DUF488 family protein [Nodularia spumigena]
DUF488 family protein( domain architecture ID 10009342)
DUF488 family protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
COG5483 | COG5483 | Uncharacterized conserved protein, DUF488 family [Function unknown]; |
7-149 | 1.85e-48 | |||
Uncharacterized conserved protein, DUF488 family [Function unknown]; : Pssm-ID: 444234 Cd Length: 147 Bit Score: 152.68 E-value: 1.85e-48
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Name | Accession | Description | Interval | E-value | |||
COG5483 | COG5483 | Uncharacterized conserved protein, DUF488 family [Function unknown]; |
7-149 | 1.85e-48 | |||
Uncharacterized conserved protein, DUF488 family [Function unknown]; Pssm-ID: 444234 Cd Length: 147 Bit Score: 152.68 E-value: 1.85e-48
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DUF488 | pfam04343 | Protein of unknown function, DUF488; This family includes several proteins of uncharacterized ... |
16-136 | 1.10e-30 | |||
Protein of unknown function, DUF488; This family includes several proteins of uncharacterized function. Pssm-ID: 427880 Cd Length: 123 Bit Score: 107.00 E-value: 1.10e-30
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MYSc_Myo11 | cd01384 | class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
78-147 | 7.91e-04 | |||
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Pssm-ID: 276835 Cd Length: 647 Bit Score: 38.43 E-value: 7.91e-04
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Name | Accession | Description | Interval | E-value | |||
COG5483 | COG5483 | Uncharacterized conserved protein, DUF488 family [Function unknown]; |
7-149 | 1.85e-48 | |||
Uncharacterized conserved protein, DUF488 family [Function unknown]; Pssm-ID: 444234 Cd Length: 147 Bit Score: 152.68 E-value: 1.85e-48
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DUF488 | pfam04343 | Protein of unknown function, DUF488; This family includes several proteins of uncharacterized ... |
16-136 | 1.10e-30 | |||
Protein of unknown function, DUF488; This family includes several proteins of uncharacterized function. Pssm-ID: 427880 Cd Length: 123 Bit Score: 107.00 E-value: 1.10e-30
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MYSc_Myo11 | cd01384 | class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
78-147 | 7.91e-04 | |||
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Pssm-ID: 276835 Cd Length: 647 Bit Score: 38.43 E-value: 7.91e-04
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Myosin_head | pfam00063 | Myosin head (motor domain); |
78-118 | 8.76e-03 | |||
Myosin head (motor domain); Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 35.33 E-value: 8.76e-03
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Blast search parameters | ||||
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