ID   SHE10_ASHGO             Reviewed;         572 AA.
AC   Q753T2;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Outer spore wall assembly protein SHE10 {ECO:0000250|UniProtKB:P53075};
DE   AltName: Full=Sensitivity to high expression protein 10 {ECO:0000250|UniProtKB:P53075};
DE   Flags: Precursor;
GN   Name=SHE10 {ECO:0000250|UniProtKB:P53075}; OrderedLocusNames=AFR244C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Involved in spore wall assembly. May be a component of the
CC       mitochondrial RNase MRP (MtMRP), a ribonucleoprotein endoribonuclease
CC       involved in the cleaving RNA transcripts to generate primers for DNA
CC       replication in mitochondria. {ECO:0000250|UniProtKB:P53075}.
CC   -!- SUBUNIT: Component of the mitochondria-localized RNase mitochondrial
CC       RNA-processing (RNase MRP) composed of one single RNA encoded by the
CC       NME1 gene and at least 31 proteins. Absent in the nucleus-localized
CC       RNase MRP (NuMRP). {ECO:0000250|UniProtKB:P53075}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P53075}.
CC   -!- SIMILARITY: Belongs to the SHE10 family. {ECO:0000305}.
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DR   EMBL; AE016819; AAS53615.1; -; Genomic_DNA.
DR   RefSeq; NP_985791.1; NM_211146.1.
DR   AlphaFoldDB; Q753T2; -.
DR   STRING; 33169.AAS53615; -.
DR   EnsemblFungi; AAS53615; AAS53615; AGOS_AFR244C.
DR   GeneID; 4622054; -.
DR   KEGG; ago:AGOS_AFR244C; -.
DR   eggNOG; ENOG502QT2T; Eukaryota.
DR   HOGENOM; CLU_023952_1_0_1; -.
DR   InParanoid; Q753T2; -.
DR   OMA; CKHARAL; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Coiled coil; Mitochondrion; Reference proteome; Ribonucleoprotein; Signal;
KW   Sporulation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..572
FT                   /note="Outer spore wall assembly protein SHE10"
FT                   /id="PRO_0000408906"
FT   REGION          539..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          351..372
FT                   /evidence="ECO:0000255"
FT   COILED          485..510
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        557..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  65094 MW;  81847D8062270BCE CRC64;
     MRAISKLFVF TVLVLGSLQY YCGRYGACPA QIAVISHYTW PCTYAPAVRD KLGKASEWYG
     ANAAPHVSVA SGWMQGKVMP HLTKVSQWTE KHVQPRMRQA GADAIVTARV AWNVVQQYQR
     RHVVPLTGRL LAKCPCLERW AEQAARGWQW LCKHARALAT AVQQQYPAFV AHMGGIWEPL
     HGAYNRIYLD LGRPVQEKTS EDASAAPGGT QYITSTITMT MTSLDELVTV TAEDGLSDVV
     EASFKDLVAD EFSAWQQAIE RKADSVLQAF TEEVGEFEMQ QHEAVAPKFR ALLKHISAKS
     QEHYAKINQA IRDINSTMEL DPATNQTIWF DAHGTQLHQY ITRPLMREYF SQANDELANI
     TNHIRAELRE VVDSVNGQVD VIRQEHIEVY EEWADVMVSE WSRRMAYIDV VDRDLEAEAE
     RNRNWKRFLK LKKRVIKVRD QLLEHPVKFN QLETFLKEIQ STLRILAQEN GEYLYILRSK
     ANLSFQEREK NDRLREQHEQ EAREMTLREQ LSTELAANGT EVIIDTFEVD LDQLLRSNST
     SWSVPPADAR AEPASGSPIQ QAASEAAQQP SV