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Conserved domains on  [gi|490285979|ref|WP_004181771|]
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MULTISPECIES: AAA family ATPase [Enterobacteriaceae]

Protein Classification

ATP-binding protein( domain architecture ID 10543770)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain similar to Escherichia coli protein YehL

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
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 103-243 1.58e-32

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: 118.16  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  103 GICLQGESGSGKTELALYISHML-NWPITIKQINNELSIDDLEGMRTLENGNTRYVYSDLVQGYRDGHIILLDEIDKINP 181
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490285979  182 DTAAKLHMPLERKPWATGkEGGELIYANRY-TRFIGTANTNMSGEdmrfassQSQDSAFIKRF 243
Cdd:pfam07728  81 DVLNSLLSLLDERRLLLP-DGGELVKAAPDgFRLIATMNPLDRGL-------NELSPALRSRF 135
 
Name Accession Description Interval E-value
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 103-243 1.58e-32

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: 118.16  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  103 GICLQGESGSGKTELALYISHML-NWPITIKQINNELSIDDLEGMRTLENGNTRYVYSDLVQGYRDGHIILLDEIDKINP 181
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490285979  182 DTAAKLHMPLERKPWATGkEGGELIYANRY-TRFIGTANTNMSGEdmrfassQSQDSAFIKRF 243
Cdd:pfam07728  81 DVLNSLLSLLDERRLLLP-DGGELVKAAPDgFRLIATMNPLDRGL-------NELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 88-228 2.17e-06

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: 46.76  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  88 LRRMVKLLLNNEVTAGICLQGESGSGKTELALYISHMLNWP------ITIKQINNELSIDDLEGMRTLENGNTRYVysdl 161
Cdd:cd00009    6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgapflyLNASDLLEGLVVAELFGHFLVRLLFELAE---- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490285979 162 vqgYRDGHIILLDEIDKINPDTAAKLHMPLErkpwatgkEGGELIYANRYTRFIGTANTNMSGEDMR 228
Cdd:cd00009   82 ---KAKPGVLFIDEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDR 137
PHA02244 PHA02244
ATPase-like protein
 106-243 3.90e-06

ATPase-like protein


Pssm-ID: 107157 [Multi-domain]  Cd Length: 383  Bit Score: 48.19  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979 106 LQGESGSGKTELALYISHMLNWPITIKQinnelSIDDLEGMRTLENGNTRYVYSDLVQGYRDGHIILLDEIDKINPDTAA 185
Cdd:PHA02244 124 LKGGAGSGKNHIAEQIAEALDLDFYFMN-----AIMDEFELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALI 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490285979 186 KLHMPLERKPWatgKEGGELIYANRYTRFIGTANTNMSGEDMRFASSQSQDSAFIKRF 243
Cdd:PHA02244 199 IINSAIANKFF---DFADERVTAHEDFRVISAGNTLGKGADHIYVARNKIDGATLDRF 253
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 104-219 1.36e-04

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: 41.59  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979   104 ICLQGESGSGKTELALYISHMLNWP-ITIKQINNELSIDDLEGMRTLENGNTRYVYSDLVQGYRDGH---------IILL 173
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALalarklkpdVLIL 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 490285979   174 DEIDKINPDTAAKLHMPLERKPWATGKEGGELIyanrytRFIGTAN 219
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEELRLLLLLKSEKNL------TVILTTN 124
HprK COG1493
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ...
 103-119 4.65e-03

Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms];


Pssm-ID: 441102 [Multi-domain]  Cd Length: 142  Bit Score: 37.08  E-value: 4.65e-03
                         10
                 ....*....|....*..
gi 490285979 103 GICLQGESGSGKTELAL 119
Cdd:COG1493   13 GVLITGPSGSGKSELAL 29
 
Name Accession Description Interval E-value
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 103-243 1.58e-32

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: 118.16  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  103 GICLQGESGSGKTELALYISHML-NWPITIKQINNELSIDDLEGMRTLENGNTRYVYSDLVQGYRDGHIILLDEIDKINP 181
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490285979  182 DTAAKLHMPLERKPWATGkEGGELIYANRY-TRFIGTANTNMSGEdmrfassQSQDSAFIKRF 243
Cdd:pfam07728  81 DVLNSLLSLLDERRLLLP-DGGELVKAAPDgFRLIATMNPLDRGL-------NELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 88-228 2.17e-06

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: 46.76  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  88 LRRMVKLLLNNEVTAGICLQGESGSGKTELALYISHMLNWP------ITIKQINNELSIDDLEGMRTLENGNTRYVysdl 161
Cdd:cd00009    6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgapflyLNASDLLEGLVVAELFGHFLVRLLFELAE---- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490285979 162 vqgYRDGHIILLDEIDKINPDTAAKLHMPLErkpwatgkEGGELIYANRYTRFIGTANTNMSGEDMR 228
Cdd:cd00009   82 ---KAKPGVLFIDEIDSLSRGAQNALLRVLE--------TLNDLRIDRENVRVIGATNRPLLGDLDR 137
PHA02244 PHA02244
ATPase-like protein
 106-243 3.90e-06

ATPase-like protein


Pssm-ID: 107157 [Multi-domain]  Cd Length: 383  Bit Score: 48.19  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979 106 LQGESGSGKTELALYISHMLNWPITIKQinnelSIDDLEGMRTLENGNTRYVYSDLVQGYRDGHIILLDEIDKINPDTAA 185
Cdd:PHA02244 124 LKGGAGSGKNHIAEQIAEALDLDFYFMN-----AIMDEFELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALI 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490285979 186 KLHMPLERKPWatgKEGGELIYANRYTRFIGTANTNMSGEDMRFASSQSQDSAFIKRF 243
Cdd:PHA02244 199 IINSAIANKFF---DFADERVTAHEDFRVISAGNTLGKGADHIYVARNKIDGATLDRF 253
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 104-219 1.36e-04

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: 41.59  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979   104 ICLQGESGSGKTELALYISHMLNWP-ITIKQINNELSIDDLEGMRTLENGNTRYVYSDLVQGYRDGH---------IILL 173
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALalarklkpdVLIL 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 490285979   174 DEIDKINPDTAAKLHMPLERKPWATGKEGGELIyanrytRFIGTAN 219
Cdd:smart00382  85 DEITSLLDAEQEALLLLLEELRLLLLLKSEKNL------TVILTTN 124
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 88-182 2.86e-03

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: 38.03  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  88 LRRMVKLLLNNEVTAGICLQGESGSGKTELALYISHMLNWPITIkqinneLSIDDLEGMRTLENG-NTRYVYSDLVQgyR 166
Cdd:cd19481   13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIV------VKLSSLLSKYVGESEkNLRKIFERARR--L 84

                         90
                 ....*....|....*.
gi 490285979 167 DGHIILLDEIDKINPD 182
Cdd:cd19481   85 APCILFIDEIDAIGRK 100
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 73-179 3.02e-03

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: 38.24  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490285979  73 FRAPLNSKYRPNPITLRRMVKLLlnnevtAGICLQGESGSGKTELALYISHMLNW--PitiKQINNELSIDDLEGMrtlE 150
Cdd:cd19504   13 FRRAFASRVFPPEIVEQLGCKHV------KGILLYGPPGTGKTLMARQIGKMLNAreP---KIVNGPEILNKYVGE---S 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490285979 151 NGNTRYVYSDLVQGYRDG------HIILLDEIDKI 179
Cdd:cd19504   81 EANIRKLFADAEEEQRRLgansglHIIIFDEIDAI 115
HprK COG1493
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ...
 103-119 4.65e-03

Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms];


Pssm-ID: 441102 [Multi-domain]  Cd Length: 142  Bit Score: 37.08  E-value: 4.65e-03
                         10
                 ....*....|....*..
gi 490285979 103 GICLQGESGSGKTELAL 119
Cdd:COG1493   13 GVLITGPSGSGKSELAL 29
 
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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