ID MAK16_YEAST Reviewed; 306 AA. AC P10962; D6VPJ3; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 02-SEP-2026, entry version 190. DE RecName: Full=Protein MAK16; DE AltName: Full=Maintenance of killer protein 16; GN Name=MAK16; OrderedLocusNames=YAL025C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=3045810; DOI=10.1073/pnas.85.16.6007; RA Wickner R.B.; RT "Host function of MAK16: G1 arrest by a mak16 mutant of Saccharomyces RT cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 85:6007-6011(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809; RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., RA Storms R.K.; RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995). RN [3] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 250. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). CC -!- FUNCTION: Its role might be as part of the apparatus concerned with the CC nuclear events of the cell cycle. {ECO:0000269|PubMed:3045810}. CC -!- INTERACTION: CC P10962; Q06218: DBP9; NbExp=5; IntAct=EBI-10937, EBI-5640; CC P10962; P39744: NOC2; NbExp=3; IntAct=EBI-10937, EBI-29259; CC P10962; Q07896: NOC3; NbExp=3; IntAct=EBI-10937, EBI-36093; CC P10962; P40693: RLP7; NbExp=3; IntAct=EBI-10937, EBI-15415; CC P10962; P38805: RPF1; NbExp=4; IntAct=EBI-10937, EBI-24614; CC P10962; P34241: URB1; NbExp=3; IntAct=EBI-10937, EBI-26595; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the MAK16 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J03852; AAA34752.1; -; Genomic_DNA. DR EMBL; U12980; AAC05007.1; -; Genomic_DNA. DR EMBL; BK006935; DAA06963.2; -; Genomic_DNA. DR PIR; A35588; BVBYK6. DR RefSeq; NP_009377.2; NM_001178170.2. DR PDB; 5Z3G; EM; 3.65 A; Z=1-306. DR PDB; 6C0F; EM; 3.70 A; D=1-306. DR PDB; 6CB1; EM; 4.60 A; D=1-306. DR PDB; 6EM1; EM; 3.60 A; 3=1-306. DR PDB; 6EM3; EM; 3.20 A; 3=1-306. DR PDB; 6EM4; EM; 4.10 A; 3=1-306. DR PDB; 6EM5; EM; 4.30 A; 3=1-306. DR PDB; 7OHS; EM; 4.38 A; 3=1-306. DR PDB; 7OHW; EM; 3.50 A; 3=1-306. DR PDB; 7OHX; EM; 3.30 A; 3=1-306. DR PDB; 8E5T; EM; 4.00 A; D=1-306. DR PDB; 8V83; EM; 2.53 A; R=1-306. DR PDB; 8V84; EM; 2.70 A; R=1-306. DR PDB; 9QJC; EM; 3.20 A; D=1-306. DR AlphaFoldDB; P10962; -. DR EMDB; EMD-12907; -. DR EMDB; EMD-12911; -. DR EMDB; EMD-12912; -. DR EMDB; EMD-27919; -. DR EMDB; EMD-43017; -. DR EMDB; EMD-43021; -. DR EMDB; EMD-53201; -. DR EMDB; EMD-6878; -. DR EMDB; EMD-7324; -. DR SMR; P10962; -. DR BioGRID; 31741; 390. DR DIP; DIP-6521N; -. DR FunCoup; P10962; 1177. DR IntAct; P10962; 62. DR MINT; P10962; -. DR STRING; 4932.YAL025C; -. DR iPTMnet; P10962; -. DR PaxDb; 4932-YAL025C; -. DR PeptideAtlas; P10962; -. DR EnsemblFungi; YAL025C_mRNA; YAL025C; YAL025C. DR GeneID; 851208; -. DR KEGG; sce:YAL025C; -. DR AGR; SGD:S000000023; -. DR SGD; S000000023; MAK16. DR VEuPathDB; FungiDB:YAL025C; -. DR eggNOG; KOG3064; Eukaryota. DR HOGENOM; CLU_050888_0_1_1; -. DR InParanoid; P10962; -. DR OMA; DKGQNFC; -. DR OrthoDB; 10251342at2759; -. DR BioCyc; YEAST:G3O-28836-MONOMER; -. DR BioGRID-ORCS; 851208; 4 hits in 10 CRISPR screens. DR PRO; PR:P10962; -. DR Proteomes; UP000002311; Chromosome I. DR RNAct; P10962; protein. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD. DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central. DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD. DR FunFam; 3.30.390.110:FF:000001; Protein MAK16 homolog; 1. DR Gene3D; 3.30.390.110; -; 1. DR InterPro; IPR006958; Mak16. DR InterPro; IPR029004; Ribosomal_eL28/Mak16. DR PANTHER; PTHR23405; MAINTENANCE OF KILLER 16 MAK16 PROTEIN-RELATED; 1. DR PANTHER; PTHR23405:SF4; PROTEIN MAK16 HOMOLOG; 1. DR Pfam; PF04874; Mak16; 1. DR Pfam; PF01778; Ribosomal_L28e; 1. DR PIRSF; PIRSF003352; MAK16; 1. DR PDBsum; 5Z3G; -. DR PDBsum; 6C0F; -. DR PDBsum; 6CB1; -. DR PDBsum; 6EM1; -. DR PDBsum; 6EM3; -. DR PDBsum; 6EM4; -. DR PDBsum; 6EM5; -. DR PDBsum; 7OHS; -. DR PDBsum; 7OHW; -. DR PDBsum; 7OHX; -. DR PDBsum; 8E5T; -. DR PDBsum; 8V83; -. DR PDBsum; 8V84; -. DR PDBsum; 9QJC; -. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Nucleus; Reference proteome; Repeat. FT CHAIN 1..306 FT /note="Protein MAK16" FT /id="PRO_0000203793" FT REPEAT 213..220 FT /note="1" FT REPEAT 222..229 FT /note="2" FT REGION 194..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 213..229 FT /note="2 X 8 AA repeats" FT REGION 251..264 FT /note="7 X 2 AA repeats of S-[DE]" FT MOTIF 139..144 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 282..287 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 194..233 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..245 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..265 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 270..284 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 250 FT /note="E -> Q (in Ref. 1; AAA34752 and 2; AAC05007)" FT /evidence="ECO:0000305" FT HELIX 3..12 FT /evidence="ECO:0007829|PDB:8V83" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:8V83" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:8V83" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:8V83" FT TURN 40..42 FT /evidence="ECO:0007829|PDB:8V83" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:8V83" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:8V83" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:8V83" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 86..96 FT /evidence="ECO:0007829|PDB:8V83" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 102..127 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 139..155 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 158..172 FT /evidence="ECO:0007829|PDB:8V83" FT TURN 173..175 FT /evidence="ECO:0007829|PDB:8V83" FT HELIX 184..190 FT /evidence="ECO:0007829|PDB:8V83" SQ SEQUENCE 306 AA; 35696 MW; 309ED6897EA24F73 CRC64; MSDEIVWQVI NQSFCSHRIK APNGQNFCRN EYNVTGLCTR QSCPLANSKY ATVKCDNGKL YLYMKTPERA HTPAKLWERI KLSKNYTKAL QQIDEHLLHW SKFFRHKCKQ RFTKLTQVMI TERRLALREE ERHYVGVAPK VKRREQNRER KALVAAKIEK AIEKELMDRL KSGAYGDKPL NVDEKVWKKI MGQMEEENSQ DEEEDWDEEE ESDDGEVEYV ADDGEGEYVD VDDLEKWLAD SDREASSASE SESDSESESD SDSDEENKNS AKRRKKGTSA KTKRPKVEIE YEEEHEVQNA EQEVAQ //