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Conserved domains on  [gi|1330208628|ref|WP_102382038|]
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AAA family ATPase [Vibrio breoganii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAA_7 super family cl48144
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 161-198 3.09e-04

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


The actual alignment was detected with superfamily member pfam12775:

Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 41.22  E-value: 3.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1330208628 161 INSGRALLLYGHAGTGKSFVAARILNSLNTSVYVPHAV 198
Cdd:pfam12775  28 LKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFI 65
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 162-352 2.05e-03

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 cd00009:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 151  Bit Score: 38.67  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330208628 162 NSGRALLLYGHAGTGKSFVAARILNSLNTSvyvphavyaagniikvfseqhhkpidsshNREVISLKSHydkrwvlcerp 241
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELFRP-----------------------------GAPFLYLNAS----------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330208628 242 nvqvggELTMDMLEVNHSEHNRIWIAPLQM-IANNGILVIDDLGRQPMPVATLLNRWIvpMEYNYDHLSLPNGQQItipf 320
Cdd:cd00009    57 ------DLLEGLVVAELFGHFLVRLLFELAeKAKPGVLFIDEIDSLSRGAQNALLRVL--ETLNDLRIDRENVRVI---- 124

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1330208628 321 vltmaFSTNLNPQKIADPAFLRRLGYKIQFQP 352
Cdd:cd00009   125 -----GATNRPLLGDLDRALYDRLDIRIVIPL 151
 
Name Accession Description Interval E-value
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 161-198 3.09e-04

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 41.22  E-value: 3.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1330208628 161 INSGRALLLYGHAGTGKSFVAARILNSLNTSVYVPHAV 198
Cdd:pfam12775  28 LKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFI 65
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 162-352 2.05e-03

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: 38.67  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330208628 162 NSGRALLLYGHAGTGKSFVAARILNSLNTSvyvphavyaagniikvfseqhhkpidsshNREVISLKSHydkrwvlcerp 241
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELFRP-----------------------------GAPFLYLNAS----------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330208628 242 nvqvggELTMDMLEVNHSEHNRIWIAPLQM-IANNGILVIDDLGRQPMPVATLLNRWIvpMEYNYDHLSLPNGQQItipf 320
Cdd:cd00009    57 ------DLLEGLVVAELFGHFLVRLLFELAeKAKPGVLFIDEIDSLSRGAQNALLRVL--ETLNDLRIDRENVRVI---- 124

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1330208628 321 vltmaFSTNLNPQKIADPAFLRRLGYKIQFQP 352
Cdd:cd00009   125 -----GATNRPLLGDLDRALYDRLDIRIVIPL 151
PRK08116 PRK08116
hypothetical protein; Validated
 164-188 4.59e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.85  E-value: 4.59e-03
                          10        20
                  ....*....|....*....|....*
gi 1330208628 164 GRALLLYGHAGTGKSFVAARILNSL 188
Cdd:PRK08116  114 NVGLLLWGSVGTGKTYLAACIANEL 138
 
Name Accession Description Interval E-value
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 161-198 3.09e-04

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 41.22  E-value: 3.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1330208628 161 INSGRALLLYGHAGTGKSFVAARILNSLNTSVYVPHAV 198
Cdd:pfam12775  28 LKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFI 65
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 162-352 2.05e-03

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: 38.67  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330208628 162 NSGRALLLYGHAGTGKSFVAARILNSLNTSvyvphavyaagniikvfseqhhkpidsshNREVISLKSHydkrwvlcerp 241
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELFRP-----------------------------GAPFLYLNAS----------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330208628 242 nvqvggELTMDMLEVNHSEHNRIWIAPLQM-IANNGILVIDDLGRQPMPVATLLNRWIvpMEYNYDHLSLPNGQQItipf 320
Cdd:cd00009    57 ------DLLEGLVVAELFGHFLVRLLFELAeKAKPGVLFIDEIDSLSRGAQNALLRVL--ETLNDLRIDRENVRVI---- 124

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1330208628 321 vltmaFSTNLNPQKIADPAFLRRLGYKIQFQP 352
Cdd:cd00009   125 -----GATNRPLLGDLDRALYDRLDIRIVIPL 151
PRK08116 PRK08116
hypothetical protein; Validated
 164-188 4.59e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.85  E-value: 4.59e-03
                          10        20
                  ....*....|....*....|....*
gi 1330208628 164 GRALLLYGHAGTGKSFVAARILNSL 188
Cdd:PRK08116  114 NVGLLLWGSVGTGKTYLAACIANEL 138
 
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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