transmembrane protein, putative (DUF247) [Arabidopsis thaliana]
Protein Classification
DUF247 domain-containing protein( domain architecture ID 10504334)
DUF247 domain-containing protein similar to Arabidopsis thaliana UPF0481 protein At3g47200
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| DUF247 | pfam03140 | Plant protein of unknown function; The function of the plant proteins constituting this family ... |
33-408 | 3.13e-140 | ||||||
Plant protein of unknown function; The function of the plant proteins constituting this family is unknown. : Pssm-ID: 460823 Cd Length: 390 Bit Score: 406.63 E-value: 3.13e-140
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| Name | Accession | Description | Interval | E-value | ||||||
| DUF247 | pfam03140 | Plant protein of unknown function; The function of the plant proteins constituting this family ... |
33-408 | 3.13e-140 | ||||||
Plant protein of unknown function; The function of the plant proteins constituting this family is unknown. Pssm-ID: 460823 Cd Length: 390 Bit Score: 406.63 E-value: 3.13e-140
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| MYSc_Myh11 | cd14921 | class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
179-303 | 3.72e-03 | ||||||
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving 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. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy. Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 39.61 E-value: 3.72e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| DUF247 | pfam03140 | Plant protein of unknown function; The function of the plant proteins constituting this family ... |
33-408 | 3.13e-140 | ||||||
Plant protein of unknown function; The function of the plant proteins constituting this family is unknown. Pssm-ID: 460823 Cd Length: 390 Bit Score: 406.63 E-value: 3.13e-140
|
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| MYSc_Myh11 | cd14921 | class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
179-303 | 3.72e-03 | ||||||
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving 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. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy. Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 39.61 E-value: 3.72e-03
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