##gff-version 3 P22211 UniProtKB Chain 1 790 . . . ID=PRO_0000086445;Note=Nitrogen permease reactivator protein P22211 UniProtKB Domain 438 742 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P22211 UniProtKB Region 1 68 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Region 151 188 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Region 234 258 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Region 276 357 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Region 666 704 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Region 766 790 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Compositional bias 18 68 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Compositional bias 276 356 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Compositional bias 676 690 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22211 UniProtKB Active site 561 561 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P22211 UniProtKB Binding site 444 452 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P22211 UniProtKB Binding site 467 467 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P22211 UniProtKB Modified residue 47 47 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:18980262,ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:18980262,PMID:19779198 P22211 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18980262,ECO:0007744|PubMed:19779198;Dbxref=PMID:18980262,PMID:19779198 P22211 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18980262,ECO:0007744|PubMed:19779198;Dbxref=PMID:18980262,PMID:19779198 P22211 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 259 259 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 288 288 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 292 292 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 334 334 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P22211 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 353 353 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 356 356 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Modified residue 357 357 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18980262,ECO:0007744|PubMed:17330950;Dbxref=PMID:17330950,PMID:18980262 P22211 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Mutagenesis 47 47 . . . Note=Abolishes autophosphorylation%3B when associated with A-257 and A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes autophosphorylation%3B when associated with A-47 and A-357. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Mutagenesis 257 257 . . . Note=Abolishes autophosphorylation. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Mutagenesis 357 357 . . . Note=Abolishes autophosphorylation%3B when associated with A-47 and A-257. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18980262;Dbxref=PMID:18980262 P22211 UniProtKB Sequence conflict 154 154 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P22211 UniProtKB Sequence conflict 277 277 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305