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Conserved domains on  [gi|46946460|emb|CAD90038|]
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C-phycocyanin alpha subunit, partial [Planktothrix agardhii CCAP 1459/21]

Protein Classification

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

CATH:  1.10.490.10
Gene Ontology:  GO:0019825|GO:0020037
SCOP:  3000554

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpcA super family cl46744
Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion];
1-50 1.79e-25

Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion];


The actual alignment was detected with superfamily member COG5687:

Pssm-ID: 444401  Cd Length: 162  Bit Score: 90.51  E-value: 1.79e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 46946460   1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:COG5687   1 MKTPLTEAIAAADSQGRFLSSTELQSVFGRFQRAAARLEAAKALAANADS 50
 
Name Accession Description Interval E-value
CpcA COG5687
Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion];
1-50 1.79e-25

Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion];


Pssm-ID: 444401  Cd Length: 162  Bit Score: 90.51  E-value: 1.79e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 46946460   1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:COG5687   1 MKTPLTEAIAAADSQGRFLSSTELQSVFGRFQRAAARLEAAKALAANADS 50
PC-PEC_alpha cd14770
Alpha subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components; ...
1-50 5.40e-25

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: 89.52  E-value: 5.40e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 46946460   1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:cd14770   1 MKTPLTEAIAAADSQGRFLSNTELQAAFGRFRRATASLEAARALTSNADS 50
cpcA CHL00170
phycocyanin alpha subunit; Reviewed
1-48 4.97e-17

phycocyanin alpha subunit; Reviewed


Pssm-ID: 100270  Cd Length: 162  Bit Score: 69.26  E-value: 4.97e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 46946460    1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKS 48
Cdd:CHL00170   1 MKTPITEAIASADSQGRFLSNGELQACNGRFQRAAASLEAARSLTSNA 48
Phycobilisome pfam00502
Phycobilisome protein;
7-50 1.10e-11

Phycobilisome protein;


Pssm-ID: 425723 [Multi-domain]  Cd Length: 155  Bit Score: 55.19  E-value: 1.10e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 46946460     7 EAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:pfam00502   1 EVIAAADAEGRYLSDGELEALKGFFQSGEARLEAANALASNADE 44
 
Name Accession Description Interval E-value
CpcA COG5687
Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion];
1-50 1.79e-25

Phycocyanin alpha chain, CpcA/CpeB [Energy production and conversion];


Pssm-ID: 444401  Cd Length: 162  Bit Score: 90.51  E-value: 1.79e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 46946460   1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:COG5687   1 MKTPLTEAIAAADSQGRFLSSTELQSVFGRFQRAAARLEAAKALAANADS 50
PC-PEC_alpha cd14770
Alpha subunits of phycoerythrin and phycoerythrocyanin; phycobilisome rod components; ...
1-50 5.40e-25

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: 89.52  E-value: 5.40e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 46946460   1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:cd14770   1 MKTPLTEAIAAADSQGRFLSNTELQAAFGRFRRATASLEAARALTSNADS 50
cpcA CHL00170
phycocyanin alpha subunit; Reviewed
1-48 4.97e-17

phycocyanin alpha subunit; Reviewed


Pssm-ID: 100270  Cd Length: 162  Bit Score: 69.26  E-value: 4.97e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 46946460    1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKS 48
Cdd:CHL00170   1 MKTPITEAIASADSQGRFLSNGELQACNGRFQRAAASLEAARSLTSNA 48
PE-PC-PEC_alpha cd12129
Alpha subunits of phycoerythrin, phycocyanin and phycoerythrocyanin; phycobilisome rod ...
2-50 7.94e-14

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: 60.70  E-value: 7.94e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 46946460   2 KTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:cd12129   1 KTPITEAIAAADAAGRFLSNTELQAVQGRFQRAAARLEAARALANNHEA 49
Phycobilisome pfam00502
Phycobilisome protein;
7-50 1.10e-11

Phycobilisome protein;


Pssm-ID: 425723 [Multi-domain]  Cd Length: 155  Bit Score: 55.19  E-value: 1.10e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 46946460     7 EAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:pfam00502   1 EVIAAADAEGRYLSDGELEALKGFFQSGEARLEAANALASNADE 44
PE_alpha cd14769
Phycoerythrin alpha subunit, a phycobilisome rod component; phycobilisomes (PBSs) are the main ...
1-50 1.47e-05

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: 39.11  E-value: 1.47e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 46946460   1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:cd14769   1 MKSVITTVISAADAAGRFPSSSDLESVQGNIQRAAARLEAAEKLAANHEA 50
PBP-like cd08919
Phycobiliproteins (PBPs) and related proteins; phycobilisomes (PBSs) are the main ...
4-50 3.10e-05

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: 38.04  E-value: 3.10e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 46946460   4 PLTEAVTTADSqGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:cd08919   1 ALTKLIAEADG-GRYLSSSELQALKGYIQSAEARLEAAEKLRENAEE 46
cpeA CHL00173
phycoerythrin alpha subunit; Provisional
1-50 1.39e-04

phycoerythrin alpha subunit; Provisional


Pssm-ID: 100273  Cd Length: 164  Bit Score: 36.64  E-value: 1.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 46946460    1 MKTPLTEAVTTADSQGRFLSSTEIQVAFGRFRQAKAGLEAAKALTAKSDS 50
Cdd:CHL00173   1 MKSVITTTISAADAAGRFPSSSDLESVQGNIQRAAARLEAAEKLASNHEA 50
 
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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