ID   TOXK_CYBMR              Reviewed;         125 AA.
AC   P10410; Q00913;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Killer toxin HM-1;
DE   Flags: Precursor;
GN   Name=HMK;
OS   Cyberlindnera mrakii (Yeast) (Williopsis mrakii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=1004253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 0895 / NCYC 2251 / VTT C-01434;
RX   PubMed=8299957; DOI=10.1016/0378-1119(93)90018-x;
RA   Kimura T., Kitamoto N., Matsuoka K., Nakamura K., Iimura Y., Kito Y.;
RT   "Isolation and nucleotide sequences of the genes encoding killer toxins
RT   from Hansenula mrakii and H. saturnus.";
RL   Gene 137:265-270(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 38-125.
RX   PubMed=3943610; DOI=10.1016/0014-5793(86)80170-3;
RA   Yamamoto T., Imai M., Tachibana K., Mayumi M.;
RT   "Application of monoclonal antibodies to the isolation and characterization
RT   of a killer toxin secreted by Hansenula mrakii.";
RL   FEBS Lett. 195:253-257(1986).
RN   [3]
RP   STRUCTURE BY NMR OF 38-125.
RX   PubMed=8756320; DOI=10.1038/nsb0896-662;
RA   Antuch W., Guntert P., Wuethrich K.;
RT   "Ancestral beta gamma-crystallin precursor structure in a yeast killer
RT   toxin.";
RL   Nat. Struct. Biol. 3:662-665(1996).
CC   -!- FUNCTION: This toxin kills sensitive strains of yeast. It inhibits
CC       beta-1,3-glucan synthesis.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable over a wide pH range.;
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; D13445; BAA02704.1; -; Genomic_DNA.
DR   PIR; A23618; TZHQK.
DR   PDB; 1WKT; NMR; -; A=38-125.
DR   PDBsum; 1WKT; -.
DR   AlphaFoldDB; P10410; -.
DR   BMRB; P10410; -.
DR   SMR; P10410; -.
DR   EvolutionaryTrace; P10410; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; IEA:InterPro.
DR   Gene3D; 2.60.20.20; -; 1.
DR   InterPro; IPR011024; G_crystallin-like.
DR   InterPro; IPR015290; Yeast-kill-tox.
DR   InterPro; IPR038651; Yeast_kill_tox_sf.
DR   Pfam; PF09207; Yeast-kill-tox; 1.
DR   SUPFAM; SSF49695; SSF49695; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..37
FT                   /evidence="ECO:0000269|PubMed:3943610"
FT                   /id="PRO_0000022568"
FT   CHAIN           38..125
FT                   /note="Killer toxin HM-1"
FT                   /id="PRO_0000022569"
FT   DISULFID        45..55
FT   DISULFID        48..109
FT   DISULFID        64..95
FT   DISULFID        86..103
FT   DISULFID        104..110
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   TURN            79..82
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   STRAND          99..104
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   STRAND          106..111
FT                   /evidence="ECO:0007829|PDB:1WKT"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:1WKT"
SQ   SEQUENCE   125 AA;  13539 MW;  8EE4BB0479E38925 CRC64;
     MKFSFVYGLT GFLAATSSAL PSEILSTGYE RSALEKRGDG YLIMCKNCDP NTGSCDWKQN
     WNTCVGIGAN VHWMVTGGST DGKQGCATIW EGSGCVGRST TMCCPANTCC NINTGFYIRS
     YRRVE