam06068   51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEALTQAF 103
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 746-881 2.88e-05

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: 45.44  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  746 LRPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKWFG---------------DAEKLTkALFSFATKLAPV 810
Cdd:cd19505      9 LSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPDfgnddwidgmlilkeSLHRLN-LQFELAKAMSPC 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039009527  811 IIFVDEIDSL----LGARGGSSEHEATRRMRNEFMaawDGLRSKDSQRILILGATNRPFDLDDAVI--RRLPRRIYV 881
Cdd:cd19505     88 IIWIPNIHELnvnrSTQNLEEDPKLLLGLLLNYLS---RDFEKSSTRNILVIASTHIPQKVDPALIapNRLDTCINI 161
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 546-770 4.79e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.07  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  546 KGLTEGFTGRGKSEENEIYKLFTNVMRLHPPKEEDTLRLFKKQLGEDRRIVISRSNINELLKALEEHELLCTDLYQVNTD 625
Cdd:COG1401      9 KFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  626 GVILTKQKAEKAIGWAKNHYLASCPVPLVKGGRLSLPRESLEISIARLRKLEDNSLKPSQNLKNIAKDEYERNFVSAVVA 705
Cdd:COG1401     89 NEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAA 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527  706 PGEIGVKFEDIGALEDVKKALNELVILPMRRPELFARGN---------LLRPCKGILLFGPPGTGKTLLAKALA 770
Cdd:COG1401    169 PEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFeetleaflaALKTKKNVILAGPPGTGKTYLARRLA 242
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
741-773 5.50e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.93  E-value: 5.50e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039009527  741 ARGNLLRPCKGILLFGPPGTGKTLLAKALATEA 773
Cdd:COG1484     91 ATLDFIERGENLILLGPPGTGKTHLAIALGHEA 123
PRK04195 PRK04195
replication factor C large subunit; Provisional
 747-829 1.59e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 45.30  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  747 RPCKGILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKwfGDAEK------LTKALFSFATKLapviIFVDEIDSL 820
Cdd:PRK04195    37 KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQRTA--DVIERvageaaTSGSLFGARRKL----ILLDEVDGI 110

                           90
                   ....*....|.
gi 1039009527  821 LGA--RGGSSE 829
Cdd:PRK04195   111 HGNedRGGARA 121
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 752-817 1.75e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 45.07  E-value: 1.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLtskwfgdaEKlTKALFSFATKLAPV-IIFVDEI 817
Cdd:COG2255     57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI--------EK-PGDLAAILTNLEEGdVLFIDEI 114
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 714-961 6.29e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 43.68  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  714 EDIGaLEDVK---KALNELVILPMRRPElfaRG-NLLRPCKGILLFGPPGTGKTLLAKALATE-AG------ANFISITG 782
Cdd:TIGR03922  277 EQIG-LERVKrqvAALKSSTAMALARAE---RGlPVAQTSNHMLFAGPPGTGKTTIARVVAKIyCGlgvlrkPLVREVSR 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  783 STLTSKWFGDAEKLTKALFSFATKlapVIIFVDEIDSLLGARGGSseheatrrmRNEF-MAAWDGLRSK---DSQRILIL 858
Cdd:TIGR03922  353 ADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGYGQ---------KDPFgLEAIDTLLARmenDRDRLVVI 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  859 GA-----TNRPFDLDDAVIRRLPRRIYVDLPDAENRLKILKIFLTPEnlESDFQ----------FEKLAK-ETEGYSGSD 922
Cdd:TIGR03922  421 GAgyrkdLDKFLEVNEGLRSRFTRVIEFPSYSPDELVEIARRMATER--DSVLDdaaadalleaATTLAQdTTPDANGDL 498

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1039009527  923 LKNLCIAAAYRPVQELLQ--EEQKGARAEASPGLRSLSLDD 961
Cdd:TIGR03922  499 RRGLDIAGNGRFVRNVVEraEEERDFRLDHSDRLDAVTVDD 539
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
752-780 7.21e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.44  E-value: 7.21e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISI 780
Cdd:COG0645      2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 752-818 7.44e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 43.11  E-value: 7.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALA---------------TEAG----------------ANFisitgstltskwfgDAEKLTKAl 800
Cdd:COG1219    112 ILLIGPTGSGKTLLAQTLArildvpfaiadattlTEAGyvgedvenillkllqaADY--------------DVEKAERG- 176

                           90
                   ....*....|....*...
gi 1039009527  801 fsfatklapvIIFVDEID 818
Cdd:COG1219    177 ----------IIYIDEID 184
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 741-773 8.41e-04

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 42.07  E-value: 8.41e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039009527  741 ARGNLLRPCKGILLFGPPGTGKTLLAKALATEA 773
Cdd:NF038214    82 ATLDFIERAENVLLLGPPGTGKTHLAIALGYAA 114
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 752-820 8.46e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 42.67  E-value: 8.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLTSKwfGDaekLTKALfsfaTKLAP-VIIFVDEIDSL 820
Cdd:TIGR00635   33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GD---LAAIL----TNLEEgDVLFIDEIHRL 93
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 752-771 9.33e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.11  E-value: 9.33e-04
                           10        20
                   ....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALAT 771
Cdd:COG0606    214 LLMIGPPGSGKTMLARRLPG 233
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
752-818 1.00e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.84  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALA---------------TEAG----------------ANFisitgstltskwfgDAEKLTKAl 800
Cdd:PRK05342   111 ILLIGPTGSGKTLLAQTLArildvpfaiadattlTEAGyvgedvenillkllqaADY--------------DVEKAQRG- 175

                           90
                   ....*....|....*...
gi 1039009527  801 fsfatklapvIIFVDEID 818
Cdd:PRK05342   176 ----------IVYIDEID 183
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 719-780 1.52e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 40.62  E-value: 1.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527  719 LEDVKKalnelvilpmRRPELFARGNLLRPCKG-ILLF-GPPGTGKTLLAKALATEAGANFISI 780
Cdd:cd19500     15 LEDVKE----------RILEYLAVRKLKGSMKGpILCLvGPPGVGKTSLGKSIARALGRKFVRI 68
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 752-771 2.45e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.21  E-value: 2.45e-03
                           10        20
                   ....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALAT 771
Cdd:pfam01078   25 LLMIGPPGSGKTMLAKRLPG 44
44 PHA02544
clamp loader, small subunit; Provisional
 752-783 2.52e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 41.13  E-value: 2.52e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039009527  752 ILLFGP-PGTGKTLLAKALATEAGANFISITGS 783
Cdd:PHA02544    45 MLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGS 77
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 752-816 3.88e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.16  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANF--ISITGSTLTSKWF--------------GDAEKLTKALFSFATKLA----PVI 811
Cdd:COG3267     46 VVLTGEVGTGKTTLLRRLLERLPDDVkvAYIPNPQLSPAELlraiadelglepkgASKADLLRQLQEFLLELAaagrRVV 125


                   ....*
gi 1039009527  812 IFVDE 816
Cdd:COG3267    126 LIIDE 130
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 752-818 4.62e-03

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 39.10  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAG---ANFISITGSTLTSKW--------------FGDAEKLTKALfsfaTKLAPVIIFV 814
Cdd:pfam07724    6 FLFLGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMEEHsvsrligappgyvgYEEGGQLTEAV----RRKPYSIVLI 81


                   ....
gi 1039009527  815 DEID 818
Cdd:pfam07724   82 DEIE 85
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 752-878 4.70e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 38.44  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFIS-------ITGSTLTSK-WFGDAEKLTKA-LFSFATKLA----PVII---FVD 815
Cdd:pfam13671    2 ILLVGLPGSGKSTLARRLLEELGAVRLSsdderkrLFGEGRPSIsYYTDATDRTYErLHELARIALragrPVILdatNLR 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039009527  816 EiDSLLGARGGSSEHEATRRMRnEFMAAWDGLRSKDSQRiliLGATNRPFDLDDAVIRRLPRR 878
Cdd:pfam13671   82 R-DERARLLALAREYGVPVRIV-VFEAPEEVLRERLAAR---ARAGGDPSDVPEEVLDRQKAR 139
PRK13341 PRK13341
AAA family ATPase;
738-780 5.57e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 5.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039009527  738 ELFARGNLLRpcKGI--------LLFGPPGTGKTLLAKALATEAGANFISI 780
Cdd:PRK13341    35 HILGEGRLLR--RAIkadrvgslILYGPPGVGKTTLARIIANHTRAHFSSL 83
AAA_22 pfam13401
AAA domain;
752-820 6.09e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  752 ILLFGPPGTGKTLLAKALA---TEAGANFISITGSTLTS-----KWF-------GDAEKLTKALFSF------ATKLAPV 810
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVDLPSGTSpkdllRALlralglpLSGRLSKEELLAAlqqlllALAVAVV 87

                           90
                   ....*....|
gi 1039009527  811 IIfVDEIDSL 820
Cdd:pfam13401   88 LI-IDEAQHL 96
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 752-790 7.64e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.81  E-value: 7.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGST----LTSKWF 790
Cdd:pfam00910    1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSVysrnPDDDFW 43
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 690-893 7.75e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 40.21  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  690 IAKDEYERNFVSAVVAPGEIGVKFEDigALEDVKKALNELV----ILPM--RRPELFARGNLL--RPCKGILLFGPPGTG 761
Cdd:PRK11034   142 TRKDEPSQSSDPGSQPNSEEQAGGEE--RMENFTTNLNQLArvggIDPLigREKELERAIQVLcrRRKNNPLLVGESGVG 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039009527  762 KTLLAKALA--------TEAGANFISIT---GSTLT-SKWFGDAEKLTKALFSFATKLAPVIIFVDEIDSLLGARGGSSE 829
Cdd:PRK11034   220 KTAIAEGLAwrivqgdvPEVMADCTIYSldiGSLLAgTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGG 299

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039009527  830 HEATRRMRNEFMAawdglrskdSQRILILGAT-----NRPFDLDDAVIRRLpRRIYVDLPDAENRLKIL 893
Cdd:PRK11034   300 QVDAANLIKPLLS---------SGKIRVIGSTtyqefSNIFEKDRALARRF-QKIDITEPSIEETVQII 358
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 752-818 9.92e-03

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 39.12  E-value: 9.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039009527  752 ILLFGPPGTGKTLLAKALATEAGANFISITGSTLT-SKWFG-DAEK-----LTKALFSFAtKLAPVIIFVDEID 818
Cdd:cd19497     53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGeDVENillklLQAADYDVE-RAQRGIVYIDEID 125
 
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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