allophycocyanin beta subunit (plastid) [Erythrotrichia carnea]
globin family protein( domain architecture ID 229384)
globin family protein is an all-helical protein that may bind porphyrins, phycobilins, and other non-heme cofactors, and may play various roles including as a sensor or transporter of oxygen
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Globin-like super family | cl21461 | Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ... |
1-161 | 8.14e-106 | ||||
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety of all-helical proteins that bind porphyrins, phycobilins, and other non-heme cofactors, and play various roles in all three kingdoms of life, including sensors or transporters of oxygen. It includes the M/myoglobin-like, S/sensor globin, and T/truncated globin (TrHb) families, and the phycobiliproteins (PBPs). The M family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The S family includes GCS/globin-coupled sensors, Pgbs/protoglobins, and SSDgbs/sensor single domain globins. The T family is classified into three main groups: TrHb1s (N), TrHb2s (O) and TrHb3s (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). For M family Adgbs, this globin domain is permuted, such that C-H are followed by A-B. The T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. PBPs bind the linear tetrapyrrole chromophore, phycobilin, a prosthetic group chemically and metabolically related to iron protoporphyrin IX/protoheme. Examples of other globin-like domains which bind non-heme cofactors include those of the Bacillus anthracis sporulation inhibitors pXO1-118 and pXO2-61 which bind fatty acid and halide in vitro, and the globin-like domain of Bacillus subtilis RsbRA which is presumed to channel sensory input to the C-terminal sulfate transporter/ anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B). The actual alignment was detected with superfamily member CHL00088: Pssm-ID: 473869 [Multi-domain] Cd Length: 161 Bit Score: 299.21 E-value: 8.14e-106
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Name | Accession | Description | Interval | E-value | ||||
apcB | CHL00088 | allophycocyanin beta subunit |
1-161 | 8.14e-106 | ||||
allophycocyanin beta subunit Pssm-ID: 164493 [Multi-domain] Cd Length: 161 Bit Score: 299.21 E-value: 8.14e-106
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ApcB | COG5685 | Allophycocyanin beta chain [Energy production and conversion]; |
1-161 | 1.28e-88 | ||||
Allophycocyanin beta chain [Energy production and conversion]; Pssm-ID: 444399 [Multi-domain] Cd Length: 162 Bit Score: 255.63 E-value: 1.28e-88
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APC_beta | cd12126 | Allophycocyanin beta subunit of the phycobilisome core; Phycobilisomes (PBSs) are the main ... |
1-160 | 4.85e-88 | ||||
Allophycocyanin beta subunit of the phycobilisome core; Phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 271281 [Multi-domain] Cd Length: 163 Bit Score: 254.19 E-value: 4.85e-88
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apcB | TIGR01337 | allophycocyanin, beta subunit; The alpha and beta subunits of allophycocyanin form ... |
2-161 | 3.55e-78 | ||||
allophycocyanin, beta subunit; The alpha and beta subunits of allophycocyanin form heterodimers, six of which associate into larger aggregates as part of the phycobilisome, a light-harvesting complex of phycobiliproteins and linker proteins. This model describes allophycocyanin beta subunit. Other, homologous phyobiliproteins include allophycocyanin alpha chain and the phycocyanin and phycoerythrin alpha and beta chains. [Energy metabolism, Photosynthesis] Pssm-ID: 273559 Cd Length: 167 Bit Score: 229.32 E-value: 3.55e-78
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Phycobilisome | pfam00502 | Phycobilisome protein; |
7-160 | 1.50e-65 | ||||
Phycobilisome protein; Pssm-ID: 425723 [Multi-domain] Cd Length: 155 Bit Score: 196.94 E-value: 1.50e-65
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Name | Accession | Description | Interval | E-value | ||||
apcB | CHL00088 | allophycocyanin beta subunit |
1-161 | 8.14e-106 | ||||
allophycocyanin beta subunit Pssm-ID: 164493 [Multi-domain] Cd Length: 161 Bit Score: 299.21 E-value: 8.14e-106
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ApcB | COG5685 | Allophycocyanin beta chain [Energy production and conversion]; |
1-161 | 1.28e-88 | ||||
Allophycocyanin beta chain [Energy production and conversion]; Pssm-ID: 444399 [Multi-domain] Cd Length: 162 Bit Score: 255.63 E-value: 1.28e-88
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APC_beta | cd12126 | Allophycocyanin beta subunit of the phycobilisome core; Phycobilisomes (PBSs) are the main ... |
1-160 | 4.85e-88 | ||||
Allophycocyanin beta subunit of the phycobilisome core; Phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 271281 [Multi-domain] Cd Length: 163 Bit Score: 254.19 E-value: 4.85e-88
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apcB | TIGR01337 | allophycocyanin, beta subunit; The alpha and beta subunits of allophycocyanin form ... |
2-161 | 3.55e-78 | ||||
allophycocyanin, beta subunit; The alpha and beta subunits of allophycocyanin form heterodimers, six of which associate into larger aggregates as part of the phycobilisome, a light-harvesting complex of phycobiliproteins and linker proteins. This model describes allophycocyanin beta subunit. Other, homologous phyobiliproteins include allophycocyanin alpha chain and the phycocyanin and phycoerythrin alpha and beta chains. [Energy metabolism, Photosynthesis] Pssm-ID: 273559 Cd Length: 167 Bit Score: 229.32 E-value: 3.55e-78
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Phycobilisome | pfam00502 | Phycobilisome protein; |
7-160 | 1.50e-65 | ||||
Phycobilisome protein; Pssm-ID: 425723 [Multi-domain] Cd Length: 155 Bit Score: 196.94 E-value: 1.50e-65
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apcF | CHL00089 | allophycocyanin beta 18 subunit |
1-141 | 3.58e-54 | ||||
allophycocyanin beta 18 subunit Pssm-ID: 100206 Cd Length: 169 Bit Score: 168.82 E-value: 3.58e-54
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PBP-like | cd08919 | Phycobiliproteins (PBPs) and related proteins; phycobilisomes (PBSs) are the main ... |
4-160 | 4.53e-50 | ||||
Phycobiliproteins (PBPs) and related proteins; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This family also contains allophycocyanin-like (Apl) proteins, which conserve the residues critical for chromophore interactions, but may not maintain the proper alpha-beta subunit interactions and tertiary structure of PBPs. The genes encoding the Apl proteins cluster with light-responsive regulatory components, so these may have photoresponsive regulatory role(s). Included in this family is the PBP-like domain of the core-membrane linker polypeptide (LCM). The LCM serves both as a terminal energy acceptor and as a linker polypeptide. Its single phycocyanobilin (PCB) chromophore is one of two terminal energy transmitters, and transfers excitations from the hundreds of chromophores of the PBS to the RCs. This family also includes some proteins which have glutathione-S-transferases (GST) domains N-terminal to this PBP-like domain. Pssm-ID: 381259 Cd Length: 153 Bit Score: 157.84 E-value: 4.53e-50
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CpcB | COG5688 | Phycocyanin/phycoerythrin beta chain, CpcB/CpeB [Energy production and conversion]; |
1-161 | 1.75e-40 | ||||
Phycocyanin/phycoerythrin beta chain, CpcB/CpeB [Energy production and conversion]; Pssm-ID: 444402 Cd Length: 172 Bit Score: 134.00 E-value: 1.75e-40
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ApcA | COG5684 | Allophycocyanin alpha chain [Energy production and conversion]; |
5-161 | 3.50e-40 | ||||
Allophycocyanin alpha chain [Energy production and conversion]; Pssm-ID: 444398 [Multi-domain] Cd Length: 161 Bit Score: 132.68 E-value: 3.50e-40
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APC_alpha | cd12125 | Allophycocyanin alpha subunit of the phycobilisome core; Phycobilisomes (PBSs) are the main ... |
5-155 | 2.31e-36 | ||||
Allophycocyanin alpha subunit of the phycobilisome core; Phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 381265 [Multi-domain] Cd Length: 159 Bit Score: 123.16 E-value: 2.31e-36
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apcA | CHL00086 | allophycocyanin alpha subunit |
5-160 | 1.20e-35 | ||||
allophycocyanin alpha subunit Pssm-ID: 164492 [Multi-domain] Cd Length: 161 Bit Score: 121.25 E-value: 1.20e-35
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cpeB | CHL00172 | phycoerythrin beta subunit; Provisional |
1-161 | 3.74e-35 | ||||
phycoerythrin beta subunit; Provisional Pssm-ID: 133617 Cd Length: 177 Bit Score: 120.56 E-value: 3.74e-35
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cpcB | CHL00171 | phycocyanin beta subunit; Reviewed |
1-160 | 5.25e-34 | ||||
phycocyanin beta subunit; Reviewed Pssm-ID: 100271 Cd Length: 172 Bit Score: 117.41 E-value: 5.25e-34
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PC_PEC_beta | cd14768 | Beta subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components; ... |
1-158 | 5.43e-34 | ||||
Beta subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 271301 Cd Length: 171 Bit Score: 117.24 E-value: 5.43e-34
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PE-PC-PEC_beta | cd12127 | Beta subunits of phycocyanin, phycoerythrin and phycoerythrocyanin; phycobilisome rod ... |
1-161 | 1.63e-33 | ||||
Beta subunits of phycocyanin, phycoerythrin and phycoerythrocyanin; phycobilisome rod components; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This family also includes the beta subunits of Cryptophyte phycobiliproteins which represent another type of biliprotein antenna with different structure and organization. The beta subunits of cryptophyte PBPs share a high degree of sequence identity with both the alpha and beta subunits of the cyanobacterial and red algal PBPs, however the alpha cryptophyte subunits are shorter, and unrelated. There is only one type of PBP present in a single species, either phycocyanin or phycoerythrin, but not allophycocyanin. Structurally, phycoerythrin in cryptophytes is an alpha1alpha2betabeta dimer and not a trimer as in the PBS. Pssm-ID: 381266 Cd Length: 174 Bit Score: 116.43 E-value: 1.63e-33
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PE_beta-like | cd14767 | Phycoerythrin beta subunit, a component of the phycobilisome rod; and related proteins; ... |
1-161 | 1.40e-30 | ||||
Phycoerythrin beta subunit, a component of the phycobilisome rod; and related proteins; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This subfamily also includes the beta subunits of Cryptophyte phycobiliproteins which represent another type of biliprotein antenna with different structure and organization. The beta subunits of cryptophyte PBPs share a high degree of sequence identity with both the alpha and beta subunits of the cyanobacterial and red algal PBPs, however the alpha cryptophyte subunits are shorter, and unrelated. There is only one type of PBP present in a single species, either phycocyanin or phycoerythrin, but not allophycocyanin. Structurally, phycoerythrin in cryptophytes is an alpha1alpha2betabeta dimer and not a trimer as in the PBS. Pssm-ID: 271300 Cd Length: 176 Bit Score: 108.83 E-value: 1.40e-30
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apcD | CHL00090 | allophycocyanin gamma subunit |
5-161 | 5.72e-30 | ||||
allophycocyanin gamma subunit Pssm-ID: 164494 Cd Length: 161 Bit Score: 106.79 E-value: 5.72e-30
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Globin-like | cd01067 | Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ... |
62-160 | 1.01e-21 | ||||
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety of all-helical proteins that bind porphyrins, phycobilins, and other non-heme cofactors, and play various roles in all three kingdoms of life, including sensors or transporters of oxygen. It includes the M/myoglobin-like, S/sensor globin, and T/truncated globin (TrHb) families, and the phycobiliproteins (PBPs). The M family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The S family includes GCS/globin-coupled sensors, Pgbs/protoglobins, and SSDgbs/sensor single domain globins. The T family is classified into three main groups: TrHb1s (N), TrHb2s (O) and TrHb3s (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). For M family Adgbs, this globin domain is permuted, such that C-H are followed by A-B. The T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. PBPs bind the linear tetrapyrrole chromophore, phycobilin, a prosthetic group chemically and metabolically related to iron protoporphyrin IX/protoheme. Examples of other globin-like domains which bind non-heme cofactors include those of the Bacillus anthracis sporulation inhibitors pXO1-118 and pXO2-61 which bind fatty acid and halide in vitro, and the globin-like domain of Bacillus subtilis RsbRA which is presumed to channel sensory input to the C-terminal sulfate transporter/ anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B). Pssm-ID: 381255 [Multi-domain] Cd Length: 119 Bit Score: 84.43 E-value: 1.01e-21
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PE-PC-PEC_alpha | cd12129 | Alpha subunits of phycoerythrin, phycocyanin and phycoerythrocyanin; phycobilisome rod ... |
5-161 | 1.90e-17 | ||||
Alpha subunits of phycoerythrin, phycocyanin and phycoerythrocyanin; phycobilisome rod components; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 271284 Cd Length: 161 Bit Score: 74.57 E-value: 1.90e-17
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Apl | cd12130 | Allophycocyanin-like globins; phycobilisomes (PBSs) are the main light-harvesting complex in ... |
7-160 | 1.18e-16 | ||||
Allophycocyanin-like globins; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). This subfamily contains allophycocyanin-like proteins (Apls), which have conserved the residues critical for chromophore interactions, but may not maintain the proper alpha-beta subunit interactions and tertiary structure of phycobiliproteins. Indeed AplA isolated from Fremyella diplosiphon was not detected in phycobilisomes. As the genes encoding Apls cluster with light-responsive regulatory components, Apls may have photoresponsive regulatory role(s). Pssm-ID: 381268 Cd Length: 154 Bit Score: 72.32 E-value: 1.18e-16
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PE_alpha | cd14769 | Phycoerythrin alpha subunit, a phycobilisome rod component; phycobilisomes (PBSs) are the main ... |
1-161 | 3.88e-16 | ||||
Phycoerythrin alpha subunit, a phycobilisome rod component; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 271302 Cd Length: 164 Bit Score: 71.09 E-value: 3.88e-16
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cpeA | CHL00173 | phycoerythrin alpha subunit; Provisional |
1-161 | 3.79e-13 | ||||
phycoerythrin alpha subunit; Provisional Pssm-ID: 100273 Cd Length: 164 Bit Score: 63.22 E-value: 3.79e-13
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PC-PEC_alpha | cd14770 | Alpha subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components; ... |
1-161 | 4.12e-13 | ||||
Alpha subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae. In general, they consist of a central core and surrounding rods and function to harvest and channel light energy toward the photosynthetic reaction centers within the membrane. They are comprised of phycobiliproteins/chromophorylated proteins (PBPs) maintained together by linker polypeptides. PBPs have different numbers of chromophores, and the basic monomer component (alpha/beta heterodimers) can further oligomerize to ring-shaped trimers (heterohexamers) and hexamers (heterododecamers). Stacked PBP hexamers form both the core and the rods of the PBS; the core is mainly made up by allophycocyanin (APC) while the rods can be composed of the PBPs phycoerythrin (PE), phycocyanin (PC) and phycoerythrocyanin (PEC). Pssm-ID: 271303 Cd Length: 162 Bit Score: 63.33 E-value: 4.12e-13
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cpcA | CHL00170 | phycocyanin alpha subunit; Reviewed |
1-161 | 9.86e-12 | ||||
phycocyanin alpha subunit; Reviewed Pssm-ID: 100270 Cd Length: 162 Bit Score: 59.63 E-value: 9.86e-12
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PBP_PBS-LCM | cd12128 | Phycobiliprotein-like domain of the phycobilisome core-membrane linker polypeptide; ... |
73-154 | 1.15e-11 | ||||
Phycobiliprotein-like domain of the phycobilisome core-membrane linker polypeptide; phycobilisomes (PBSs) are the main light-harvesting complex in cyanobacteria and red algae, they consist of a central core and radiating rods and function to harvest and channel light energy toward the photosynthetic reaction centers (RCs) within the membrane. They are comprised of phycobiliproteins or chromophorylated proteins (PBPs) maintained together by linker polypeptides. LCM is a chromophore-bearing PBS linker protein; it facilitates PBS assembly and functionally connects the PBS to the chlorophyll-containing core-complexes in the photosynthetic membrane. In addition to being a linker polypeptide that stabilizes the PBS architecture, the LCM also serves as a terminal energy acceptor. The single phycocyanobilin (PCB) chromophore of LCM are one of two terminal energy transmitters that transfer excitations from the hundreds of chromophores of the PBS to the RCs within the membrane. Pssm-ID: 381267 [Multi-domain] Cd Length: 172 Bit Score: 59.64 E-value: 1.15e-11
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ApcE | COG5693 | Phycobilisome linker protein ApcE [Energy production and conversion]; |
64-134 | 3.16e-09 | ||||
Phycobilisome linker protein ApcE [Energy production and conversion]; Pssm-ID: 444407 [Multi-domain] Cd Length: 904 Bit Score: 54.74 E-value: 3.16e-09
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apcE | CHL00091 | phycobillisome linker protein |
73-140 | 1.78e-08 | ||||
phycobillisome linker protein Pssm-ID: 164495 [Multi-domain] Cd Length: 877 Bit Score: 52.52 E-value: 1.78e-08
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Blast search parameters | ||||
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