ID   MZM1_SCLS1              Reviewed;         111 AA.
AC   A7EDS9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Mitochondrial zinc maintenance protein 1, mitochondrial;
DE   Flags: Precursor;
GN   Name=MZM1; ORFNames=SS1G_03469;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(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; CH476624; EDO00995.1; -; Genomic_DNA.
DR   RefSeq; XP_001595380.1; XM_001595330.1.
DR   AlphaFoldDB; A7EDS9; -.
DR   SMR; A7EDS9; -.
DR   STRING; 665079.A7EDS9; -.
DR   EnsemblFungi; EDO00995; EDO00995; SS1G_03469.
DR   GeneID; 5491683; -.
DR   KEGG; ssl:SS1G_03469; -.
DR   VEuPathDB; FungiDB:sscle_07g056380; -.
DR   eggNOG; ENOG502S6EF; Eukaryota.
DR   HOGENOM; CLU_147114_2_2_1; -.
DR   InParanoid; A7EDS9; -.
DR   OMA; KYKLRIH; -.
DR   Proteomes; UP000001312; 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; IPR045298; Complex1_LYR_LYRM7.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..111
FT                   /note="Mitochondrial zinc maintenance protein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000405515"
FT   REGION          88..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   111 AA;  12331 MW;  2CFD9A5F28ADF1AE CRC64;
     MALEAYRHLL RATRIAFNGD IAILTSARNQ ARSTFLTNRS LTPESPESIA AIAHAEDVAK
     FLRHNVVQGQ KAEGDEKYKL NIHEHTERGD NDTIKMPSGK NVTIDGKTCK D