ID   MMM1_AJECG              Reviewed;         591 AA.
AC   C0NZU3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN   Name=MMM1 {ECO:0000255|HAMAP-Rule:MF_03103}; ORFNames=HCBG_08673;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC       molecular tether to connect the endoplasmic reticulum (ER) and
CC       mitochondria. Components of this complex are involved in the control of
CC       mitochondrial shape and protein biogenesis, and function in
CC       nonvesicular lipid trafficking between the ER and mitochondria. The
CC       MDM12-MMM1 subcomplex functions in the major beta-barrel assembly
CC       pathway that is responsible for biogenesis of all outer membrane beta-
CC       barrel proteins, and acts in a late step after the SAM complex. The
CC       MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway
CC       after the action of the MDM12-MMM1 complex. Essential for establishing
CC       and maintaining the structure of mitochondria and maintenance of mtDNA
CC       nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}.
CC   -!- SUBUNIT: Homodimer. Component of the ER-mitochondria encounter
CC       structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and
CC       MDM34. A MMM1 homodimer associates with one molecule of MDM12 on each
CC       side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1
CC       and MDM12 generate a continuous hydrophobic tunnel for phospholipid
CC       trafficking. {ECO:0000255|HAMAP-Rule:MF_03103}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03103}. Note=The ERMES/MDM complex localizes
CC       to a few discrete foci (around 10 per single cell), that represent
CC       mitochondria-endoplasmic reticulum junctions. These foci are often
CC       found next to mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}.
CC   -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC       various types of glycerophospholipids in its interior and mediate their
CC       transfer between two adjacent bilayers. {ECO:0000255|HAMAP-
CC       Rule:MF_03103}.
CC   -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03103}.
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DR   EMBL; GG663379; EEH03033.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NZU3; -.
DR   SMR; C0NZU3; -.
DR   STRING; 447093.C0NZU3; -.
DR   EnsemblFungi; EEH03033; EEH03033; HCBG_08673.
DR   VEuPathDB; FungiDB:HCBG_08673; -.
DR   HOGENOM; CLU_032730_2_0_1; -.
DR   InParanoid; C0NZU3; -.
DR   OrthoDB; 1248004at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03103; Mmm1; 1.
DR   InterPro; IPR027537; Mmm1.
DR   InterPro; IPR019411; MMM1_dom.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR13466:SF5; PTHR13466:SF5; 1.
DR   Pfam; PF10296; MMM1; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..591
FT                   /note="Maintenance of mitochondrial morphology protein 1"
FT                   /id="PRO_0000384208"
FT   TOPO_DOM        1..83
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TOPO_DOM        105..591
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   DOMAIN          192..462
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   REGION          138..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  63165 MW;  9105E3F6371905A3 CRC64;
     MGFNIPWNGT QAEYHVTHCF LPSDKIDLIS FSTSTSQFCN GRPFKFVPAA LPSILPQAKP
     ITTDQTQAPP PALAQPSLSF TQGLLVGQLS VVLLIGAFIK FFIFGEAPPP PSRSGLYNRT
     SSHRRSYSIN AISTDFSPRT LREKPSTSNI LRPVPSSSTN TRSILRKTYY SATPTNPTSK
     HGRSRVHHSS HQPESLDWFN VLIAQTIAQY RQTAYILKDS PTSSILASLS EALNNPEKKP
     SFIDTIKVTD ISLGEEFPIF SNCRVIAVED PNSDGGRLQA LMDVDLSDDN LSLAVETSLL
     LNYPKPFSAV LPVALAVSVV RFSGTLCISF VPGPGTSDQT MGPSASPPNQ STSTETASIN
     DQTSEGQSTQ RHTFHQHKPT NSTPTAATAD DAHTKHAHGI PKTSLAFSFL PDYRLDLSVR
     SLIGSRSRLQ DVPKVAQLVE ARMQAWFEER VVEPRVQVVG LPNIWPRMGR TGVRGSQEEA
     EARAGVGSVP VDIPGTAGGD GMRGRGGGGG GGGLRGNSSG RGMGYDGLRY RPNAHGDGGT
     GVVQGQGAGG IFCEAGPQNQ NRGGDDGEGP GRRSDERFAM PGSMPDSVAV T