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Conserved domains on  [gi|109255220|ref|NP_001035883|]
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calcium-binding tyrosine phosphorylation-regulated protein isoform a [Mus musculus]

Protein Classification

CABYR/SP17 family protein( domain architecture ID 10186655)

CABYR/SP17 family protein similar to Homo sapiens calcium-binding tyrosine phosphorylation-regulated protein (CABYR) and Mus musculus sperm surface protein Sp17, which are naturally located in the human sperm fibrous sheath (FS)

CATH:  1.20.890.10
Gene Ontology:  GO:0046983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD_CABYR_SP17 cd12100
dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding ...
 7-48 1.90e-18

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: 78.27  E-value: 1.90e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 109255220   7 RLVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKELIVFR 48
Cdd:cd12100    1 RLRLPYGLKSLLEGLSREVLREQPEDIPEFAADYFEELLKFR 42
 
Name Accession Description Interval E-value
DD_CABYR_SP17 cd12100
dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding ...
 7-48 1.90e-18

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: 78.27  E-value: 1.90e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 109255220   7 RLVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKELIVFR 48
Cdd:cd12100    1 RLRLPYGLKSLLEGLSREVLREQPEDIPEFAADYFEELLKFR 42
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
12-44 3.92e-07

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 46.16  E-value: 3.92e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 109255220   12 YGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKL 33
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 12-44 5.05e-07

RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit portion of type II PKA R-subunit. Contains dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs).


Pssm-ID: 197697  Cd Length: 38  Bit Score: 45.79  E-value: 5.05e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 109255220    12 YGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKL 33
 
Name Accession Description Interval E-value
DD_CABYR_SP17 cd12100
dimerization/docking (D/D) domain of the sperm fibrous sheath proteins, Calcium-Binding ...
 7-48 1.90e-18

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: 78.27  E-value: 1.90e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 109255220   7 RLVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKELIVFR 48
Cdd:cd12100    1 RLRLPYGLKSLLEGLSREVLREQPEDIPEFAADYFEELLKFR 42
DD_RII_PKA-like cd12084
dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein ...
 10-44 1.06e-07

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: 47.80  E-value: 1.06e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 109255220  10 VPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:cd12084    1 VPEGLRELLEDFTREVLREQPEDVYEFAADYFEKL 35
RIIa pfam02197
Regulatory subunit of type II PKA R-subunit;
12-44 3.92e-07

Regulatory subunit of type II PKA R-subunit;


Pssm-ID: 396669  Cd Length: 37  Bit Score: 46.16  E-value: 3.92e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 109255220   12 YGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:pfam02197   1 HGLQALLEDLTVEVLRAQPSDPLQFAADYFEKL 33
RIIa smart00394
RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit ...
 12-44 5.05e-07

RIIalpha, Regulatory subunit portion of type II PKA R-subunit; RIIalpha, Regulatory subunit portion of type II PKA R-subunit. Contains dimerisation interface and binding site for A-kinase-anchoring proteins (AKAPs).


Pssm-ID: 197697  Cd Length: 38  Bit Score: 45.79  E-value: 5.05e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 109255220    12 YGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:smart00394   1 HGLQALLEDLTVEVLRAQPSDLVQFAADYFEKL 33
DD_CrRSP7-like cd22984
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 3-44 6.36e-05

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: 40.27  E-value: 6.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 109255220   3 SSK--PRLVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:cd22984    1 ASKyaKKYTIPEEFPAILKDFAREVLREQPKDIYEFGAQYFKRL 44
DD_RII_PKA cd12099
dimerization/docking (D/D) domain of the Type II Regulatory subunit of cAMP-dependent protein ...
 10-44 1.09e-04

dimerization/docking (D/D) domain of the Type II Regulatory subunit of cAMP-dependent protein kinase; 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIalpha plays a role in the association and dissociation of PKA with the centrosome during interphase and mitosis, respectively. RIIbeta plays an important role in adipocytes and neuronal tissues. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. 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: 438520  Cd Length: 37  Bit Score: 39.38  E-value: 1.09e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 109255220  10 VPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:cd12099    1 VPPGLTELLQDFTVAVLREQPTDLVDFAAEYFTRL 35
DD_ROP-like cd22972
dimerization/docking (D/D) domain found in the ropporin (ROP)-like subfamily; The ROP-like ...
 8-44 1.43e-04

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: 39.20  E-value: 1.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 109255220   8 LVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:cd22972    4 IVIPEGLPEILKAYAKEAIRSQPEDLIQWSAKYFRAL 40
DD_RIIAD1 cd22971
dimerization/docking (D/D) domain found in RIIa domain-containing protein 1 (RIIAD1) and ...
 14-41 8.19e-04

dimerization/docking (D/D) domain found in RIIa domain-containing protein 1 (RIIAD1) and similar proteins; The family includes uncharacterized RIIa domain-containing protein 1 (RIIAD1), which contains a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438540  Cd Length: 41  Bit Score: 37.00  E-value: 8.19e-04
                         10        20
                 ....*....|....*....|....*...
gi 109255220  14 LKTLLEGVSRAILKTNPTNITQFAAVYF 41
Cdd:cd22971    6 IRALISGFLREVLKKKPENIREFAAEFF 33
DD_CrRSP11-like cd22985
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 8-44 2.32e-03

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: 36.00  E-value: 2.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 109255220   8 LVVPYGLKTLLEGVSRAILKTNPTNITQFAAVYFKEL 44
Cdd:cd22985    9 INIPPELPDILKNYTKEVIRAQPADLYEFSAEYFAKL 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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