##gff-version 3 P48591 UniProtKB Chain 1 812 . . . ID=PRO_0000187193;Note=Ribonucleoside-diphosphate reductase large subunit P48591 UniProtKB Domain 12 103 . . . Note=ATP-cone;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00492 P48591 UniProtKB Active site 438 438 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Active site 440 440 . . . Note=Cysteine radical intermediate;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Active site 442 442 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Binding site 16 17 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 22 28 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 64 64 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 68 68 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 213 213 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 228 228 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 237 239 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 267 267 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 274 275 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 438 438 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 442 442 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Binding site 615 618 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23921 P48591 UniProtKB Site 229 229 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Site 455 455 . . . Note=Important for hydrogen atom transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Site 748 748 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Site 749 749 . . . Note=Important for electron transfer;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Site 807 807 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Site 810 810 . . . Note=Interacts with thioredoxin/glutaredoxin;Ontology_term=ECO:0000250;evidence=ECO:0000250 P48591 UniProtKB Modified residue 778 778 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897 P48591 UniProtKB Modified residue 782 782 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897 P48591 UniProtKB Modified residue 786 786 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18327897;Dbxref=PMID:18327897 P48591 UniProtKB Disulfide bond 229 455 . . . Note=Redox-active;Ontology_term=ECO:0000250;evidence=ECO:0000250