Conserved domains on
[gi|6322907|ref|NP_012980|]
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dynein heavy chain [Saccharomyces cerevisiae S288C]
Protein Classification
dynein heavy chain( domain architecture ID 1001887)
dynein heavy chain is part of the cytoplasmic dynein that acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules; has ATPase activity; similar to Saccharomyces cerevisiae cytoplasmic dynein heavy chain
PubMed: 15661525
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||||||||||||||||||||||||||||||||||
| DYN1 super family | cl34955 | Dynein, heavy chain [Cytoskeleton]; |
774-4083 | 0e+00 | |||||||||||||||||||||||||||||||||||||||||||
Dynein, heavy chain [Cytoskeleton]; The actual alignment was detected with superfamily member COG5245: Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 4592.26 E-value: 0e+00
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| DHC_N1 super family | cl20356 | Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
219-763 | 6.24e-36 | |||||||||||||||||||||||||||||||||||||||||||
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: 146.95 E-value: 6.24e-36
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| Name | Accession | Description | Interval | E-value | |||||||||||||||||||||||||||||||||||||||||||
| DYN1 | COG5245 | Dynein, heavy chain [Cytoskeleton]; |
774-4083 | 0e+00 | |||||||||||||||||||||||||||||||||||||||||||
Dynein, heavy chain [Cytoskeleton]; Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 4592.26 E-value: 0e+00
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| AAA_6 | pfam12774 | Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1758-2081 | 1.53e-113 | |||||||||||||||||||||||||||||||||||||||||||
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: 364.88 E-value: 1.53e-113
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| DHC_N1 | pfam08385 | Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
219-763 | 6.24e-36 | |||||||||||||||||||||||||||||||||||||||||||
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: 146.95 E-value: 6.24e-36
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| AAA | cd00009 | The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2393-2561 | 3.01e-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: 67.17 E-value: 3.01e-12
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2410-2553 | 9.32e-08 | |||||||||||||||||||||||||||||||||||||||||||
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: 9.32e-08
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
3022-3131 | 2.61e-04 | |||||||||||||||||||||||||||||||||||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 2.61e-04
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| Name | Accession | Description | Interval | E-value | |||||||||||||||||||||||||||||||||||||||||||
| DYN1 | COG5245 | Dynein, heavy chain [Cytoskeleton]; |
774-4083 | 0e+00 | |||||||||||||||||||||||||||||||||||||||||||
Dynein, heavy chain [Cytoskeleton]; Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 4592.26 E-value: 0e+00
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| AAA_6 | pfam12774 | Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1758-2081 | 1.53e-113 | |||||||||||||||||||||||||||||||||||||||||||
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: 364.88 E-value: 1.53e-113
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| DHC_N2 | pfam08393 | Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1221-1626 | 3.92e-99 | |||||||||||||||||||||||||||||||||||||||||||
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: 326.52 E-value: 3.92e-99
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| AAA_9 | pfam12781 | ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3378-3597 | 3.10e-67 | |||||||||||||||||||||||||||||||||||||||||||
ATP-binding 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 fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk. Pssm-ID: 463702 [Multi-domain] Cd Length: 222 Bit Score: 227.71 E-value: 3.10e-67
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| DHC_N1 | pfam08385 | Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
219-763 | 6.24e-36 | |||||||||||||||||||||||||||||||||||||||||||
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: 146.95 E-value: 6.24e-36
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| AAA_8 | pfam12780 | P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2731-2977 | 1.24e-33 | |||||||||||||||||||||||||||||||||||||||||||
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor. Pssm-ID: 463701 [Multi-domain] Cd Length: 259 Bit Score: 132.35 E-value: 1.24e-33
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| AAA_7 | pfam12775 | P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2389-2562 | 1.54e-32 | |||||||||||||||||||||||||||||||||||||||||||
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: 126.35 E-value: 1.54e-32
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| MT | pfam12777 | Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3014-3346 | 9.19e-23 | |||||||||||||||||||||||||||||||||||||||||||
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component. Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 102.84 E-value: 9.19e-23
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| AAA | cd00009 | The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2393-2561 | 3.01e-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: 67.17 E-value: 3.01e-12
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| AAA_lid_11 | pfam18198 | Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3930-4016 | 8.33e-10 | |||||||||||||||||||||||||||||||||||||||||||
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the C-terminal region of dynein heavy chain. Pssm-ID: 465676 Cd Length: 139 Bit Score: 59.78 E-value: 8.33e-10
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| Dynein_heavy | pfam03028 | Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3794-3891 | 2.10e-09 | |||||||||||||||||||||||||||||||||||||||||||
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained. Pssm-ID: 460782 Cd Length: 115 Bit Score: 57.84 E-value: 2.10e-09
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| AAA_5 | pfam07728 | AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2070-2210 | 2.29e-09 | |||||||||||||||||||||||||||||||||||||||||||
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: 58.46 E-value: 2.29e-09
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2410-2553 | 9.32e-08 | |||||||||||||||||||||||||||||||||||||||||||
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: 9.32e-08
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| AAA_5 | pfam07728 | AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2413-2552 | 4.21e-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: 49.21 E-value: 4.21e-06
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| PRK00409 | PRK00409 | recombination and DNA strand exchange inhibitor protein; Reviewed |
3022-3131 | 2.61e-04 | |||||||||||||||||||||||||||||||||||||||||||
recombination and DNA strand exchange inhibitor protein; Reviewed Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 2.61e-04
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| HEC1 | COG5185 | Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2998-3335 | 9.63e-04 | |||||||||||||||||||||||||||||||||||||||||||
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 9.63e-04
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1793-1845 | 5.79e-03 | |||||||||||||||||||||||||||||||||||||||||||
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: 40.43 E-value: 5.79e-03
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| PRK12704 | PRK12704 | phosphodiesterase; Provisional |
3022-3099 | 6.11e-03 | |||||||||||||||||||||||||||||||||||||||||||
phosphodiesterase; Provisional Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.11e-03
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| Mg_chelatase | pfam01078 | Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
2414-2537 | 8.01e-03 | |||||||||||||||||||||||||||||||||||||||||||
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa. Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 40.98 E-value: 8.01e-03
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| PilT | COG2805 | Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
2385-2425 | 8.43e-03 | |||||||||||||||||||||||||||||||||||||||||||
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures]; Pssm-ID: 442056 Cd Length: 342 Bit Score: 41.62 E-value: 8.43e-03
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| Blast search parameters | ||||
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