ID   MATK_CARAN              Reviewed;         504 AA.
AC   Q9GF55;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 55.
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   Cardamine amara (Large bitter-cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Cardamine.
OX   NCBI_TaxID=50461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Koch M., Mitchell-Olds T.;
RT   "Evolutionary analysis of plastidic maturase K and nuclear chalcone
RT   synthase and their utility for phylogenetic reconstructions within the
RT   Brassicaceae.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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; AF144337; AAG43306.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9GF55; -.
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..504
FT                   /note="Maturase K"
FT                   /id="PRO_0000143310"
SQ   SEQUENCE   504 AA;  60333 MW;  F557BF392972C7EF CRC64;
     MEKFQGYLEF DGARQQSFLY PLFFREYIYV LAYDHGLNRL NRNRSIFLEN ADYDKKYSSL
     IVKRLILRMY EQNRLIIPTK DLNQNNFLGH TSLFYYQMIS VLFAVIVEIP FSLRLGSSFE
     GNLFKKSYNL QSIHSIFPFL EDKLSHFNYV LDVVIPYPIH LEILVQTLRY RVKDASSLHF
     LRFCVYEYFN CKNFYIKKKS ILNPRFFLFL YNSHVCEYES IFFFLRKRSS HLRSTSYEVL
     FERIFFYGKI QHFFKVFVNN FPAILGLLKD PFIHYVRYHG RSILATKDTP LLMNKWKYYF
     VNLWQCYFSV WFQSQKVHIK QLSKDNLEFL GYLSSLRLNP LVVRSQMLEN SFLIDNVRIK
     LDSKIPISSI IGSLAKDKFC NVLGHPISKV IWTHSSDSDI LNRFVRICRN ISHYYSGSSK
     KKFLYRIKYI LRLCCVKTLA RKHKSTVRAF LKRLGSGLLE EFLTGEDQVL SLIFPISYYA
     SKRLYRVRIW YLDILYLNDL ANHE