ID   AIM21_CANDC             Reviewed;         847 AA.
AC   B9W923;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Altered inheritance of mitochondria protein 21;
GN   Name=AIM21; ORFNames=CD36_09490;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
CC   -!- FUNCTION: Involved in mitochondrial migration along actin filaments.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000250}. Note=Cortical actin patches. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AIM21 family. {ECO:0000305}.
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DR   EMBL; FM992688; CAX45248.1; -; Genomic_DNA.
DR   RefSeq; XP_002417593.1; XM_002417548.1.
DR   AlphaFoldDB; B9W923; -.
DR   SMR; B9W923; -.
DR   STRING; 42374.XP_002417593.1; -.
DR   EnsemblFungi; CAX45248; CAX45248; CD36_09490.
DR   GeneID; 8045140; -.
DR   KEGG; cdu:CD36_09490; -.
DR   CGD; CAL0000170653; Cd36_09490.
DR   VEuPathDB; FungiDB:CD36_09490; -.
DR   eggNOG; ENOG502S25J; Eukaryota.
DR   HOGENOM; CLU_336152_0_0_1; -.
DR   OrthoDB; 1596014at2759; -.
DR   Proteomes; UP000002605; Chromosome 1.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton.
FT   CHAIN           1..847
FT                   /note="Altered inheritance of mitochondria protein 21"
FT                   /id="PRO_0000399516"
FT   REGION          1..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..742
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..773
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  93673 MW;  1DD488AD8CD4A654 CRC64;
     MSDLEPSESL NHESDSHLEQ LKPSTTPSIP ARPQSRPQKQ TTTTTTKVPT DQDSNDKTPL
     EKPQDELDQL AHEIEKVLTD PVIPPRPQHG SSAKPNETQT EHKEQDFGSA HPVIPSRPTN
     KKETIETEMV DQNNGLESKS DSTANKESLE NQVPIDEDST HVKPSIPNVP SRPQNRDLDS
     SEVDNTKAST TPSIPARPQR QTAPTQNEHK PQVSNTPVIP TRPQTKTEKL HLNEELDKLD
     GESSSKNQEN KRHTDDNNTS KPIYEAESIV PPEEKEGETA NKQALPTTST DPPAEPTAST
     RGFRLPLHMQ QSSGPISTST PVTGSEAELN SLDNSNTFGD GEITPGNSDT KATFKSDEDV
     ENNNRTDSSS FDDDMETISQ DQEDREEDRR HRQETTTGEN VQESEDPQFE TTIIESGEIE
     ERDGDDTDSG ELYSEQQQNK EKEDVVPATS TPKIPQRPPK KQSLSRATTD DSLTSLDNTS
     KPPKPVVPKR PTSEESSSNL EPTIPTRPSI KKAPSIGESD PEPIVPNRPG NKELESIPRD
     TQTSIKSKPP PPKPKKLSSK IAAFQQQLFN PMNASSEEDV GSTGSKQPEP GIRKRSTENS
     ILSRFGGKAI PLPGMFNPNQ MPKPSISHGE ETSDDKEEKE EKEENVTANV PVRRTRGPRG
     KKLPKAVADA EIKTESRFTI ESGKLWSLEF KREIKEEKEI GHSDLEKSKI LVDDVEADGD
     GEEKAAENEV IESQENTIGD KLEHNDVVNI ASAAADIDND GDVDDDDDDD VPPEVNERFI
     KDEEISNVGI ERTIASETTT EKHSTDEEVE EEEEELEVDS VDIPIRRVTV NTVDTIEDQK
     DVDDEPL