PREDICTED: uncharacterized protein LOC100880059 isoform X1 [Megachile rotundata]
Protein Classification
ropporin family protein( domain architecture ID 17786836)
ropporin family protein similar to Homo sapiens ropporin-1A, ropporin-1B and and ropporin-1-like protein, which play important roles in male fertility
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| DD_ROP | cd23019 | dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A ... |
10-52 | 4.10e-21 | ||
dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A (ROP1A, also called cancer/testis antigen 91, CT91, or rhophilin-associated protein 1A), ropporin-1B (ROP1B, also called rhophilin-associated protein 1B), and ropporin-1-like protein (ROPN1L, also called ROPN1-like protein, AKAP-associated sperm protein, or ASP). ROP1A, ROP1B and ROPN1L play important roles in male fertility. They are involved in fibrous sheath integrity and sperm motility and play roles in cAMP-dependent protein kinase (PKA)-dependent signaling processes required for spermatozoa capacitation. Members of this subfamily contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domain of the regulatory subunit of PKA, which dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). ROP1A and ROP1B have been shown to bind AKAP3. : Pssm-ID: 438555 Cd Length: 43 Bit Score: 85.42 E-value: 4.10e-21
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| DD_ROP | cd23019 | dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A ... |
10-52 | 4.10e-21 | ||
dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A (ROP1A, also called cancer/testis antigen 91, CT91, or rhophilin-associated protein 1A), ropporin-1B (ROP1B, also called rhophilin-associated protein 1B), and ropporin-1-like protein (ROPN1L, also called ROPN1-like protein, AKAP-associated sperm protein, or ASP). ROP1A, ROP1B and ROPN1L play important roles in male fertility. They are involved in fibrous sheath integrity and sperm motility and play roles in cAMP-dependent protein kinase (PKA)-dependent signaling processes required for spermatozoa capacitation. Members of this subfamily contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domain of the regulatory subunit of PKA, which dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). ROP1A and ROP1B have been shown to bind AKAP3. Pssm-ID: 438555 Cd Length: 43 Bit Score: 85.42 E-value: 4.10e-21
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| DD_ROP | cd23019 | dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A ... |
10-52 | 4.10e-21 | ||
dimerization/docking (D/D) domain found in ropporins; The ROP subfamily includes ropporin-1A (ROP1A, also called cancer/testis antigen 91, CT91, or rhophilin-associated protein 1A), ropporin-1B (ROP1B, also called rhophilin-associated protein 1B), and ropporin-1-like protein (ROPN1L, also called ROPN1-like protein, AKAP-associated sperm protein, or ASP). ROP1A, ROP1B and ROPN1L play important roles in male fertility. They are involved in fibrous sheath integrity and sperm motility and play roles in cAMP-dependent protein kinase (PKA)-dependent signaling processes required for spermatozoa capacitation. Members of this subfamily contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domain of the regulatory subunit of PKA, which dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). ROP1A and ROP1B have been shown to bind AKAP3. Pssm-ID: 438555 Cd Length: 43 Bit Score: 85.42 E-value: 4.10e-21
|
||||||
| DD_ROP-like | cd22972 | dimerization/docking (D/D) domain found in the ropporin (ROP)-like subfamily; The ROP-like ... |
10-52 | 3.23e-16 | ||
dimerization/docking (D/D) domain found in the ropporin (ROP)-like subfamily; The ROP-like family includes ropporin-1A (ROP1A, also called cancer/testis antigen 91, CT91, or rhophilin-associated protein 1A), ropporin-1B (ROP1B, also called rhophilin-associated protein 1B), and ropporin-1-like protein (ROPN1L, also called ROPN1-like protein, AKAP-associated sperm protein, or ASP), as well as Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP7 and RSP11. ROP1A, ROP1B and ROPN1L play important roles in male fertility. They are involved in fibrous sheath integrity and sperm motility and play roles in cAMP-dependent protein kinase (PKA)-dependent signaling processes required for spermatozoa capacitation. RSP7 is a PKA RII-like protein. RSP11 is a non-PKA RIIa protein that contains a RII domain but lack any features required for cAMP signaling or phosphorylation. It is involved in the control of ciliary and flagellar beating. Members of this subfamily contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domain of the regulatory subunit of PKA. Pssm-ID: 438541 Cd Length: 43 Bit Score: 71.95 E-value: 3.23e-16
|
||||||
| DD_CrRSP11-like | cd22985 | dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ... |
4-51 | 6.12e-14 | ||
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 11 (RSP11) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP11 is a non-PKA (cAMP-dependent protein kinase) RIIa protein that contains a RII domain but lack any features required for cAMP signaling or phosphorylation. It is involved in the control of ciliary and flagellar beating. RSP11 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP11 heterodimerizes with the D/D domain of RSP7 to form an X-type four-helix bundle within the radial spoke RS1 complex. Pssm-ID: 438554 Cd Length: 49 Bit Score: 65.66 E-value: 6.12e-14
|
||||||
| DD_CrRSP7-like | cd22984 | dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ... |
11-52 | 4.22e-08 | ||
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 7 (RSP7) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP7 is a cAMP-dependent protein kinase (PKA) RII-like protein. RSP7 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP7 heterodimerizes with the D/D domain of RSP11 to form an X-type four-helix bundle within the radial spoke RS1 complex. Pssm-ID: 438553 Cd Length: 47 Bit Score: 49.13 E-value: 4.22e-08
|
||||||
| DD_CABYR_SP17 | cd12100 | dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding ... |
13-49 | 2.32e-03 | ||
dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding tYrosine-phosphorylation Regulated protein and Sperm Protein 17; CABYR and SP17 are naturally located in the human sperm fibrous sheath (FS). CABYR was originally isolated from spermatoza and was thought to be testis-specific, but has recently been observed in lung and brain tumors. It is a polymorphic calcium binding protein that is phosphorylated during capacitation. SP17 plays an important role in the interaction of sperm with the zona pellucida during fertilization. It also promotes cell-cell adhesion. SP17 is found in various human tumors of unrelated histological origin including metastatic squamous cell carcinoma, multiple myeloma, ovarian cancer, and primary nervous system tumors, among others. Both CABYR and SP17 contain an N-terminal dimerization/docking (D/D) domain with similarity to the D/D domain of the R subunit of cAMP-dependent protein kinase (PKA). The D/D domain of the R subunit dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. The D/D domain of CABYR and SP17 have been shown to bind to AKAP3, a protein that is also associated to the FS of mammalian spermatozoa. Pssm-ID: 438521 Cd Length: 42 Bit Score: 35.51 E-value: 2.32e-03
|
||||||
| DD_RII_PKA-like | cd12084 | dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein ... |
15-49 | 3.17e-03 | ||
dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein kinase and similar domains; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. RI and RII subunits are distinguished by their IS; RII subunits contain a phosphorylation site and are both substrates and inhibitors while RI subunits are pseudo-substrates. RI subunits require ATP and Mg ions to form a stable holoenzyme while RII subunits do not. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. Pssm-ID: 438517 Cd Length: 36 Bit Score: 35.09 E-value: 3.17e-03
|
||||||
| Blast search parameters | ||||
|
