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Conserved domains on  [gi|2154925|emb|CAB06071|]
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axonemal dynein heavy chain, partial [Mus musculus]

Protein Classification

ATP-binding protein( domain architecture ID 1000883)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain may function as an ATPase; similar to dynein heavy chain, hydrolytic ATP-binding dynein motor region

Gene Ontology:  GO:0005524
PubMed:  15037234|18208389|16828312|18466635

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAA_6 super family cl37597
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
 2-205 5.73e-147

Hydrolytic ATP binding site of 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 first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.


The actual alignment was detected with superfamily member pfam12774:

Pssm-ID: 463697 [Multi-domain]  Cd Length: 327  Bit Score: 411.49  E-value: 5.73e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925      2 VITPLTDRCYITLAQALGMNMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDE 81
Cdd:pfam12774  13 VITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKGLAQCGAWGCFDE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925     82 FNRIELPVLSVAAQQINIVLTARRERTKQFIFsDGDCVDLNPEFGIFLTMNPGYAGRQELPENLKIQFRTVAMMVPDRQI 161
Cdd:pfam12774  93 FNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFRPVAMMVPDYAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2154925    162 IMRVKLASCGFLENVILAQKFYVLYKLCEEQLTKQVHYDFGLRA 205
Cdd:pfam12774 172 IAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRA 215
 
Name Accession Description Interval E-value
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
 2-205 5.73e-147

Hydrolytic ATP binding site of 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 first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.


Pssm-ID: 463697 [Multi-domain]  Cd Length: 327  Bit Score: 411.49  E-value: 5.73e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925      2 VITPLTDRCYITLAQALGMNMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDE 81
Cdd:pfam12774  13 VITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKGLAQCGAWGCFDE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925     82 FNRIELPVLSVAAQQINIVLTARRERTKQFIFsDGDCVDLNPEFGIFLTMNPGYAGRQELPENLKIQFRTVAMMVPDRQI 161
Cdd:pfam12774  93 FNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFRPVAMMVPDYAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2154925    162 IMRVKLASCGFLENVILAQKFYVLYKLCEEQLTKQVHYDFGLRA 205
Cdd:pfam12774 172 IAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRA 215
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
30-169 1.79e-10

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 59.62  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925    30 AGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSGSWGcFDEFNRIELPVLSVAAqqiNIVLTARRERT- 108
Cdd:COG5245  952 VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILV---DEYLNSDEFRMl 1019

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2154925   109 KQFIFSDGDCVDLNPEFGIFLTMNPgyagRQELPENLKIQFRTVAMMVPDRQII-MRVKLAS 169
Cdd:COG5245 1020 EELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKsRRESLDR 1077
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 28-113 7.59e-04

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: 7.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925   28 GPAGTGKTETTKDMGRCL---GKYVVVFNCSD---QMDFRGL-----GRIFKGLAQSGSWGC--FDEFNRIELPVLSVAA 94
Cdd:cd00009  26 GPPGTGKTTLARAIANELfrpGAPFLYLNASDlleGLVVAELfghflVRLLFELAEKAKPGVlfIDEIDSLSRGAQNALL 105

                        90
                ....*....|....*....
gi 2154925   95 QQINIVLTARRERTKQFIF 113
Cdd:cd00009 106 RVLETLNDLRIDRENVRVI 124
 
Name Accession Description Interval E-value
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
 2-205 5.73e-147

Hydrolytic ATP binding site of 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 first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.


Pssm-ID: 463697 [Multi-domain]  Cd Length: 327  Bit Score: 411.49  E-value: 5.73e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925      2 VITPLTDRCYITLAQALGMNMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDE 81
Cdd:pfam12774  13 VITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKGLAQCGAWGCFDE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925     82 FNRIELPVLSVAAQQINIVLTARRERTKQFIFsDGDCVDLNPEFGIFLTMNPGYAGRQELPENLKIQFRTVAMMVPDRQI 161
Cdd:pfam12774  93 FNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFRPVAMMVPDYAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2154925    162 IMRVKLASCGFLENVILAQKFYVLYKLCEEQLTKQVHYDFGLRA 205
Cdd:pfam12774 172 IAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRA 215
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
30-169 1.79e-10

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 59.62  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925    30 AGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSGSWGcFDEFNRIELPVLSVAAqqiNIVLTARRERT- 108
Cdd:COG5245  952 VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILV---DEYLNSDEFRMl 1019

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2154925   109 KQFIFSDGDCVDLNPEFGIFLTMNPgyagRQELPENLKIQFRTVAMMVPDRQII-MRVKLAS 169
Cdd:COG5245 1020 EELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKsRRESLDR 1077
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
28-205 3.92e-08

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 52.68  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925    28 GPAGTGKTETTKDMG-RCLGKYVVVFNCSDQMdfRGLGRIFKGLAQsGSWGCFDEFNRIELPVLSVAAQQINIVltarRE 106
Cdd:COG5245 1616 GACNPGTDEGRVKYYeRFIRKPVFVFCCYPEL--ASLRNIYEAVLM-GSYLCFDEFNRLSEETMSASVELYLSS----KD 1688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925   107 RTKqfifsdgdcvdlnpefgIFLTMNPGYAGRqELPENLkIQFRTVAMMVPDRQIIMRVKLASCGflenvILAQKFYVLY 186
Cdd:COG5245 1689 KTK-----------------FFLQMNYGYKPR-ELTRSL-RAIFGYAETRIDTPDVSLIIDWYCE-----AIREKIDRLV 1744

                        170
                 ....*....|....*....
gi 2154925   187 KLCEEQLTKQVHYDFGLRA 205
Cdd:COG5245 1745 QQKESSTSRQDLYDFGLRA 1763
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 28-149 1.11e-06

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: 46.13  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925     28 GPAGTGKTETTKDMGRCLGKY-VVVFNCSDQM---DFRGlGRIFKGL------------AQSGSWGCFDEFNRIELPVLs 91
Cdd:pfam07728   6 GPPGTGKTELAERLAAALSNRpVFYVQLTRDTteeDLFG-RRNIDPGgaswvdgplvraAREGEIAVLDEINRANPDVL- 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2154925     92 vaaqqiNIVLTARRERTKQFIFSDGDCVDLNPEFGIFLTMNPGYAGRQELPENLKIQF 149
Cdd:pfam07728  84 ------NSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPLDRGLNELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 28-113 7.59e-04

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: 7.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2154925   28 GPAGTGKTETTKDMGRCL---GKYVVVFNCSD---QMDFRGL-----GRIFKGLAQSGSWGC--FDEFNRIELPVLSVAA 94
Cdd:cd00009  26 GPPGTGKTTLARAIANELfrpGAPFLYLNASDlleGLVVAELfghflVRLLFELAEKAKPGVlfIDEIDSLSRGAQNALL 105

                        90
                ....*....|....*....
gi 2154925   95 QQINIVLTARRERTKQFIF 113
Cdd:cd00009 106 RVLETLNDLRIDRENVRVI 124
 
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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