ID   SHE10_CANGA             Reviewed;         556 AA.
AC   Q6FQR7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=CAGL0I04092g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380955; CAG60364.1; -; Genomic_DNA.
DR   RefSeq; XP_447427.1; XM_447427.1.
DR   AlphaFoldDB; Q6FQR7; -.
DR   SMR; Q6FQR7; -.
DR   STRING; 5478.XP_447427.1; -.
DR   EnsemblFungi; CAG60364; CAG60364; CAGL0I04092g.
DR   GeneID; 2889099; -.
DR   KEGG; cgr:CAGL0I04092g; -.
DR   CGD; CAL0132508; CAGL0I04092g.
DR   VEuPathDB; FungiDB:CAGL0I04092g; -.
DR   eggNOG; ENOG502QT2T; Eukaryota.
DR   HOGENOM; CLU_023952_1_0_1; -.
DR   InParanoid; Q6FQR7; -.
DR   OMA; MINEWSK; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
PE   3: Inferred from homology;
KW   Coiled coil; Mitochondrion; Reference proteome; Ribonucleoprotein; Signal;
KW   Sporulation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..556
FT                   /note="Outer spore wall assembly protein SHE10"
FT                   /id="PRO_0000408907"
FT   REGION          190..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          135..201
FT                   /evidence="ECO:0000255"
FT   COILED          481..547
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        190..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  64520 MW;  8D090F23C9935C0D CRC64;
     MRFLTKFLLF LATVYFGLKY ACESPLRAQY PQLQLACHYS QPALWNDYLL KNSPAYKNSV
     HPQLVVAKGK YEELVQPHVK DVCKRVHTQL DRIDKKKYCD LAHSYANLAY QKAQFYYSIS
     AGKYVHDFCK SDLYNKNLKR HVERAKEDLS KAYHLAVVRI PQLFTRENVE KFTSSASAYI
     NEKTESLKKE AKQITSDVKK TVESEIKKRT TSSESEEEPI VSTSTIVKTI TRTRHSSSST
     TSTKSAEETS EKNLETKEEE DITDIEIDHQ AQLQRDFDKW TSNIDKKVKM VNKMLVRDVK
     KHLKPKIDAN DKLFKDKLKV LHKEANDNFQ LINKAIQDIN CTQGIDPETG KQIYFDSEGK
     SQIEKYITRE MIRTMLNDTQ TTLNSLVADI ENDVSKILED FKKIAENSRE QHLTTFEEWG
     DIMINEWSKK LAYLDVLAPH EDAEHEGKSK TELSEKNWKK FMAIKKQILD ARDKMAKRQI
     KISEFKLLLD NVQNTLQAVT NENGEYLYIL RAQANLAFQE RERLEKEAEE AKLRKEAGEV
     NESSEEEQIV EEPISA