ID   MATK_PENHE              Reviewed;         510 AA.
AC   Q8SM04;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, 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   Penstemon heterophyllus (Foothill penstemon).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Cheloneae; Penstemon.
OX   NCBI_TaxID=160372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND23289696;
RA   Wolfe A.D., Datwyler S.L., Randle C.P.;
RT   "A phylogenetic and biogeographic analysis of the Cheloneae
RT   (Scrophulariaceae) based on ITS and matK sequence data.";
RL   Syst. Bot. 27:138-148(2002).
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; AF375219; AAM19391.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8SM04; -.
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_0000143579"
SQ   SEQUENCE   510 AA;  60296 MW;  990F02889C065527 CRC64;
     MEEIQRYLQL KRSQQHNFLY PLIFQEYIYA FAHDRSFSRS ILSEKTGYEK KSSLLIVKRV
     ITRMYQQNPF IIFLNDSTQN KFLGHNNNFY SQLISEGFAF IVEIPFFLRL ISSREGKKKK
     IVKSQNLRSI HSIFPFLEDS FSHLNFLLDI LIPHPVHVEI LVQTLRYWVK DASSLHLIRF
     LLNEYCNSNC VFIPKKASSS FSNSKRNQRL FLFLYNSHVC EYESIFFFLR NQSSRLRSTS
     SRVLLERIYF YGKIEHLVNV VVKVKDFQAN LWLVKEPCMH YVRYQRKAIL ASKGTSLFMN
     KWKCFLVTFW QWHFSLWFHP RRIYINQLSK NFLECLGYLS SVQMNPSVVR SQILENSFLI
     NNAIKKFDTL VPIIPLIASL ANTKFCNVLG HPISKPVWAD LSDSHIIDRF GRICRNLSHY
     HSGSSKKKSL YRIKYILRLS CARTLARKHK STVRAFFKRL GSELLEEFLM SEEDVLFLTF
     PKASSTLRGV SKSRIWYLDI LCISDLVNYK