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Conserved domains on  [gi|375134669|ref|YP_004995319|]
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MoxR-like ATPase [Acinetobacter pittii PHEA-2]

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
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 ...
1-267 7.27e-65

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: 204.63  E-value: 7.27e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   1 MSADTQHFTGTDQYIATDSLKLAVKAARALQKPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLYEYDAV 80
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  81 SRlrdsqlgddrvyDIKNYIKPGKLWeaftseeRCVLLIDEIDKADIEFPNDLLHELDKMSFYVYetNETITATQRPIVI 160
Cdd:COG0714   81 QQ------------TGEFEFRPGPLF-------ANVLLADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 161 ITSN-----NEKELPDAFLRRC-FFHYIEFPDEATMREIIAVHFPN-------------------------ISATLVNEA 209
Cdd:COG0714  140 ATQNpieqeGTYPLPEAQLDRFlLKLYIGYPDAEEEREILRRHTGRhlaevepvlspeellalqelvrqvhVSEAVLDYI 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 210 LQVFFKLREIPNLKKPPSTSELIDWLSLLMADDMpedvLRNRD--TSKAIPPLYGALIKN 267
Cdd:COG0714  220 VDLVRATREHPDLRKGPSPRASIALLRAARALAL----LDGRDyvTPDDVKAVAGPVLKH 275
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
1-267 7.27e-65

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: 204.63  E-value: 7.27e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   1 MSADTQHFTGTDQYIATDSLKLAVKAARALQKPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLYEYDAV 80
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  81 SRlrdsqlgddrvyDIKNYIKPGKLWeaftseeRCVLLIDEIDKADIEFPNDLLHELDKMSFYVYetNETITATQRPIVI 160
Cdd:COG0714   81 QQ------------TGEFEFRPGPLF-------ANVLLADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 161 ITSN-----NEKELPDAFLRRC-FFHYIEFPDEATMREIIAVHFPN-------------------------ISATLVNEA 209
Cdd:COG0714  140 ATQNpieqeGTYPLPEAQLDRFlLKLYIGYPDAEEEREILRRHTGRhlaevepvlspeellalqelvrqvhVSEAVLDYI 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 210 LQVFFKLREIPNLKKPPSTSELIDWLSLLMADDMpedvLRNRD--TSKAIPPLYGALIKN 267
Cdd:COG0714  220 VDLVRATREHPDLRKGPSPRASIALLRAARALAL----LDGRDyvTPDDVKAVAGPVLKH 275
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
21-185 1.42e-12

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: 64.09  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  21 KLAVKAARALQKPLLIKGEPGTGKTLLAEQVAQSLGlklitwhiksttKAQQGLYEYDAvSRLRdsqlGDDRVYDIKNYI 100
Cdd:cd00009    9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELF------------RPGAPFLYLNA-SDLL----EGLVVAELFGHF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 101 KPGKLWEAFTSEERCVLLIDEIDKADIEFPNDLLHELDKMSFYVYETNETItatqrpIVIITSNNEKELPDAFLRRCFFH 180
Cdd:cd00009   72 LVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR------VIGATNRPLLGDLDRALYDRLDI 145

                 ....*
gi 375134669 181 YIEFP 185
Cdd:cd00009  146 RIVIP 150
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
34-185 2.50e-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: 62.61  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   34 LLIKGEPGTGKTLLAEQVAQSLGLKLITWhiksttkaqqglyeydAVSRLRDSQLGDdrvydiknyiKPGKLWEAFTSEE 113
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEI----------------SGSELVSKYVGE----------SEKRLRELFEAAK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  114 R---CVLLIDEIDK-------ADIEFPND----LLHELDKMSfyvyetnetiTATQRPIVIITSNNEKELPDAFLRRCFF 179
Cdd:pfam00004  55 KlapCVIFIDEIDAlagsrgsGGDSESRRvvnqLLTELDGFT----------SSNSKVIVIAATNRPDKLDPALLGRFDR 124

                  ....*.
gi 375134669  180 HyIEFP 185
Cdd:pfam00004 125 I-IEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
32-186 4.21e-09

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: 54.30  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669    32 KPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLYEYDAVSRLRDSQLGDDRVYDIKNYIkpgklweAFTS 111
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL-------ALAR 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134669   112 EER-CVLLIDEIDKADiefpnDLLHELDKMSFYVYETNETITATQRPIVIITSNNEKELPDAFLRRCFFHYIEFPD 186
Cdd:smart00382  76 KLKpDVLILDEITSLL-----DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLL 146
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
25-206 2.04e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 42.71  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  25 KAARALQKPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLyeydAVSRLRDsqlgddrvydiknyikpgk 104
Cdd:PRK10733 179 KLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV----GASRVRD------------------- 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 105 LWEAFTSEERCVLLIDEIDKADIEFP--------------NDLLHELDKmsfyvYETNETItatqrpIVIITSNNEKELP 170
Cdd:PRK10733 236 MFEQAKKAAPCIIFIDEIDAVGRQRGaglggghdereqtlNQMLVEMDG-----FEGNEGI------IVIAATNRPDVLD 304
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 375134669 171 DAFLRRCFFH---YIEFPDEATMREIIAVHF------PNISATLV 206
Cdd:PRK10733 305 PALLRPGRFDrqvVVGLPDVRGREQILKVHMrrvplaPDIDAAII 349
 
Name Accession Description Interval E-value
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
1-267 7.27e-65

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: 204.63  E-value: 7.27e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   1 MSADTQHFTGTDQYIATDSLKLAVKAARALQKPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLYEYDAV 80
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  81 SRlrdsqlgddrvyDIKNYIKPGKLWeaftseeRCVLLIDEIDKADIEFPNDLLHELDKMSFYVYetNETITATQRPIVI 160
Cdd:COG0714   81 QQ------------TGEFEFRPGPLF-------ANVLLADEINRAPPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 161 ITSN-----NEKELPDAFLRRC-FFHYIEFPDEATMREIIAVHFPN-------------------------ISATLVNEA 209
Cdd:COG0714  140 ATQNpieqeGTYPLPEAQLDRFlLKLYIGYPDAEEEREILRRHTGRhlaevepvlspeellalqelvrqvhVSEAVLDYI 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 210 LQVFFKLREIPNLKKPPSTSELIDWLSLLMADDMpedvLRNRD--TSKAIPPLYGALIKN 267
Cdd:COG0714  220 VDLVRATREHPDLRKGPSPRASIALLRAARALAL----LDGRDyvTPDDVKAVAGPVLKH 275
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
34-201 1.40e-12

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: 67.24  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  34 LLIKGEPGTGKTLLAEQVAQSLGLKLItwHIKsttkaqqglyeydaVSRLRDSQLGDdrvydiknyiKPGKLWEAFT--- 110
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGELGLPLI--EVD--------------LSDLVSKYVGE----------TEKNLREVFDkar 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 111 SEERCVLLIDEIDK--ADIEFPND---------LLHELDKMSFYVyetnetitatqrpIVIITSNNEKELPDAFLRRcFF 179
Cdd:COG0464  248 GLAPCVLFIDEADAlaGKRGEVGDgvgrrvvntLLTEMEELRSDV-------------VVIAATNRPDLLDPALLRR-FD 313
                        170       180
                 ....*....|....*....|....
gi 375134669 180 HYIEF--PDEATMREIIAVHFPNI 201
Cdd:COG0464  314 EIIFFplPDAEERLEIFRIHLRKR 337
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
21-185 1.42e-12

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: 64.09  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  21 KLAVKAARALQKPLLIKGEPGTGKTLLAEQVAQSLGlklitwhiksttKAQQGLYEYDAvSRLRdsqlGDDRVYDIKNYI 100
Cdd:cd00009    9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELF------------RPGAPFLYLNA-SDLL----EGLVVAELFGHF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 101 KPGKLWEAFTSEERCVLLIDEIDKADIEFPNDLLHELDKMSFYVYETNETItatqrpIVIITSNNEKELPDAFLRRCFFH 180
Cdd:cd00009   72 LVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR------VIGATNRPLLGDLDRALYDRLDI 145

                 ....*
gi 375134669 181 YIEFP 185
Cdd:cd00009  146 RIVIP 150
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
34-185 2.50e-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: 62.61  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   34 LLIKGEPGTGKTLLAEQVAQSLGLKLITWhiksttkaqqglyeydAVSRLRDSQLGDdrvydiknyiKPGKLWEAFTSEE 113
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEI----------------SGSELVSKYVGE----------SEKRLRELFEAAK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  114 R---CVLLIDEIDK-------ADIEFPND----LLHELDKMSfyvyetnetiTATQRPIVIITSNNEKELPDAFLRRCFF 179
Cdd:pfam00004  55 KlapCVIFIDEIDAlagsrgsGGDSESRRvvnqLLTELDGFT----------SSNSKVIVIAATNRPDKLDPALLGRFDR 124

                  ....*.
gi 375134669  180 HyIEFP 185
Cdd:pfam00004 125 I-IEFP 129
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
34-195 1.15e-10

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 60.28  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  34 LLIKGEPGTGKTLLAEQVAQSLGLKLITwhIKSTTKAQQglYEYDAVSRLRdsqlgddrvydiknyikpgKLWEaFTSEE 113
Cdd:COG1223   38 ILFYGPPGTGKTMLAEALAGELKLPLLT--VRLDSLIGS--YLGETARNLR-------------------KLFD-FARRA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 114 RCVLLIDEID--KADIEFPND----------LLHELDKMSFYVyetnetitatqrpIVIITSNNEKELPDAFLRRcFFHY 181
Cdd:COG1223   94 PCVIFFDEFDaiAKDRGDQNDvgevkrvvnaLLQELDGLPSGS-------------VVIAATNHPELLDSALWRR-FDEV 159
                        170
                 ....*....|....*.
gi 375134669 182 IEF--PDEATMREIIA 195
Cdd:COG1223  160 IEFplPDKEERKEILE 175
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
16-176 6.05e-10

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: 56.91  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  16 ATDSLKLAVKAARA----------LQKPLLIKGEPGTGKTLLAEQVAQSLGLKLItwHIKSTTKAQQGLYEYDAvsrlrd 85
Cdd:cd19481    1 LKASLREAVEAPRRgsrlrryglgLPKGILLYGPPGTGKTLLAKALAGELGLPLI--VVKLSSLLSKYVGESEK------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  86 sqlgddrvydiknyiKPGKLWEAFTSEERCVLLIDEIDKADIEFP------------NDLLHELDKmsfyvYETNETIta 153
Cdd:cd19481   73 ---------------NLRKIFERARRLAPCILFIDEIDAIGRKRDssgesgelrrvlNQLLTELDG-----VNSRSKV-- 130
                        170       180
                 ....*....|....*....|...
gi 375134669 154 tqrpIVIITSNNEKELPDAFLRR 176
Cdd:cd19481  131 ----LVIAATNRPDLLDPALLRP 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
32-186 4.21e-09

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: 54.30  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669    32 KPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLYEYDAVSRLRDSQLGDDRVYDIKNYIkpgklweAFTS 111
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL-------ALAR 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134669   112 EER-CVLLIDEIDKADiefpnDLLHELDKMSFYVYETNETITATQRPIVIITSNNEKELPDAFLRRCFFHYIEFPD 186
Cdd:smart00382  76 KLKpDVLILDEITSLL-----DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLL 146
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
33-177 1.76e-08

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: 51.91  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   33 PLLIKGEPGTGKTLLAEQVA-----QSLGLKLITwhiKSTTKAQ-QGLYEYDAvsrlrdsqLGDDRVydiknyikPGKLW 106
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnRPVFYVQLT---RDTTEEDlFGRRNIDP--------GGASWV--------DGPLV 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134669  107 EAFTseERCVLLIDEIDKADIEFPNDLLHELDKMSFYVYETNETITATQRPIVIITSNNE-----KELPDAFLRRC 177
Cdd:pfam07728  62 RAAR--EGEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPldrglNELSPALRSRF 135
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
38-197 1.48e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 51.93  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  38 GEPGTGKTLLAEQVAQSLGLKLItwhiksttkaqqglyeydavsRLRDSQLgddrvydIKNYIKPG-----KLWEAFTSE 112
Cdd:COG1222  119 GPPGTGKTLLAKAVAGELGAPFI---------------------RVRGSEL-------VSKYIGEGarnvrEVFELAREK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 113 ERCVLLIDEID------KADIEFP------NDLLHELDKmsfyvYETNETItatqrpIVIITSNNEKELPDAFLR--RcF 178
Cdd:COG1222  171 APSIIFIDEIDaiaarrTDDGTSGevqrtvNQLLAELDG-----FESRGDV------LIIAATNRPDLLDPALLRpgR-F 238
                        170       180
                 ....*....|....*....|.
gi 375134669 179 FHYIEF--PDEATMREIIAVH 197
Cdd:COG1222  239 DRVIEVplPDEEAREEILKIH 259
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
23-176 6.99e-06

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: 45.63  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  23 AVKAARA-LQKP------LLIKGEPGTGKTLLAEQVAQSL---GLKLITwhiksttkAQQGLY-EYDAVSRLRDSQLGdd 91
Cdd:cd19499   26 AIRRARAgLSDPnrpigsFLFLGPTGVGKTELAKALAELLfgdEDNLIR--------IDMSEYmEKHSVSRLIGAPPG-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  92 rvydIKNYIKPGKLWEAFTSEERCVLLIDEIDKADIEFPNDLLHELDkmsfyvyetNETITATQ-------RPIVIITSN 164
Cdd:cd19499   96 ----YVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLD---------DGRLTDSHgrtvdfkNTIIIMTSN 162
                        170
                 ....*....|..
gi 375134669 165 NekeLPDAFLRR 176
Cdd:cd19499  163 H---FRPEFLNR 171
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
35-139 9.16e-06

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: 44.88  E-value: 9.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669   35 LIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQqglyEYDAVSRLRDSQLGDdrvydiKNYIKPGKLWEAFTSEER 114
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYM----EEHSVSRLIGAPPGY------VGYEEGGQLTEAVRRKPY 76
                          90       100
                  ....*....|....*....|....*
gi 375134669  115 CVLLIDEIDKADIEFPNDLLHELDK 139
Cdd:pfam07724  77 SIVLIDEIEKAHPGVQNDLLQILEG 101
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
31-176 3.27e-05

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: 43.18  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  31 QKPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGlyeydavsrlrDSQLGDDRVYDIKNYIKPgklweaft 110
Cdd:cd19520   35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYG-----------ESQKLVAAVFSLASKLQP-------- 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 111 seerCVLLIDEIDK-ADIEFPNDllHELDKM---SFYVYETNETITATQRPIVIITSNNEKELPDAFLRR 176
Cdd:cd19520   96 ----SIIFIDEIDSfLRQRSSTD--HEATAMmkaEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRR 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
32-123 7.43e-05

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: 42.28  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  32 KPLLIKGEPGTGKTLLAEQVAQSLGLKLITwhIKSttKAQQGLYEYDAVSRLRdsqlgddrvydiknyikpgKLWEAFTS 111
Cdd:cd19503   35 RGVLLHGPPGTGKTLLARAVANEAGANFLS--ISG--PSIVSKYLGESEKNLR-------------------EIFEEARS 91
                         90
                 ....*....|..
gi 375134669 112 EERCVLLIDEID 123
Cdd:cd19503   92 HAPSIIFIDEID 103
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
25-206 2.04e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 42.71  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  25 KAARALQKPLLIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTKAQQGLyeydAVSRLRDsqlgddrvydiknyikpgk 104
Cdd:PRK10733 179 KLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV----GASRVRD------------------- 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669 105 LWEAFTSEERCVLLIDEIDKADIEFP--------------NDLLHELDKmsfyvYETNETItatqrpIVIITSNNEKELP 170
Cdd:PRK10733 236 MFEQAKKAAPCIIFIDEIDAVGRQRGaglggghdereqtlNQMLVEMDG-----FEGNEGI------IVIAATNRPDVLD 304
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 375134669 171 DAFLRRCFFH---YIEFPDEATMREIIAVHF------PNISATLV 206
Cdd:PRK10733 305 PALLRPGRFDrqvVVGLPDVRGREQILKVHMrrvplaPDIDAAII 349
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
12-122 2.96e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  12 DQYI----ATDSLKLAVKAARALQKPL---LIKGEPGTGKTLLAEQVAQSLGLKlitwhIKSTtkaqQG-LYEydavsrl 83
Cdd:PRK00080  25 DEFIgqekVKENLKIFIEAAKKRGEALdhvLLYGPPGLGKTTLANIIANEMGVN-----IRIT----SGpALE------- 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 375134669  84 rdsqlgddrvydiknyiKPGKLWEAFTS-EERCVLLIDEI 122
Cdd:PRK00080  89 -----------------KPGDLAAILTNlEEGDVLFIDEI 111
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
10-156 3.12e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.13  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  10 GTDQyiATDSLKLAVKAARA----LQKPL---LIKGEPGTGKTLLAEQVAQSLGLKLITWHIKSTTkaqqglyEYDAVSR 82
Cdd:PRK11034 462 GQDK--AIEALTEAIKMSRAglghEHKPVgsfLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYM-------ERHTVSR 532
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  83 LRDSQLGddrvydIKNYIKPGKLWEAFTSEERCVLLIDEIDKADIEFPNDLLHELD----------KMSF----YVYETN 148
Cdd:PRK11034 533 LIGAPPG------YVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDngtltdnngrKADFrnvvLVMTTN 606

                 ....*...
gi 375134669 149 ETITATQR 156
Cdd:PRK11034 607 AGVRETER 614
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
25-54 9.81e-04

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 40.27  E-value: 9.81e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 375134669  25 KAARALQK--PLLIKGEPGTGKTLLAEQVAQS 54
Cdd:COG3284  336 RARRLADRdiPVLILGETGTGKELFARAIHAA 367
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
23-45 2.52e-03

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 38.38  E-value: 2.52e-03
                         10        20
                 ....*....|....*....|....
gi 375134669  23 AVKAAraLQKPL-LIKGEPGTGKT 45
Cdd:cd18039    9 AVKTA--LQRPLsLIQGPPGTGKT 30
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
24-58 2.54e-03

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: 38.83  E-value: 2.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 375134669   24 VKAARALQKPLLIKGEPGTGKTLLAEQVAQSLGLK 58
Cdd:pfam06068  43 IKEGKIAGRAVLIAGPPGTGKTALAIAISKELGED 77
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
34-137 2.71e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 38.68  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  34 LLIKGEPGTGKTLLA-------EQVAQSLGLKLITWHI---KSTTkaqqglyEYDAVSRLRDsQLGD-----------DR 92
Cdd:COG1474   54 VLIYGPTGTGKTAVAkyvleelEEEAEERGVDVRVVYVncrQAST-------RYRVLSRILE-ELGSgedipstglstDE 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 375134669  93 VYDiknyikpgKLWEAFTSEERCVLLI-DEIDKADIEFPNDLLHEL 137
Cdd:COG1474  126 LFD--------RLYEALDERDGVLVVVlDEIDYLVDDEGDDLLYQL 163
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
34-86 2.96e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 37.49  E-value: 2.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 375134669  34 LLIKGEPGTGKTLLAEQVAQSLGLKLItwHIKSTTKaQQGLY-EYDAvsrLRDS 86
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVI--HLNDLVK-EEGLYtEVDE---ERDS 50
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
38-122 4.82e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.14  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134669  38 GEPGTGKTLLAEQVAQSLGLKlitwhiksttkaqqgLYEYDAVSrlrdsqlgdDRVYDIKNYIKPGKlwEAFTSEERCVL 117
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAP---------------FEALSAVT---------SGVKDLREVIEEAR--QRRSAGRRTIL 96

                 ....*
gi 375134669 118 LIDEI 122
Cdd:PRK13342  97 FIDEI 101
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
30-61 8.23e-03

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: 36.25  E-value: 8.23e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 375134669  30 LQKPLLIKGEPGTGKTLLAEQVAQSLGLKLIT 61
Cdd:cd19526   26 LRSGILLYGPPGCGKTLLASAIASECGLNFIS 57
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
16-49 9.16e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 37.39  E-value: 9.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 375134669  16 ATDSLKLAVKAARA--------LqkPLLIKGEPGTGKTLLAE 49
Cdd:COG1221  109 ANGSLKNAIEQAKAailyppkgL--HTLILGPTGVGKSFFAE 148
 
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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