ID   MMM1_ASPFN              Reviewed;         491 AA.
AC   B8NDR8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=AFLA_055590;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963477; EED51296.1; -; Genomic_DNA.
DR   RefSeq; XP_002378303.1; XM_002378262.1.
DR   AlphaFoldDB; B8NDR8; -.
DR   SMR; B8NDR8; -.
DR   STRING; 5059.CADAFLAP00006168; -.
DR   EnsemblFungi; EED51296; EED51296; AFLA_055590.
DR   VEuPathDB; FungiDB:AFLA_055590; -.
DR   eggNOG; ENOG502QUUW; Eukaryota.
DR   HOGENOM; CLU_032730_1_0_1; -.
DR   OMA; KWFVERC; -.
DR   Proteomes; UP000001875; 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   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..491
FT                   /note="Maintenance of mitochondrial morphology protein 1"
FT                   /id="PRO_0000384213"
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..491
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   DOMAIN          131..384
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   REGION          50..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  52867 MW;  06672B34E9E79BB5 CRC64;
     MTFQQNEPSA VPAQSSLSFT QGFLLGQLSV VLLIGAFIKF FIFGEAPPPP SRGLSHRAST
     HRRSNSIYTI NPNEGTSRSL REKPSTSNVL RPVPSSATNT RSILRKTYYS AIPTNPSGKH
     GRHRIHHSSH QPESLDWFNV LIAQTIAQYR QTAYLLKDDP TSSILSSLTA ALNNPEKKPS
     FIDKIAVTDI SLGEEFPIFS NCRIIAVDDP NSDGGRLQAL LDVDLSDDNL SIAVETSLLL
     NYPKPCSAIL PVALSISIVR FSGTLCISLV PASTPPLHTP SPSPSPPTAD GAVNAGIHPT
     NGSREPTQEA PNAQEESPPK TSPKSNVAFS FLPDYRLDLS VRSLIGSRSR LQDVPKVAQL
     VEARVHSWFE ERVVEPRVQV VGLPDLWPRM GRTGVRTGED SETGSNAASR SAMSADMGNS
     LRADDIGREP DGLRFRGLGA RPPFDSVSRT SSFNVETGGF RSHSMTREGS GGGMSDDFHM
     PGTLPGGAAA N