ZEAM_MAIZE
ID ZEAM_MAIZE Reviewed; 227 AA.
AC P33679;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Zeamatin;
DE Flags: Precursor;
GN Name=Zlp;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73; TISSUE=Seed;
RX PubMed=7846159; DOI=10.1104/pp.106.4.1471;
RA Malehorn D.E., Borgmeyer J.R., Smith C.E., Shah D.M.;
RT "Characterization and expression of an antifungal zeamatin-like protein
RT (Zlp) gene from Zea mays.";
RL Plant Physiol. 106:1471-1481(1994).
RN [2]
RP PROTEIN SEQUENCE OF 21-48.
RA Roberts W.K., Selitrennikoff C.P.;
RT "Zeamatin, an antifungal protein from maize with membrane-permeabilizing
RT activity.";
RL J. Gen. Microbiol. 136:1771-1778(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8548448; DOI=10.1038/nsb0196-19;
RA Batalia M.A., Monzingo A.F., Ernst S., Roberts W., Robertus J.D.;
RT "The crystal structure of the antifungal protein zeamatin, a member of the
RT thaumatin-like, PR-5 protein family.";
RL Nat. Struct. Biol. 3:19-23(1996).
CC -!- FUNCTION: Has antifungal activity. Inhibits Candida albicans and
CC Trichoderma reesei; marginal inhibition observed against Alternaria
CC solani and Neurospora crassa.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699}.
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DR EMBL; U06831; AAA92882.1; -; mRNA.
DR PIR; JS0646; JS0646.
DR PIR; T02075; T02075.
DR RefSeq; NP_001105356.1; NM_001111886.1.
DR PDB; 1DU5; X-ray; 2.50 A; A/B=22-227.
DR PDBsum; 1DU5; -.
DR AlphaFoldDB; P33679; -.
DR SMR; P33679; -.
DR STRING; 4577.GRMZM2G374971_P01; -.
DR PaxDb; P33679; -.
DR PRIDE; P33679; -.
DR EnsemblPlants; Zm00001eb325340_T001; Zm00001eb325340_P001; Zm00001eb325340.
DR GeneID; 542299; -.
DR Gramene; Zm00001eb325340_T001; Zm00001eb325340_P001; Zm00001eb325340.
DR KEGG; zma:542299; -.
DR MaizeGDB; 78797; -.
DR eggNOG; ENOG502QV4N; Eukaryota.
DR HOGENOM; CLU_043181_5_0_1; -.
DR OMA; ACPVFKK; -.
DR OrthoDB; 1135904at2759; -.
DR EvolutionaryTrace; P33679; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; P33679; baseline and differential.
DR Genevisible; P33679; ZM.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:AgBase.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051841; P:positive regulation by host of cytolysis of symbiont cells; IDA:AgBase.
DR Gene3D; 2.60.110.10; -; 1.
DR InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR InterPro; IPR001938; Thaumatin.
DR InterPro; IPR017949; Thaumatin_CS.
DR PANTHER; PTHR31048; PTHR31048; 1.
DR Pfam; PF00314; Thaumatin; 1.
DR PIRSF; PIRSF002703; Thaumatin; 1.
DR PRINTS; PR00347; THAUMATIN.
DR SMART; SM00205; THN; 1.
DR SUPFAM; SSF49870; SSF49870; 1.
DR PROSITE; PS00316; THAUMATIN_1; 1.
DR PROSITE; PS51367; THAUMATIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Plant defense; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 21..227
FT /note="Zeamatin"
FT /id="PRO_0000034047"
FT DISULFID 30..226
FT DISULFID 72..82
FT DISULFID 87..93
FT DISULFID 139..215
FT DISULFID 145..198
FT DISULFID 153..163
FT DISULFID 167..176
FT DISULFID 177..185
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1DU5"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1DU5"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1DU5"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1DU5"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:1DU5"
SQ SEQUENCE 227 AA; 23999 MW; 33ABFE0B1EB781E4 CRC64;
MAGSVAIVGI FVALLAVAGE AAVFTVVNQC PFTVWAASVP VGGGRQLNRG ESWRITAPAG
TTAARIWART GCKFDASGRG SCRTGDCGGV LQCTGYGRAP NTLAEYALKQ FNNLDFFDIS
LIDGFNVPMS FLPDGGSGCS RGPRCAVDVN ARCPAELRQD GVCNNACPVF KKDEYCCVGS
AANDCHPTNY SRYFKGQCPD AYSYPKDDAT STFTCPAGTN YKVVFCP
