ID   MATK_GRAOF              Reviewed;         510 AA.
AC   Q7YKQ3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Maturase K {ECO:0000255|HAMAP-Rule:MF_01390};
DE   AltName: Full=Intron maturase {ECO:0000255|HAMAP-Rule:MF_01390};
GN   Name=matK {ECO:0000255|HAMAP-Rule:MF_01390};
OS   Gratiola officinalis (Hedgehyssop).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Gratioleae; Gratiola.
OX   NCBI_TaxID=204382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15248131; DOI=10.1055/s-2004-817909;
RA   Mueller K.F., Borsch T., Legendre L., Porembski S., Theisen I.,
RA   Barthlott W.;
RT   "Evolution of carnivory in lentibulariaceae and the Lamiales.";
RL   Plant Biol. 6:477-490(2004).
CC   -!- FUNCTION: Usually encoded in the trnK tRNA gene intron. Probably
CC       assists in splicing its own and other chloroplast group II introns.
CC       {ECO:0000255|HAMAP-Rule:MF_01390}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01390}.
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DR   EMBL; AF531777; AAP87837.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YKQ3; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   HAMAP; MF_01390; MatK; 1.
DR   InterPro; IPR024937; Domain_X.
DR   InterPro; IPR002866; Maturase_MatK.
DR   InterPro; IPR024942; Maturase_MatK_N.
DR   PANTHER; PTHR34811; PTHR34811; 1.
DR   Pfam; PF01348; Intron_maturas2; 1.
DR   Pfam; PF01824; MatK_N; 1.
PE   3: Inferred from homology;
KW   Chloroplast; mRNA processing; Plastid; RNA-binding; tRNA processing.
FT   CHAIN           1..510
FT                   /note="Maturase K"
FT                   /id="PRO_0000143410"
SQ   SEQUENCE   510 AA;  60348 MW;  09E730121FDCF24E CRC64;
     MEEIQRYLQL ERYHQHDFLY PLIFQEYIYT FAHDRDYNRS ILSENSCYEK KFSLLIVKRL
     ITRMYQQNHF LIFSNDSNQN PFEGRNKNFY FQIISEGFAL IAEIPFSRRL RASLKEKKIV
     KFQNLRSIQA IFSFLEDSFS HLNFVLDILI PHSVHVEILV QTLRYWVKDA SSLHLLRFFL
     NEYCNSNSLI TPKEVSSSFS TKRNKRLFLF LYNSHVCEYE SILVFLRKQS SHLRSTSSGL
     LLERIYFYAK IERLVNLFVK VKGFQVNLWL VKEPCMHYVR YQRKSIWASN GASLLIKKWK
     SYLVAFWQWH FSMWFHPRRI SINQLSNHSL EFLGYHSSVR MNPSVVRSQS LENSFLINNA
     LKKFDTLVPI ISLIAALAQA KFCNVLGDPI SKPVWADLSD SNIIYRFGHI CRNLSHYYSG
     SSKKNSLYRI KYILRLSCAR TLARKHKSTV RAFLKKLGSE LLEEFLMSEK DVLSLTFPKA
     SSIFGGGYRR QIWYLDIISI NDLANHKSKF