ID   MATK_THLAR              Reviewed;         504 AA.
AC   Q9GF35;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   11-DEC-2019, entry version 51.
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   Thlaspi arvense (Field penny-cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Thlaspideae; Thlaspi.
OX   NCBI_TaxID=13288;
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; AF144360; AAG43329.1; -; 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_0000143733"
SQ   SEQUENCE   504 AA;  60068 MW;  388855A989A75A16 CRC64;
     MXXXXGYLEF DGARQQSFLY PLFFREYIYV LAYDHRLNRL NRNRSIFVEN VDSDKKYSSL
     IVKRLILRMY EQNCLIFSIK DLNQNTSLGH TNLFYYQMIS VLFAVIVEIP FSLRLGSSFE
     GKQLKKSYNL QSIHSIFPFL EDKLTHFNYV LDVLIPYPIH LEILVQTLRY RVKDASSLHF
     FRFCLYESCN WKNFDIKKTS ILNPRFFLFL YNSHVCEYES IFFVLRKRSS HLRSTSYKVL
     FERILFYVKI QHFFKVFVNN FPAILGLLKD PFLHYVRYHG KCILATKDTP LLMNKWKYYF
     VNLWQCYFSV WFQPQKVNIN QLSKDNFEFM GYLSSLRLNP LVVRSQMLEN SFLIDNVRIK
     LYSKIPISSI IGSLAKDKFC NVLGHPISKA TWADSSDSDI LNRFVRICRN ISHYYSGSSK
     KKNLYRIKYI LRLCCVKTLA RKHKSTVRAF LKRLGSGLLE EFLTGEDQVL SLIFPRSYYA
     SKRLYRVRIW YLDILSLNDL VNHE