ID   MMM1_NEOFI              Reviewed;         496 AA.
AC   A1DLT0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=NFIA_050960;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW15751.1; -; Genomic_DNA.
DR   RefSeq; XP_001257648.1; XM_001257647.1.
DR   AlphaFoldDB; A1DLT0; -.
DR   SMR; A1DLT0; -.
DR   STRING; 36630.CADNFIAP00004275; -.
DR   EnsemblFungi; EAW15751; EAW15751; NFIA_050960.
DR   GeneID; 4584163; -.
DR   KEGG; nfi:NFIA_050960; -.
DR   VEuPathDB; FungiDB:NFIA_050960; -.
DR   eggNOG; ENOG502QUUW; Eukaryota.
DR   HOGENOM; CLU_032730_1_0_1; -.
DR   OMA; KWFVERC; -.
DR   OrthoDB; 1248004at2759; -.
DR   Proteomes; UP000006702; 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..496
FT                   /note="Maintenance of mitochondrial morphology protein 1"
FT                   /id="PRO_0000384238"
FT   TOPO_DOM        1..22
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TOPO_DOM        44..496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   DOMAIN          131..388
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   REGION          50..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  53680 MW;  B87B95265056D985 CRC64;
     MSSQLNDPTP IPAQSSLSFT QGFLLGQLSV VLLIAAFIKF FIFGEAPPPP SRGLSHRSAT
     HRRSNSIYSS TQHDGNTRTL REKPSNSNVL RPVPSSATNT RSILRKTYYT AIPTNPSSKH
     GRHRIHHSSH QPESLDWFNV LIAQTIAQYR QTAYLLKDSP TSSILSSLTA ALNNPEKKPS
     FIDKITVTDI SLGEEFPIFS NCRIIAVDDP NSDGGRLQAL MDVDLSDDNL SIAIETQLLL
     NYPKPCSAIL PVALSISVVR FSGTLCISLV PASTPPLDTP SHSPSPPTAQ TTTTGRSKRE
     DQTGGSHSRA GGSSEEPSGE NPPKTSPKSN VAFSFLPDYR LDLSVRSLIG SRSRLQDVPK
     VAQLVEARVH AWFEERVVEP RVQVVGLPDL WPRMGRTGVR TGDDSETGSN APRSSTAADA
     SGPAHHEDSS REPEVLRFGS LLGTRPPFDL ASRTSSFNVE TGDLRSRSMT REESSGNLSD
     QFHMPGSLPG GGVTTT