##gff-version 3
P92919	UniProtKB	Transit peptide	1	35	.	.	.	Note=Chloroplast;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P92919	UniProtKB	Chain	36	264	.	.	.	ID=PRO_0000003646;Note=Chlorophyll a-b binding protein%2C chloroplastic	
P92919	UniProtKB	Transmembrane	98	118	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P92919	UniProtKB	Transmembrane	150	170	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P92919	UniProtKB	Transmembrane	218	238	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P92919	UniProtKB	Binding site	56	56	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	78	78	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	84	84	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	97	97	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	100	100	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	102	102	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	135	135	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	145	145	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	151	151	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	155	155	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	163	163	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	163	163	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P07371	
P92919	UniProtKB	Binding site	171	171	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	174	174	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	180	180	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	211	211	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	212	212	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	215	215	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	217	217	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	229	229	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	244	244	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12333	
P92919	UniProtKB	Binding site	253	253	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Binding site	260	260	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Modified residue	36	36	.	.	.	Note=N2-acetylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P92919	UniProtKB	Modified residue	38	38	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250