ID   MIC60_PYRTR             Reviewed;         641 AA.
AC   B2WBQ6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=MICOS complex subunit MIC60;
DE   AltName: Full=Mitofilin;
DE   Flags: Precursor;
GN   Name=MIC60; ORFNames=PTRG_07069;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC       the mitochondrial inner membrane that plays crucial roles in the
CC       maintenance of crista junctions, inner membrane architecture, and
CC       formation of contact sites to the outer membrane. Plays a role in
CC       keeping cristae membranes connected to the inner boundary membrane.
CC       Also promotes protein import via the mitochondrial intermembrane space
CC       assembly (MIA) pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC       {ECO:0000305}.
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DR   EMBL; DS231621; EDU49988.1; -; Genomic_DNA.
DR   RefSeq; XP_001937401.1; XM_001937366.1.
DR   AlphaFoldDB; B2WBQ6; -.
DR   SMR; B2WBQ6; -.
DR   STRING; 45151.EDU49988; -.
DR   EnsemblFungi; EDU49988; EDU49988; PTRG_07069.
DR   GeneID; 6345340; -.
DR   eggNOG; KOG1854; Eukaryota.
DR   HOGENOM; CLU_008024_1_2_1; -.
DR   InParanoid; B2WBQ6; -.
DR   OMA; LQGWAKV; -.
DR   OrthoDB; 1540241at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   PANTHER; PTHR15415; PTHR15415; 1.
DR   Pfam; PF09731; Mitofilin; 2.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..641
FT                   /note="MICOS complex subunit MIC60"
FT                   /id="PRO_0000406672"
FT   TOPO_DOM        17..125
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..641
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          35..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          311..408
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        85..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  70195 MW;  309F44D4267EB990 CRC64;
     MLRASILRAR PAVRPLARAA RPQWHVAQRF YVDDKKNLGE TAVPNPAPTT QPSSSPSNPT
     PVQENTIPAS EVPKGPPAPD STIGASRDAP TTQPSTTPPT GTGTASVAPD PIKPLPKKKR
     RRFRRFLLWL TILSGLGYAG GVWYSLVSDN FHDFFTEYIP YGEDAVAYFE EREFRRRFPG
     RAGEPRLHPQ ISGENKVTIP GRSGLTARPA KENSSDLASR GPHVSAVDDN KKQDKTESGG
     QQPKVSSQTP VAKEQPVQAT ETASSKAITP LDHLNVPSAT EPVVQDVVKI VNDIITVVNA
     DNAHDGKYNS ALDKAKSELT KVVSDINAMK ETLEQQAEAK VKAAHAEFDQ AAKELIQRLD
     HQMQAQETQF KEEFENERER LSQSYKERLQ SELQAAQKVY EQSLKNRLLE QSIKMQKSFT
     ATVRERVEAE REGRLGKLNE LSSSVHELEK LTAEWNSVVD ANLKTQHLVV AVEAVKSALE
     TQVVPKPFVT ELAALKEIAA DDPVVSAAIA SINPAAYQRG IPSSALLIDR FRRVAGEVRK
     AALLPEDAGM ASHLASLAMS KVLFKKSGLA VGADVEAVLA RTEVLLEEGD LDAAAREMNG
     LQGWAKVLSK DWLSECRRVL EVKQALDVIA TEARLNSLLI D