##gff-version 3 Q63942 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Chain 2 219 . . . ID=PRO_0000121090;Note=GTP-binding protein Rab-3D Q63942 UniProtKB Region 190 219 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63942 UniProtKB Motif 49 58 . . . Note=Switch 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63012 Q63942 UniProtKB Motif 80 96 . . . Note=Switch 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63012 Q63942 UniProtKB Compositional bias 193 203 . . . Note=Low complexity;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63942 UniProtKB Compositional bias 209 219 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q63942 UniProtKB Binding site 29 37 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Binding site 31 31 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 32 32 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 33 33 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 34 34 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 35 35 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 36 36 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 36 36 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Binding site 37 37 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 49 49 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 53 53 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 54 54 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 77 77 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 80 80 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 135 138 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Binding site 135 135 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 136 136 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 138 138 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 165 167 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Binding site 166 166 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Binding site 167 167 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Modified residue 86 86 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95716 Q63942 UniProtKB Modified residue 190 190 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20337 Q63942 UniProtKB Modified residue 219 219 . . . Note=Cysteine methyl ester%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9716267;Dbxref=PMID:9716267 Q63942 UniProtKB Lipidation 217 217 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q63942 UniProtKB Lipidation 219 219 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q63942 UniProtKB Sequence conflict 205 205 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305