ID   MZM1_PHANO              Reviewed;         115 AA.
AC   Q0UIG9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Mitochondrial zinc maintenance protein 1, mitochondrial;
DE   Flags: Precursor;
GN   Name=MZM1; ORFNames=SNOG_08445;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Assembly factor required for Rieske Fe-S protein RIP1
CC       incorporation into the cytochrome b-c1 (CIII) complex. Functions as a
CC       chaperone, binding to this subunit within the mitochondrial matrix and
CC       stabilizing it prior to its translocation and insertion into the late
CC       CIII dimeric intermediate within the mitochondrial inner membrane.
CC       Modulates the mitochondrial matrix zinc pool (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RIP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I LYR family. MZM1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH445336; EAT84721.2; -; Genomic_DNA.
DR   RefSeq; XP_001798756.1; XM_001798704.1.
DR   AlphaFoldDB; Q0UIG9; -.
DR   SMR; Q0UIG9; -.
DR   STRING; 13684.SNOT_08445; -.
DR   PRIDE; Q0UIG9; -.
DR   EnsemblFungi; SNOT_08445; SNOT_08445; SNOG_08445.
DR   GeneID; 5975654; -.
DR   KEGG; pno:SNOG_08445; -.
DR   eggNOG; ENOG502S6EF; Eukaryota.
DR   HOGENOM; CLU_147114_2_2_1; -.
DR   InParanoid; Q0UIG9; -.
DR   OrthoDB; 1585902at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IBA:GO_Central.
DR   CDD; cd20267; Complex1_LYR_LYRM7; 1.
DR   InterPro; IPR008011; Complex1_LYR_dom.
DR   InterPro; IPR045298; Complex1_LYR_LYRM7.
DR   Pfam; PF05347; Complex1_LYR; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..115
FT                   /note="Mitochondrial zinc maintenance protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000405507"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   115 AA;  12916 MW;  7D78D0C4A5816B2A CRC64;
     MSREMALVAY RNLLRSARVA FQGDMNTLFA ARAEVRRNFE SNRSLTAGSD ELSKQLTHAE
     EVAKFLRENV VQGQAADDEG SYKLRIHEHT ERGNNEDIRK GKGKSTLGRV KCCSS