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Conserved domains on  [gi|1806965802|ref|WP_162421533|]
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RuBisCO accumulation factor 1 [Myxacorys almedinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RuBisCo_chap_C pfam18087
Rubisco Assembly chaperone C-terminal domain; This is the C-terminal domain, also known as the ...
 201-338 3.74e-73

Rubisco Assembly chaperone C-terminal domain; This is the C-terminal domain, also known as the beta domain, of Rubsico Assembly Chaperone protein (Raf1). Raf1 is necessary for rubisco to catalyze the rate-limiting step of carbon fixation through carboxylating the five-carbon sugar substrate ribulose-1,5-bisphosphate. The beta domains primary function is dimerization, which is critical for Raf1 to achieve the necessary avidity for complex formation with RbcL (the large complex sub-unbit of Rubsico) assembly intermediates. The beta domain is also involved, to a small extent, in binding to RbcL with use of the lustiness near the beta domain's conserved top surface.


:

Pssm-ID: 436262  Cd Length: 138  Bit Score: 223.19  E-value: 3.74e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802 201 LPLYRLESDEELPRIVPVVGKLPLTKADLDAVPMVEEVGAFHLVQFSGIGAWVTLPGWQVVRTADDPIALLCDSDKLPNP 280
Cdd:pfam18087   1 LPVYRLESEEELPRILPVAGELPLTVADLQAVPLLEEEGPFGVVKFSGWGAWVALPGWQVVLKAEDPVAILCDSDRLPWP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1806965802 281 PSGVAEEVVVVIDRAQRDWQADSYFLMAEDDQLRLRWFEEAPEVALLGRVVLVMRPKK 338
Cdd:pfam18087  81 LKEEPEPVLVVVDRAQREWDADSYFVVEQEGQLKVQWFEEGPEIELLGQVVLVVRPKR 138
Raf1_N pfam18578
Rubisco accumulation factor 1 alpha helical domain; This is the N-terminal alpha helical ...
 82-187 1.56e-60

Rubisco accumulation factor 1 alpha helical domain; This is the N-terminal alpha helical domain found in Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive.


:

Pssm-ID: 436592  Cd Length: 106  Bit Score: 189.60  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802  82 FGQRSSDILYELRILTQRDRASAAELVFAHKLDADEVHEVARALKDFSRFGTPPDEFTTHPGDGVAYQAWKAAKQKTDLQ 161
Cdd:pfam18578   1 FDQGGSDLLYELRILSQEQRAAAAELIVEKNLDADGARELARAIKDFSRRRGLPEGFTDHPGDAVAYQYWRLARQKKDLQ 80

                          90       100
                  ....*....|....*....|....*.
gi 1806965802 162 ERSRLIARGLKFAHSATARQAVEKLL 187
Cdd:pfam18578  81 ERSRLIAKGLKFAHSETARQQIEKLL 106
Raf1_HTH pfam18579
Rubisco accumulation factor 1 helix turn helix domain; This is helix turn helix domain found ...
 11-70 5.63e-35

Rubisco accumulation factor 1 helix turn helix domain; This is helix turn helix domain found in alpha helical region of Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive.


:

Pssm-ID: 436593  Cd Length: 61  Bit Score: 122.27  E-value: 5.63e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802  11 VAELLQSLRRKEGKWVEWAHACQTLQKAGYSPQAIFEETGFEPIQQNQIVVASQVYDTLL 70
Cdd:pfam18579   2 TEELLESLRRKEGTWVEWAKACQQLQKAGYSPQTIFEATGFEPIQQNQIIVAAQVYDSLV 61
 
Name Accession Description Interval E-value
RuBisCo_chap_C pfam18087
Rubisco Assembly chaperone C-terminal domain; This is the C-terminal domain, also known as the ...
 201-338 3.74e-73

Rubisco Assembly chaperone C-terminal domain; This is the C-terminal domain, also known as the beta domain, of Rubsico Assembly Chaperone protein (Raf1). Raf1 is necessary for rubisco to catalyze the rate-limiting step of carbon fixation through carboxylating the five-carbon sugar substrate ribulose-1,5-bisphosphate. The beta domains primary function is dimerization, which is critical for Raf1 to achieve the necessary avidity for complex formation with RbcL (the large complex sub-unbit of Rubsico) assembly intermediates. The beta domain is also involved, to a small extent, in binding to RbcL with use of the lustiness near the beta domain's conserved top surface.


Pssm-ID: 436262  Cd Length: 138  Bit Score: 223.19  E-value: 3.74e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802 201 LPLYRLESDEELPRIVPVVGKLPLTKADLDAVPMVEEVGAFHLVQFSGIGAWVTLPGWQVVRTADDPIALLCDSDKLPNP 280
Cdd:pfam18087   1 LPVYRLESEEELPRILPVAGELPLTVADLQAVPLLEEEGPFGVVKFSGWGAWVALPGWQVVLKAEDPVAILCDSDRLPWP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1806965802 281 PSGVAEEVVVVIDRAQRDWQADSYFLMAEDDQLRLRWFEEAPEVALLGRVVLVMRPKK 338
Cdd:pfam18087  81 LKEEPEPVLVVVDRAQREWDADSYFVVEQEGQLKVQWFEEGPEIELLGQVVLVVRPKR 138
Raf1_N pfam18578
Rubisco accumulation factor 1 alpha helical domain; This is the N-terminal alpha helical ...
 82-187 1.56e-60

Rubisco accumulation factor 1 alpha helical domain; This is the N-terminal alpha helical domain found in Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive.


Pssm-ID: 436592  Cd Length: 106  Bit Score: 189.60  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802  82 FGQRSSDILYELRILTQRDRASAAELVFAHKLDADEVHEVARALKDFSRFGTPPDEFTTHPGDGVAYQAWKAAKQKTDLQ 161
Cdd:pfam18578   1 FDQGGSDLLYELRILSQEQRAAAAELIVEKNLDADGARELARAIKDFSRRRGLPEGFTDHPGDAVAYQYWRLARQKKDLQ 80

                          90       100
                  ....*....|....*....|....*.
gi 1806965802 162 ERSRLIARGLKFAHSATARQAVEKLL 187
Cdd:pfam18578  81 ERSRLIAKGLKFAHSETARQQIEKLL 106
Raf1_HTH pfam18579
Rubisco accumulation factor 1 helix turn helix domain; This is helix turn helix domain found ...
 11-70 5.63e-35

Rubisco accumulation factor 1 helix turn helix domain; This is helix turn helix domain found in alpha helical region of Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive.


Pssm-ID: 436593  Cd Length: 61  Bit Score: 122.27  E-value: 5.63e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802  11 VAELLQSLRRKEGKWVEWAHACQTLQKAGYSPQAIFEETGFEPIQQNQIVVASQVYDTLL 70
Cdd:pfam18579   2 TEELLESLRRKEGTWVEWAKACQQLQKAGYSPQTIFEATGFEPIQQNQIIVAAQVYDSLV 61
 
Name Accession Description Interval E-value
RuBisCo_chap_C pfam18087
Rubisco Assembly chaperone C-terminal domain; This is the C-terminal domain, also known as the ...
 201-338 3.74e-73

Rubisco Assembly chaperone C-terminal domain; This is the C-terminal domain, also known as the beta domain, of Rubsico Assembly Chaperone protein (Raf1). Raf1 is necessary for rubisco to catalyze the rate-limiting step of carbon fixation through carboxylating the five-carbon sugar substrate ribulose-1,5-bisphosphate. The beta domains primary function is dimerization, which is critical for Raf1 to achieve the necessary avidity for complex formation with RbcL (the large complex sub-unbit of Rubsico) assembly intermediates. The beta domain is also involved, to a small extent, in binding to RbcL with use of the lustiness near the beta domain's conserved top surface.


Pssm-ID: 436262  Cd Length: 138  Bit Score: 223.19  E-value: 3.74e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802 201 LPLYRLESDEELPRIVPVVGKLPLTKADLDAVPMVEEVGAFHLVQFSGIGAWVTLPGWQVVRTADDPIALLCDSDKLPNP 280
Cdd:pfam18087   1 LPVYRLESEEELPRILPVAGELPLTVADLQAVPLLEEEGPFGVVKFSGWGAWVALPGWQVVLKAEDPVAILCDSDRLPWP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1806965802 281 PSGVAEEVVVVIDRAQRDWQADSYFLMAEDDQLRLRWFEEAPEVALLGRVVLVMRPKK 338
Cdd:pfam18087  81 LKEEPEPVLVVVDRAQREWDADSYFVVEQEGQLKVQWFEEGPEIELLGQVVLVVRPKR 138
Raf1_N pfam18578
Rubisco accumulation factor 1 alpha helical domain; This is the N-terminal alpha helical ...
 82-187 1.56e-60

Rubisco accumulation factor 1 alpha helical domain; This is the N-terminal alpha helical domain found in Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive.


Pssm-ID: 436592  Cd Length: 106  Bit Score: 189.60  E-value: 1.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802  82 FGQRSSDILYELRILTQRDRASAAELVFAHKLDADEVHEVARALKDFSRFGTPPDEFTTHPGDGVAYQAWKAAKQKTDLQ 161
Cdd:pfam18578   1 FDQGGSDLLYELRILSQEQRAAAAELIVEKNLDADGARELARAIKDFSRRRGLPEGFTDHPGDAVAYQYWRLARQKKDLQ 80

                          90       100
                  ....*....|....*....|....*.
gi 1806965802 162 ERSRLIARGLKFAHSATARQAVEKLL 187
Cdd:pfam18578  81 ERSRLIAKGLKFAHSETARQQIEKLL 106
Raf1_HTH pfam18579
Rubisco accumulation factor 1 helix turn helix domain; This is helix turn helix domain found ...
 11-70 5.63e-35

Rubisco accumulation factor 1 helix turn helix domain; This is helix turn helix domain found in alpha helical region of Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive.


Pssm-ID: 436593  Cd Length: 61  Bit Score: 122.27  E-value: 5.63e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806965802  11 VAELLQSLRRKEGKWVEWAHACQTLQKAGYSPQAIFEETGFEPIQQNQIVVASQVYDTLL 70
Cdd:pfam18579   2 TEELLESLRRKEGTWVEWAKACQQLQKAGYSPQTIFEATGFEPIQQNQIIVAAQVYDSLV 61
 
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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