Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
1255-1653
1.49e-118
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
:
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 381.22 E-value: 1.49e-118
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
1791-2019
1.94e-105
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: 340.61 E-value: 1.94e-105
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ...
205-745
7.52e-19
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
The actual alignment was detected with superfamily member pfam08385:
Pssm-ID: 462457 Cd Length: 560 Bit Score: 92.64 E-value: 7.52e-19
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
1255-1653
1.49e-118
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 381.22 E-value: 1.49e-118
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
1791-2019
1.94e-105
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: 340.61 E-value: 1.94e-105
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ...
205-745
7.52e-19
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 92.64 E-value: 7.52e-19
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
1255-1653
1.49e-118
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 381.22 E-value: 1.49e-118
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
1791-2019
1.94e-105
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: 340.61 E-value: 1.94e-105
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ...
205-745
7.52e-19
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 92.64 E-value: 7.52e-19
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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