ID   MZM1_VERA1              Reviewed;         109 AA.
AC   C9SBR9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Mitochondrial zinc maintenance protein 1, mitochondrial;
DE   Flags: Precursor;
GN   Name=MZM1; ORFNames=VDBG_01912;
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985215; EEY15803.1; -; Genomic_DNA.
DR   RefSeq; XP_003007724.1; XM_003007678.1.
DR   AlphaFoldDB; C9SBR9; -.
DR   SMR; C9SBR9; -.
DR   STRING; 526221.C9SBR9; -.
DR   EnsemblFungi; EEY15803; EEY15803; VDBG_01912.
DR   GeneID; 9535351; -.
DR   KEGG; val:VDBG_01912; -.
DR   eggNOG; ENOG502S6EF; Eukaryota.
DR   HOGENOM; CLU_147114_2_2_1; -.
DR   OMA; KYKLRIH; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IEA:InterPro.
DR   CDD; cd20267; Complex1_LYR_LYRM7; 1.
DR   InterPro; IPR045298; Complex1_LYR_LYRM7.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..109
FT                   /note="Mitochondrial zinc maintenance protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000405519"
FT   REGION          68..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   109 AA;  11980 MW;  739FFA2CFEB30CE1 CRC64;
     MTALVAYRNL WRAANIAFQG DAPVLAAARQ QIRDNFREKS TLPANDPTIQ PMIEKAEEVA
     KFLRHNLVQG QPQGNDSFKL RIHKDTERGD NDSIKTAGQG KSSGGCCQG