sync_2020 protein (Synechococcus sp. CC9311)

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sync_2020

Possible Helix-turn-helix domain of resolvase. (154 aa)

Predicted Functional Partners:

proS

0.606

psb27

0.552

ppa-1

0.535

sync_2019

0.501

purA

0.445

Your Current Organism:

Synechococcus sp. CC9311

NCBI taxonomy Id: 64471
Other names: S. sp. CC9311

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ppa-1	proS	sync_2018	sync_2021	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	0.456
ppa-1	purA	sync_2018	sync_2023	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	0.422
ppa-1	sync_2019	sync_2018	sync_2019	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	Hypothetical protein; Identified by Glimmer2; putative.	0.773
ppa-1	sync_2020	sync_2018	sync_2020	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	Possible Helix-turn-helix domain of resolvase.	0.535
proS	ppa-1	sync_2021	sync_2018	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	0.456
proS	psb27	sync_2021	sync_2022	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	Possible photosystem II Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.	0.725
proS	purA	sync_2021	sync_2023	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	0.598
proS	sync_2020	sync_2021	sync_2020	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	Possible Helix-turn-helix domain of resolvase.	0.606
psb27	proS	sync_2022	sync_2021	Possible photosystem II Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	0.725
psb27	purA	sync_2022	sync_2023	Possible photosystem II Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	0.617
psb27	sync_2020	sync_2022	sync_2020	Possible photosystem II Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.	Possible Helix-turn-helix domain of resolvase.	0.552
purA	ppa-1	sync_2023	sync_2018	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	0.422
purA	proS	sync_2023	sync_2021	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	0.598
purA	psb27	sync_2023	sync_2022	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	Possible photosystem II Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.	0.617
purA	sync_2020	sync_2023	sync_2020	Adenylosuccinate synthetase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.	Possible Helix-turn-helix domain of resolvase.	0.445
sync_2019	ppa-1	sync_2019	sync_2018	Hypothetical protein; Identified by Glimmer2; putative.	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	0.773
sync_2019	sync_2020	sync_2019	sync_2020	Hypothetical protein; Identified by Glimmer2; putative.	Possible Helix-turn-helix domain of resolvase.	0.501
sync_2020	ppa-1	sync_2020	sync_2018	Possible Helix-turn-helix domain of resolvase.	Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.	0.535
sync_2020	proS	sync_2020	sync_2021	Possible Helix-turn-helix domain of resolvase.	prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]	0.606
sync_2020	psb27	sync_2020	sync_2022	Possible Helix-turn-helix domain of resolvase.	Possible photosystem II Psb27 protein; Plays a role in the repair and/or biogenesis of the calcium- manganese-oxide cluster on the lumenal face of the thylakoid membrane. Its presence in a photosystem II (PSII) preparation prevents binding of some small extrinsic subunits and thus assembly of calcium-manganese- oxide cluster.	0.552