1IST

Crystal structure of yeast cyclophilin A, CPR1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003729	molecular_function	mRNA binding
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
A	0006457	biological_process	protein folding
A	0006974	biological_process	DNA damage response
A	0009267	biological_process	cellular response to starvation
A	0015031	biological_process	protein transport
A	0016018	molecular_function	cyclosporin A binding
A	0016853	molecular_function	isomerase activity
A	0030437	biological_process	ascospore formation
A	0034967	cellular_component	Set3 complex
A	0045835	biological_process	negative regulation of meiotic nuclear division
A	0045836	biological_process	positive regulation of meiotic nuclear division
B	0000413	biological_process	protein peptidyl-prolyl isomerization
B	0003729	molecular_function	mRNA binding
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005758	cellular_component	mitochondrial intermembrane space
B	0006457	biological_process	protein folding
B	0006974	biological_process	DNA damage response
B	0009267	biological_process	cellular response to starvation
B	0015031	biological_process	protein transport
B	0016018	molecular_function	cyclosporin A binding
B	0016853	molecular_function	isomerase activity
B	0030437	biological_process	ascospore formation
B	0034967	cellular_component	Set3 complex
B	0045835	biological_process	negative regulation of meiotic nuclear division
B	0045836	biological_process	positive regulation of meiotic nuclear division

Functional Information from PROSITE/UniProt

site_id	PS00170
Number of Residues	18
Details	CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YagSpFHRVIpdFMlQGG

Chain	Residue	Details
A	TYR46-GLY63

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:2687115, ECO:0000269|PubMed:8431466, ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	GLN3
B	GLN3

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	GLY72
B	GLY72

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	LEU143
B	LEU143

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	PRO146
B	PRO146

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site_id	SWS_FT_FI5
Number of Residues	14
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047

Chain	Residue	Details
A	THR30
B	GLY43
B	HIS124
B	VAL140
B	ALA152
B	SER159
A	GLY43
A	HIS124
A	VAL140
A	ALA152
A	SER159
B	THR30

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