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Conserved domains on  [gi|763127688|ref|WP_044007579|]
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MoxR family ATPase [Jannaschia sp. CCS1]

Protein Classification

AAA family ATPase( domain architecture ID 11431245)

AAA family ATPase with an AAA (ATPases Associated with various cellular Activities) domain functions as a modulator of stress response pathways and may have a chaperone-like role for the maturation of specific protein complexes or for the insertion of cofactors into proteins; similar to MoxR that is involved in the formation of active methanol dehydrogenase

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 2-261 3.18e-60

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: 192.69  E-value: 3.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   2 RFDGTADYVATQDLTVAVNAAVTLERPLLVKGEPGTGKTELARQVADALGLPIIEWHIKSTTRAQQGLYEYDAVSRLRDs 81
Cdd:COG0714    7 RAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  82 qlgeervhdvgNYIRKGKLWQAfdrkdkcVLLIDEIDKADIEFPNDLLQELDKMEFFVYetGETVKANVRPIVIITSN-- 159
Cdd:COG0714   86 -----------FEFRPGPLFAN-------VLLADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQNpi 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 160 ---NEKELPDAFLRRC-FFHYIRFPDIDVMKKIVEVHHPG-------------------------IKPALLTTALTQFYE 210
Cdd:COG0714  146 eqeGTYPLPEAQLDRFlLKLYIGYPDAEEEREILRRHTGRhlaevepvlspeellalqelvrqvhVSEAVLDYIVDLVRA 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 763127688 211 IREQQGLKKKPSTSEVLDWLKLLLA-------EDLQPEDLRRdgasalpkLHGALLKN 261
Cdd:COG0714  226 TREHPDLRKGPSPRASIALLRAARAlalldgrDYVTPDDVKA--------VAGPVLKH 275
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 2-261 3.18e-60

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: 192.69  E-value: 3.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   2 RFDGTADYVATQDLTVAVNAAVTLERPLLVKGEPGTGKTELARQVADALGLPIIEWHIKSTTRAQQGLYEYDAVSRLRDs 81
Cdd:COG0714    7 RAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  82 qlgeervhdvgNYIRKGKLWQAfdrkdkcVLLIDEIDKADIEFPNDLLQELDKMEFFVYetGETVKANVRPIVIITSN-- 159
Cdd:COG0714   86 -----------FEFRPGPLFAN-------VLLADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQNpi 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 160 ---NEKELPDAFLRRC-FFHYIRFPDIDVMKKIVEVHHPG-------------------------IKPALLTTALTQFYE 210
Cdd:COG0714  146 eqeGTYPLPEAQLDRFlLKLYIGYPDAEEEREILRRHTGRhlaevepvlspeellalqelvrqvhVSEAVLDYIVDLVRA 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 763127688 211 IREQQGLKKKPSTSEVLDWLKLLLA-------EDLQPEDLRRdgasalpkLHGALLKN 261
Cdd:COG0714  226 TREHPDLRKGPSPRASIALLRAARAlalldgrDYVTPDDVKA--------VAGPVLKH 275
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 27-180 4.44e-13

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: 65.25  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  27 RPLLVKGEPGTGKTELARQVADALGLPIIEwhiksttraqqgLYEYDAvSRLRDSQLGEERVHDVGNYIRKGKLwqafDR 106
Cdd:cd00009   20 KNLLLYGPPGTGKTTLARAIANELFRPGAP------------FLYLNA-SDLLEGLVVAELFGHFLVRLLFELA----EK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 763127688 107 KDKCVLLIDEIDKADIEFPNDLLQELDKMEFFVYETGetvkaNVRPIVIITSNNEKELPDAFLRRCFFHyIRFP 180
Cdd:cd00009   83 AKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPLLGDLDRALYDRLDIR-IVIP 150
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 29-180 1.10e-12

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: 63.77  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   29 LLVKGEPGTGKTELARQVADALGLPIIEWhiksttraqqglyeydAVSRLRDSQLGE--ERVHDVGNYIRKgklwqafdr 106
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEI----------------SGSELVSKYVGEseKRLRELFEAAKK--------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  107 KDKCVLLIDEIDK-------ADIEFPNDLLQELdkmeFFVYETGETVKANVrpIVIITSNNEKELPDAFLRRCFFHyIRF 179
Cdd:pfam00004  56 LAPCVIFIDEIDAlagsrgsGGDSESRRVVNQL----LTELDGFTSSNSKV--IVIAATNRPDKLDPALLGRFDRI-IEF 128


                  .
gi 763127688  180 P 180
Cdd:pfam00004 129 P 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-183 8.45e-11

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: 58.92  E-value: 8.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688    27 RPLLVKGEPGTGKTELARQVADALGLPIIEWHIKSTTRAQQGLYEYDAVSRLRDSQLGEERVHDVGNYIRKGKlwqafdR 106
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR------K 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 763127688   107 KDKCVLLIDEIDKADIEFPNDLLQELDkmeffVYETGETVKANVRPIVIITSNNEKELPDAFLRRCFFHYIRFPDID 183
Cdd:smart00382  77 LKPDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
PRK15201 PRK15201
fimbriae biosynthesis transcriptional regulator FimW;
115-263 2.62e-04

fimbriae biosynthesis transcriptional regulator FimW;


Pssm-ID: 185123  Cd Length: 198  Bit Score: 41.18  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 115 DEIDKADIEFpndLLQELDKMEFFVYETGETVKANVRpiVIITSNNEKElpDAFLRRCFF---HYIRFPDID-VMKKIVE 190
Cdd:PRK15201  38 EEIDNADIAF---LALDDDWFSAGCYQIPMHTQHQLR--VIICNKCDKE--KLMFRPCLYmlpHIYREDDVEeITRKMIL 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763127688 191 VHHP-----GIKPALLTTALTQFYEIREQQGLKKKPSTSEVLDWLKLLLAEDLQPEDLRRdgaSALPKLHgalLKNEQ 263
Cdd:PRK15201 111 ILHKralrhSVPSGICHYCTTRHFSVTERHLLKLIASGYHLSETAALLSLSEEQTKSLRR---SIMRKLH---VKTEQ 182
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 2-261 3.18e-60

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: 192.69  E-value: 3.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   2 RFDGTADYVATQDLTVAVNAAVTLERPLLVKGEPGTGKTELARQVADALGLPIIEWHIKSTTRAQQGLYEYDAVSRLRDs 81
Cdd:COG0714    7 RAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  82 qlgeervhdvgNYIRKGKLWQAfdrkdkcVLLIDEIDKADIEFPNDLLQELDKMEFFVYetGETVKANVRPIVIITSN-- 159
Cdd:COG0714   86 -----------FEFRPGPLFAN-------VLLADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQNpi 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 160 ---NEKELPDAFLRRC-FFHYIRFPDIDVMKKIVEVHHPG-------------------------IKPALLTTALTQFYE 210
Cdd:COG0714  146 eqeGTYPLPEAQLDRFlLKLYIGYPDAEEEREILRRHTGRhlaevepvlspeellalqelvrqvhVSEAVLDYIVDLVRA 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 763127688 211 IREQQGLKKKPSTSEVLDWLKLLLA-------EDLQPEDLRRdgasalpkLHGALLKN 261
Cdd:COG0714  226 TREHPDLRKGPSPRASIALLRAARAlalldgrDYVTPDDVKA--------VAGPVLKH 275
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 27-180 4.44e-13

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: 65.25  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  27 RPLLVKGEPGTGKTELARQVADALGLPIIEwhiksttraqqgLYEYDAvSRLRDSQLGEERVHDVGNYIRKGKLwqafDR 106
Cdd:cd00009   20 KNLLLYGPPGTGKTTLARAIANELFRPGAP------------FLYLNA-SDLLEGLVVAELFGHFLVRLLFELA----EK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 763127688 107 KDKCVLLIDEIDKADIEFPNDLLQELDKMEFFVYETGetvkaNVRPIVIITSNNEKELPDAFLRRCFFHyIRFP 180
Cdd:cd00009   83 AKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-----NVRVIGATNRPLLGDLDRALYDRLDIR-IVIP 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 29-192 4.88e-13

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: 68.40  E-value: 4.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  29 LLVKGEPGTGKTELARQVADALGLPiiewhiksttraqqgLYEYDAvSRLRDSQLGE-ERvhdvgnyirkgKLWQAFDR- 106
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGELGLP---------------LIEVDL-SDLVSKYVGEtEK-----------NLREVFDKa 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 107 --KDKCVLLIDEIDK--ADIEFPND---------LLQELDKMEFFVyetgetvkanvrpIVIITSNNEKELPDAFLRRCF 173
Cdd:COG0464  247 rgLAPCVLFIDEADAlaGKRGEVGDgvgrrvvntLLTEMEELRSDV-------------VVIAATNRPDLLDPALLRRFD 313

                        170       180
                 ....*....|....*....|
gi 763127688 174 FH-YIRFPDIDVMKKIVEVH 192
Cdd:COG0464  314 EIiFFPLPDAEERLEIFRIH 333
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 29-180 1.10e-12

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: 63.77  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   29 LLVKGEPGTGKTELARQVADALGLPIIEWhiksttraqqglyeydAVSRLRDSQLGE--ERVHDVGNYIRKgklwqafdr 106
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEI----------------SGSELVSKYVGEseKRLRELFEAAKK--------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  107 KDKCVLLIDEIDK-------ADIEFPNDLLQELdkmeFFVYETGETVKANVrpIVIITSNNEKELPDAFLRRCFFHyIRF 179
Cdd:pfam00004  56 LAPCVIFIDEIDAlagsrgsGGDSESRRVVNQL----LTELDGFTSSNSKV--IVIAATNRPDKLDPALLGRFDRI-IEF 128


                  .
gi 763127688  180 P 180
Cdd:pfam00004 129 P 129
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 27-171 7.13e-11

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: 59.22  E-value: 7.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  27 RPLLVKGEPGTGKTELARQVADALGLPIIewHIKSTTRAQQGLYEydavsrlrdsqlGEERVHDVGNYIRkgklwqafdR 106
Cdd:cd19481   27 KGILLYGPPGTGKTLLAKALAGELGLPLI--VVKLSSLLSKYVGE------------SEKNLRKIFERAR---------R 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 763127688 107 KDKCVLLIDEIDKADIEFP------------NDLLQELDkmeffvyetGETVKANVrpIVIITSNNEKELPDAFLRR 171
Cdd:cd19481   84 LAPCILFIDEIDAIGRKRDssgesgelrrvlNQLLTELD---------GVNSRSKV--LVIAATNRPDLLDPALLRP 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-183 8.45e-11

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: 58.92  E-value: 8.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688    27 RPLLVKGEPGTGKTELARQVADALGLPIIEWHIKSTTRAQQGLYEYDAVSRLRDSQLGEERVHDVGNYIRKGKlwqafdR 106
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR------K 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 763127688   107 KDKCVLLIDEIDKADIEFPNDLLQELDkmeffVYETGETVKANVRPIVIITSNNEKELPDAFLRRCFFHYIRFPDID 183
Cdd:smart00382  77 LKPDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 28-172 1.13e-10

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 58.07  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   28 PLLVKGEPGTGKTELARQVADALG---LPIIEWHiKSTTRAQ-QGLYEYDAV-SRLRDSQLGEErvhdvgnyIRKGklwq 102
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrpVFYVQLT-RDTTEEDlFGRRNIDPGgASWVDGPLVRA--------AREG---- 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763127688  103 afdrkdkCVLLIDEIDKADIEFPNDLLQELDKMEFFVYETGETVKANVRPIVIITSNNE-----KELPDAFLRRC 172
Cdd:pfam07728  68 -------EIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPldrglNELSPALRSRF 135
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
27-190 8.62e-10

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 57.59  E-value: 8.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  27 RPLLVKGEPGTGKTELARQVADALGLPIIEwhIKSTTraqqglyeydavsrLRDSQLGE--ERVHDVgnyirkgklwqaF 104
Cdd:COG1223   36 RKILFYGPPGTGKTMLAEALAGELKLPLLT--VRLDS--------------LIGSYLGEtaRNLRKL------------F 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 105 D--RKDKCVLLIDEID--KADIEFPND----------LLQELDKMeffvyetgetvKANVrpIVIITSNNEKELPDAFLR 170
Cdd:COG1223   88 DfaRRAPCVIFFDEFDaiAKDRGDQNDvgevkrvvnaLLQELDGL-----------PSGS--VVIAATNHPELLDSALWR 154

                        170       180
                 ....*....|....*....|..
gi 763127688 171 RcFFHYIRF--PDIDVMKKIVE 190
Cdd:COG1223  155 R-FDEVIEFplPDKEERKEILE 175
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 30-159 9.94e-10

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 56.43  E-value: 9.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   30 LVKGEPGTGKTELARQVADALGLPIiewhiKSTTRAQqgLYEY---DAVSRLRDSQLGeervhDVGnYIRKGKLWQAFDR 106
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGDE-----RALIRID--MSEYmeeHSVSRLIGAPPG-----YVG-YEEGGQLTEAVRR 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 763127688  107 KDKCVLLIDEIDKADIEFPNDLLQELDKMeffVYETGETVKANVRPIVII-TSN 159
Cdd:pfam07724  74 KPYSIVLIDEIEKAHPGVQNDLLQILEGG---TLTDKQGRTVDFKNTLFImTGN 124
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 36-171 1.74e-09

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 55.65  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  36 GTGKTELARQVADAL-GLPiiewhiKSTTRAQQGLY-EYDAVSRLRDSQLGEervhdVGnYIRKGKLWQAFDRKDKCVLL 113
Cdd:cd19499   51 GVGKTELAKALAELLfGDE------DNLIRIDMSEYmEKHSVSRLIGAPPGY-----VG-YTEGGQLTEAVRRKPYSVVL 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 763127688 114 IDEIDKADIEFPNDLLQELDKMEFfvyETGETVKANVR-PIVIITSNNekeLPDAFLRR 171
Cdd:cd19499  119 LDEIEKAHPDVQNLLLQVLDDGRL---TDSHGRTVDFKnTIIIMTSNH---FRPEFLNR 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 29-192 8.44e-08

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 52.32  E-value: 8.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  29 LLVkGEPGTGKTELARQVADALGLPIIewHIKSttraqqglyeydavSRLRDSQLGE-ER-VHDVGNYIRkgklwqafdR 106
Cdd:COG1222  116 LLY-GPPGTGKTLLAKAVAGELGAPFI--RVRG--------------SELVSKYIGEgARnVREVFELAR---------E 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 107 KDKCVLLIDEID------KADIEFP------NDLLQELDkmeffvyetgeTVKANVRPIVIITSNNEKELPDAFLR--Rc 172
Cdd:COG1222  170 KAPSIIFIDEIDaiaarrTDDGTSGevqrtvNQLLAELD-----------GFESRGDVLIIAATNRPDLLDPALLRpgR- 237

                        170       180
                 ....*....|....*....|..
gi 763127688 173 FFHYIRF--PDIDVMKKIVEVH 192
Cdd:COG1222  238 FDRVIEVplPDEEAREEILKIH 259
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 27-171 8.07e-06

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: 45.09  E-value: 8.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  27 RPLLVKGEPGTGKTELARQVADALGLPIIEWhikSTTRAQQGLyeydavsrlrdSQLGEERVHDVgnyirkgklwqaFD- 105
Cdd:cd19518   35 RGVLLHGPPGCGKTMLANAIAGELKVPFLKI---SATEIVSGV-----------SGESEEKIREL------------FDq 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763127688 106 --RKDKCVLLIDEID---------KADIE--FPNDLLQELDKMEFfvyetgetVKANVRPIVIITSNNEKELPDAFLRR 171
Cdd:cd19518   89 aiSNAPCIVFIDEIDaitpkresaQREMErrIVSQLLTCMDELNN--------EKTAGGPVLVIGATNRPDSLDPALRR 159
PRK15201 PRK15201
fimbriae biosynthesis transcriptional regulator FimW;
115-263 2.62e-04

fimbriae biosynthesis transcriptional regulator FimW;


Pssm-ID: 185123  Cd Length: 198  Bit Score: 41.18  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688 115 DEIDKADIEFpndLLQELDKMEFFVYETGETVKANVRpiVIITSNNEKElpDAFLRRCFF---HYIRFPDID-VMKKIVE 190
Cdd:PRK15201  38 EEIDNADIAF---LALDDDWFSAGCYQIPMHTQHQLR--VIICNKCDKE--KLMFRPCLYmlpHIYREDDVEeITRKMIL 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763127688 191 VHHP-----GIKPALLTTALTQFYEIREQQGLKKKPSTSEVLDWLKLLLAEDLQPEDLRRdgaSALPKLHgalLKNEQ 263
Cdd:PRK15201 111 ILHKralrhSVPSGICHYCTTRHFSVTERHLLKLIASGYHLSETAALLSLSEEQTKSLRR---SIMRKLH---VKTEQ 182
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 8-133 4.72e-04

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: 40.23  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   8 DYVATQDLTVAVNAAVtlerpLLVKGEPGTGKTELARQVADALGLPIIEWhiksttraqqglyeydAVSRLRDSqlGEER 87
Cdd:cd19500   24 EYLAVRKLKGSMKGPI-----LCLVGPPGVGKTSLGKSIARALGRKFVRI----------------SLGGVRDE--AEIR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 763127688  88 VHdvgnyiRK-------GKLWQAFDR--KDKCVLLIDEIDKADIEFPND----LLQELD 133
Cdd:cd19500   81 GH------RRtyvgampGRIIQALKKagTNNPVFLLDEIDKIGSSFRGDpasaLLEVLD 133
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
13-132 5.61e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 40.99  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  13 QDLTVAVNAAVTLERP--LLVKGEPGTGKTELARQVADAL-------GLPI----IEWHIKSTtraqqglyEYDAVSRLR 79
Cdd:COG1474   36 EELASALRPALRGERPsnVLIYGPTGTGKTAVAKYVLEELeeeaeerGVDVrvvyVNCRQAST--------RYRVLSRIL 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 763127688  80 DSQLGEERVHDVGNYIRK--GKLWQAFDRKDKCVLLI-DEIDKADIEFPNDLLQEL 132
Cdd:COG1474  108 EELGSGEDIPSTGLSTDElfDRLYEALDERDGVLVVVlDEIDYLVDDEGDDLLYQL 163
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 30-133 6.92e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 40.98  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688  30 LVKGEPGTGKTELARQVADALGLPIIEWHIKSTTraqqglyEYDAVSRLRDSQLGEervhdVGnYIRKGKLWQAFDRKDK 109
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYM-------ERHTVSRLIGAPPGY-----VG-FDQGGLLTDAVIKHPH 558

                         90       100
                 ....*....|....*....|....
gi 763127688 110 CVLLIDEIDKADIEFPNDLLQELD 133
Cdd:PRK11034 559 AVLLLDEIEKAHPDVFNLLLQVMD 582
AAA_22 pfam13401
AAA domain;
26-132 5.58e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.17  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763127688   26 ERPLLVKGEPGTGKTELARQVADALG------LPIIEWHikSTTRAQqgLYEyDAVSRLRDSQLGEERVHDVGNYIRkgk 99
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPevrdsvVFVDLPS--GTSPKD--LLR-ALLRALGLPLSGRLSKEELLAALQ--- 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 763127688  100 lWQAFDRKDKCVLLIDEIDKadieFPNDLLQEL 132
Cdd:pfam13401  77 -QLLLALAVAVVLIIDEAQH----LSLEALEEL 104
 
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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