ID   MATK_LEPCM              Reviewed;         504 AA.
AC   Q9GF36;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   07-OCT-2020, entry version 54.
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   Lepidium campestre (Field pepperwort) (Thlaspi campestre).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Lepidieae; Lepidium.
OX   NCBI_TaxID=65351;
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; AF144359; AAG43328.1; -; Genomic_DNA.
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_0000143471"
SQ   SEQUENCE   504 AA;  60431 MW;  F8F0328A970DC9A8 CRC64;
     MXXXXGYLEF DGARQQSFLY PLFFREYIYV LAYDHGLNRL NRNRSIFLEN ADYDKKYSSL
     IVKRLILRMY EQNRLIIPTK DLNQNNFLGH TSLFYYQMIS VLFAVIVEIP FSLRLGSSFE
     GKQFKKSYNL QSIHSIFPFL EDKLSHFNYV LDVLIPYPIH LEILVQTLRY RVKDASSLHF
     FRFCLYEYCN WKNFYIKKKA ILNPRFLLFL YNSHICEYES IFFFLRKRSS HLRSTSYEVL
     FERILFYVKI QHFLKVFVNN FPAILGLLKD PFIHYVRYHG RCILATKDTP LLMNKWKYYF
     VNLWQCYFSV WFQSQKVNIN QLSKDNLEFL GYLSSLRLNP LVVRSQMLEN SFLLDNVRIK
     LDTKIPISSI IRSLAKDKFC TVLGHPISKA TWTDSSDSDI LNRFVRICRN ISHYYSGSSK
     KKNLYRIKYI LRLCCVKTLA RKHKSTVRAF LKRLGSGLLE EFLTGEDQIL SLIFPRSYYA
     YKKLYRVRIW YLDILYLNDL VNHE