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Database: UniProt
Entry: A0A0C3QUH9_9AGAM
LinkDB: A0A0C3QUH9_9AGAM
Original site: A0A0C3QUH9_9AGAM 
ID   A0A0C3QUH9_9AGAM        Unreviewed;        92 AA.
AC   A0A0C3QUH9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000256|RuleBase:RU368087};
GN   ORFNames=M407DRAFT_241556 {ECO:0000313|EMBL:KIO32114.1};
OS   Tulasnella calospora MUT 4182.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Tulasnellaceae; Tulasnella.
OX   NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO32114.1, ECO:0000313|Proteomes:UP000054248};
RN   [1] {ECO:0000313|EMBL:KIO32114.1, ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO32114.1,
RC   ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RA   Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA   Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits the enzyme activity of ATPase.
CC       {ECO:0000256|RuleBase:RU368087}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the ATPase inhibitor family.
CC       {ECO:0000256|ARBA:ARBA00010901, ECO:0000256|RuleBase:RU368087}.
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DR   EMBL; KN822957; KIO32114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3QUH9; -.
DR   STRING; 1051891.A0A0C3QUH9; -.
DR   HOGENOM; CLU_145563_3_0_1; -.
DR   OrthoDB; 1664632at2759; -.
DR   Proteomes; UP000054248; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042030; F:ATPase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   InterPro; IPR007648; ATPase_inhibitor_mt.
DR   Pfam; PF04568; IATP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054248}.
FT   COILED          50..84
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   92 AA;  10368 MW;  E18AEE4FE295ABF4 CRC64;
     MFTATRLARR LPALRGIAKR SYSDGRVAGA TANSREFSKK EKAHEDQYIR LHEKEQLEKL
     RKLIAKQEAD LANLKQQVEE QGKKTNGGSG SQ
//
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