ID   MDM34_AJECG             Reviewed;         622 AA.
AC   C0NY51;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105}; ORFNames=HCBG_07845;
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. MDM34
CC       is required for the interaction of the ER-resident membrane protein
CC       MMM1 and the outer mitochondrial membrane-resident beta-barrel protein
CC       MDM10. {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC       or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
CC       {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03105}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03105}. Note=The ERMES/MDM complex localizes to a few discrete
CC       foci (around 10 per single cell), that represent mitochondria-
CC       endoplasmic reticulum junctions. These foci are often found next to
CC       mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting that it
CC       resides in the membrane via beta-sheet conformations similar to those
CC       predicted for other outer membrane proteins and porin.
CC       {ECO:0000255|HAMAP-Rule:MF_03105}.
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_03105}.
CC   -!- SIMILARITY: Belongs to the MDM34 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03105}.
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DR   EMBL; GG663376; EEH03719.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NY51; -.
DR   STRING; 447093.C0NY51; -.
DR   EnsemblFungi; EEH03719; EEH03719; HCBG_07845.
DR   VEuPathDB; FungiDB:HCBG_07845; -.
DR   HOGENOM; CLU_036502_1_0_1; -.
DR   InParanoid; C0NY51; -.
DR   OrthoDB; 1120952at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0031307; C:integral component of mitochondrial outer 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   HAMAP; MF_03105; Mdm34; 1.
DR   InterPro; IPR027536; Mdm34.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR28185; PTHR28185; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Lipid-binding; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   CHAIN           1..622
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384320"
FT   DOMAIN          1..195
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT   REGION          211..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..376
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  67803 MW;  1EA12713B5297E33 CRC64;
     MAFNFNWSPL MADAGFYTRA QELLTAALNK SPKPPIIVDD IVVTELNLGS NPPELEILEI
     GDLAEDRFRG IFKMSYAGDA FLTLKTCVQA NPLNTYLLTR HPFASPQPLA AATGLTIPLQ
     ITLSDIKLSG FVILVFSKQK GITVVFRNDP LESLKVSSTF DSIPFVRDYL QKEIEGQLRI
     LFMDELPAII HRLSLRLWGT EYSELETTSA QVTNPPLEGP GLDPLLNPPE DPVDASGNVL
     STSEIASLSL DSGVEMHSLF SRKNVLRLAA LTDSQRTLSL FTPSIQEVVF RAWTGLMEQA
     DGPSGLVSPM SPPLSRTHSH VATSSLSLQD AASLASSSHS RLSLPSTGFS GYGLSMGAGR
     HSKAHARKRK KRVVDLRRRP KNTDDMESVS GESEFTESTS AASVFSGSTI PEENNDDPVT
     PPGSPPRTIR QPTLCDRIVA RNGAERNARR GIPAEFGHDI PASRTTLPTA NDIARMLATT
     SSLQQQLHPA NSKSLPPQVP PQEPALRPSL TSNSPYPIEK PNASNYTSSG DSQQQQQQQQ
     QHQTHLPSSL IMEAAQSGGI LEQAWMMKMA SEIARRIQDE KMGGEDAAGS SNNKNDNKNN
     NTGGFWEQSL MRSHTPPPAY RH