##gff-version 3 P22147 UniProtKB Chain 1 1528 . . . ID=PRO_0000071395;Note=5'-3' exoribonuclease 1 P22147 UniProtKB Region 1246 1331 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22147 UniProtKB Region 1431 1455 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22147 UniProtKB Region 1470 1528 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22147 UniProtKB Compositional bias 1270 1301 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22147 UniProtKB Compositional bias 1431 1452 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22147 UniProtKB Compositional bias 1474 1516 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22147 UniProtKB Modified residue 1506 1506 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P22147 UniProtKB Modified residue 1510 1510 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17287358,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:17287358,PMID:18407956,PMID:19779198 P22147 UniProtKB Mutagenesis 37 37 . . . Note=Strongly reduces exonuclease activity. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 41 41 . . . Note=Strongly reduces exonuclease activity. H->R%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 86 86 . . . Note=Strongly reduces exonuclease activity. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 87 87 . . . Note=Strongly reduces exonuclease activity. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 93 93 . . . Note=Strongly reduces exonuclease activity. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 97 97 . . . Note=Strongly reduces exonuclease activity. Q->E%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 101 101 . . . Note=Strongly reduces exonuclease activity. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 176 176 . . . Note=Strongly reduces exonuclease activity. E->G P22147 UniProtKB Mutagenesis 178 178 . . . Note=Strongly reduces exonuclease activity. E->D%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 201 201 . . . Note=Strongly reduces exonuclease activity. C->Y%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 206 206 . . . Note=Abolishes exonuclease activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454540;Dbxref=PMID:10454540 P22147 UniProtKB Mutagenesis 208 208 . . . Note=Abolishes exonuclease activity in vitro. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10454540;Dbxref=PMID:10454540 P22147 UniProtKB Mutagenesis 592 592 . . . Note=Strongly reduces exonuclease activity%3B when associated with Y-710. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 710 710 . . . Note=Strongly reduces exonuclease activity%3B when associated with P-592. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 798 798 . . . Note=Strongly reduces exonuclease activity%3B when associated with D-1024%3B F-1043 and P-1197. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 1024 1024 . . . Note=Strongly reduces exonuclease activity%3B when associated with R-798%3B F-1043 and P-1197. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 1043 1043 . . . Note=Strongly reduces exonuclease activity%3B when associated with R-798%3B D-1024 and P-1197. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486 P22147 UniProtKB Mutagenesis 1197 1197 . . . Note=Strongly reduces exonuclease activity%3B when associated with R-798%3B D-1024 and F-1043. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9685486;Dbxref=PMID:9685486