FAKD5_PONAB
ID FAKD5_PONAB Reviewed; 764 AA.
AC Q5RFI6; Q5R624;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=FAST kinase domain-containing protein 5, mitochondrial;
DE Flags: Precursor;
GN Name=FASTKD5;
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=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the processing of non-canonical
CC mitochondrial mRNA precursors. {ECO:0000250|UniProtKB:Q7L8L6}.
CC -!- SUBUNIT: Found in a complex with GRSF1, DDX28, DHX30 and FASTKD2.
CC Associates with the 12S mitochondrial rRNA (12S mt-rRNA).
CC {ECO:0000250|UniProtKB:Q7L8L6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q7L8L6}. Note=Localizes to mitochondrial RNA
CC granules found in close proximity to the mitochondrial nucleoids.
CC {ECO:0000250|UniProtKB:Q7L8L6}.
CC -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
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DR EMBL; CR857170; CAH89471.1; -; mRNA.
DR EMBL; CR860676; CAH92792.1; -; mRNA.
DR RefSeq; NP_001124632.1; NM_001131160.1.
DR AlphaFoldDB; Q5RFI6; -.
DR GeneID; 100171471; -.
DR KEGG; pon:100171471; -.
DR CTD; 60493; -.
DR InParanoid; Q5RFI6; -.
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:0000963; P:mitochondrial RNA processing; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IEA:InterPro.
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 Acetylation; Mitochondrion; Mitochondrion nucleoid; mRNA processing;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA-binding;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..764
FT /note="FAST kinase domain-containing protein 5,
FT mitochondrial"
FT /id="PRO_0000284982"
FT DOMAIN 697..757
FT /note="RAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT REGION 68..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L8L6"
FT MOD_RES 507
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7L8L6"
FT CONFLICT 186
FT /note="S -> G (in Ref. 1; CAH92792)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="V -> A (in Ref. 1; CAH92792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 86556 MW; BEE5D00C7E19CD39 CRC64;
MAATLKSLKL LRYQAFCSPS AFGAVRSVSY WNASSTQHGG QDPPGHISLC HSAKKVKNIC
STFSSRRIPT TSSARPGLEF SKTSSSKAST LQLGSPRATG IDEENVEVFD SFENLRVFLQ
LRPEYRVHSY SASETSQLLS VSEGELILHK VRVNQNNLQA QVIVDYLCKL SSLPAEQHPV
LLGSTSFALL CQLSVRKIKL FDTQDLINVL KAFVILGIPH SHSMLDVYET KCCHQVWEMS
VDQLLLVADL WRYIGRKVPR FLNICCSYLN LRWKDLSLSQ LVHLIYVIGE NRQVSQDLMQ
KLESLILKYI DLINLEEVGT ICLGFFKSKT NLSEFVMRKI GDLACADMQH LSSHSLVNIV
KMFRFTHVDH INFMKQIGEI APQRIPSLGV QGVMHLTLYC SALRFLDEGV MNAVAASLPP
RVAQCRSKDV AKILWSFGTL NYKPPNAEEF YSSLINEIHR KMPEFNQYPE HLPTCLLGLA
FLEYFPVELI DFALSPGFVR LAQERTKFDL IKELYTLDGT VVIECPDYRG NRLSTHLQRE
GSELLWYLAE KDMNSKPEFL ETVFLLETML GGPQYVKHHM ILPHTRSSDL EVQLDVNLKP
LPFNREATPA ENVAKLKCEH VGVSLTDDLM NQLLKGKARG HFQGKTESEP GQQHMELENK
AAVPLGGSLR NVADKSGAME MAGLCPPACM QTPRMKLAIQ FTNRNQYCYG SRDLLGLHNM
KRRQLARLGY RVVELSYWEW LPLLKRTRLE KLAFLHEKVF TSAL