##gff-version 3 P12904 UniProtKB Chain 1 322 . . . ID=PRO_0000204389;Note=5'-AMP-activated protein kinase subunit gamma P12904 UniProtKB Domain 37 97 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 P12904 UniProtKB Domain 118 181 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 P12904 UniProtKB Domain 194 253 . . . Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 P12904 UniProtKB Domain 262 322 . . . Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 P12904 UniProtKB Binding site 42 42 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 146 146 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 166 169 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 195 195 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 195 195 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3TDH;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 195 195 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3T4N;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 200 200 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3TDH;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 200 200 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3T4N;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 221 222 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 221 222 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3TDH;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 221 222 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3T4N;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 291 293 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 309 312 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q10343 P12904 UniProtKB Binding site 309 312 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3TDH;Dbxref=PMID:22019086 P12904 UniProtKB Binding site 309 312 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22019086,ECO:0007744|PDB:3T4N;Dbxref=PMID:22019086 P12904 UniProtKB Mutagenesis 63 63 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 136 136 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 145 145 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 146 146 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. R->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 166 166 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 177 177 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. N->A%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 242 242 . . . Note=Decreases SNF1-activation efficiency%3B when associated with A-291 and E-293. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223533;Dbxref=PMID:17223533 P12904 UniProtKB Mutagenesis 251 251 . . . Note=Leads to resistance to 2-deoxyglucose. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18474591;Dbxref=PMID:18474591 P12904 UniProtKB Mutagenesis 291 291 . . . Note=Decreases SNF1-activation efficiency%3B when associated with E-242 and E-293. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17223533;Dbxref=PMID:17223533 P12904 UniProtKB Mutagenesis 293 293 . . . Note=Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17223533,ECO:0000269|PubMed:18474591;Dbxref=PMID:17223533,PMID:18474591 P12904 UniProtKB Mutagenesis 293 293 . . . Note=Decreases SNF1-activation efficiency%3B when associated with E-242 and A-291. H->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17223533,ECO:0000269|PubMed:18474591;Dbxref=PMID:17223533,PMID:18474591 P12904 UniProtKB Helix 8 28 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 31 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Beta strand 37 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 50 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Beta strand 65 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Turn 70 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Beta strand 74 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 81 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 95 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 106 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 132 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Beta strand 145 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Turn 154 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Beta strand 159 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 167 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 179 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QLV P12904 UniProtKB Helix 182 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Helix 188 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Helix 208 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Beta strand 221 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Beta strand 231 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Helix 238 246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Helix 249 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 257 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Beta strand 272 274 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3T4N P12904 UniProtKB Helix 280 290 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Beta strand 293 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Beta strand 302 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC P12904 UniProtKB Helix 310 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NYC