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MAK16_YEAST
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   03-AUG-2022, entry version 174.
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=4; IntAct=EBI-10937, EBI-5640;
CC       P10962; P39744: NOC2; NbExp=3; IntAct=EBI-10937, EBI-29259;
CC       P10962; P38805: RPF1; NbExp=3; 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}.
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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   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   AlphaFoldDB; P10962; -.
DR   SMR; P10962; -.
DR   BioGRID; 31741; 355.
DR   DIP; DIP-6521N; -.
DR   IntAct; P10962; 13.
DR   MINT; P10962; -.
DR   STRING; 4932.YAL025C; -.
DR   iPTMnet; P10962; -.
DR   MaxQB; P10962; -.
DR   PaxDb; P10962; -.
DR   PRIDE; P10962; -.
DR   EnsemblFungi; YAL025C_mRNA; YAL025C; YAL025C.
DR   GeneID; 851208; -.
DR   KEGG; sce:YAL025C; -.
DR   SGD; S000000023; MAK16.
DR   VEuPathDB; FungiDB:YAL025C; -.
DR   eggNOG; KOG3064; Eukaryota.
DR   GeneTree; ENSGT00390000012859; -.
DR   HOGENOM; CLU_050888_0_1_1; -.
DR   InParanoid; P10962; -.
DR   OMA; GTYRDIY; -.
DR   BioCyc; YEAST:G3O-28836-MON; -.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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   InterPro; IPR029004; L28e/Mak16.
DR   InterPro; IPR006958; Mak16.
DR   Pfam; PF04874; Mak16; 1.
DR   Pfam; PF01778; Ribosomal_L28e; 1.
DR   PIRSF; PIRSF003352; MAK16; 1.
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        197..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..250
FT                   /note="Basic and acidic 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           4..11
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          48..58
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           86..96
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           102..116
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            117..120
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           121..126
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           149..156
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           158..170
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:6EM3"
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
 
 
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