ID   FAKD2_PONAB             Reviewed;         693 AA.
AC   Q5R776;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=FAST kinase domain-containing protein 2, mitochondrial;
DE   Flags: Precursor;
GN   Name=FASTKD2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in assembly of the mitochondrial
CC       large ribosomal subunit. As a component of a functional protein-RNA
CC       module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and
CC       16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA
CC       abundance and is required for intra-mitochondrial translation. May play
CC       a role in mitochondrial apoptosis. {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SUBUNIT: Monomer. Found in a complex with GRSF1, DDX28, DHX30 and
CC       FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA).
CC       Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN,
CC       RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC       {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9NYY8}. Mitochondrion matrix, mitochondrion
CC       nucleoid {ECO:0000250|UniProtKB:Q9NYY8}. Note=Localizes to
CC       mitochondrial RNA granules found in close proximity to the
CC       mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
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DR   EMBL; CR860242; CAH92384.1; -; mRNA.
DR   AlphaFoldDB; Q5R776; -.
DR   STRING; 9601.ENSPPYP00000014655; -.
DR   eggNOG; ENOG502QVSD; Eukaryota.
DR   InParanoid; Q5R776; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; ISS:UniProtKB.
DR   InterPro; IPR013579; FAST_2.
DR   InterPro; IPR010622; FAST_Leu-rich.
DR   InterPro; IPR013584; RAP.
DR   Pfam; PF06743; FAST_1; 1.
DR   Pfam; PF08368; FAST_2; 1.
DR   Pfam; PF08373; RAP; 1.
DR   SMART; SM00952; RAP; 1.
DR   PROSITE; PS51286; RAP; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Mitochondrion nucleoid; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..693
FT                   /note="FAST kinase domain-containing protein 2,
FT                   mitochondrial"
FT                   /id="PRO_0000050785"
FT   DOMAIN          618..675
FT                   /note="RAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
FT   MOD_RES         692
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
SQ   SEQUENCE   693 AA;  79834 MW;  5394164E5A790BBB CRC64;
     MNNKADSFFW NLRQFSTLVP TSRTMRLYRL GLCKPKIVHS NWNILSNFHN RMRSTDIIRY
     LFQDAFIFKS DVGFQTKGIS TLTARRIERL LYARRLFFDS KQSLVPVDKS DDGLKKVNLN
     HEVSNEDVLT KETKPNRISS RKLSQECNSL SDVLDAFSKA PTFPSSNYFT AMWTIAKRLS
     DGQKRFEKRL MFSHPAFNQL CEHMMREAKI MQYKYLLFSL YSMVKLGIPQ NTILVQTLLR
     VTQERINECD ETCLSVLSAV LEAMEPCKNV HVLQMGFRIL VDQQVWKIED VFTLQVVMKC
     IGKDAPIALK RKLEMKALRE LDRFSVLNSQ HMFEVLAAMN HRSLTLLDEC SKVVLDNIHG
     CPLRIMINIL QSCKDLQYHN LDLFKGLADY VAATFDIWKF RKVLFILILF ENLGFRPVGL
     MDLFMKRIVE DPESLNMKNI LPTLHTYSSL NHVYKCQNKE QFLEVMASAL TGYLHTISSE
     NLLHAVYSFC LMNYFPLAPF NQLLQKDVIS ELLTSDDMKN VYKLHMLDTC LKLDDTVYLK
     DIALSLPQLP RELPPSHPNA KVAEVLSSLL GGEGHFSKDV HLPHNYHIDF EIRMDTNRNQ
     VLPLSDVDTT SATDIQRVAV LCVSRSAYCL GSSHPRGFLA MKMRHLNAMG FRVILVNNWE
     MDKLEMEDAV TFLKTKIYSV EALPVAAVNV QST