ID   MATK_RHOFR              Reviewed;         506 AA.
AC   O62984;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 60.
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   Rhododendron ferrugineum (Alpenrose).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Ericaceae; Ericoideae; Rhodoreae; Rhododendron.
OX   NCBI_TaxID=49622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kurashige Y., Mine M., Kobayashi N., Handa T., Takayanagi K., Yukawa T.;
RT   "Investigation of sectional relationships in the genus Rhododendron
RT   (Ericaceae) based on matK sequences.";
RL   Shokubutsu Kenkyu Zasshi 73:143-154(1998).
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; AB012741; BAA25862.1; -; Genomic_DNA.
DR   AlphaFoldDB; O62984; -.
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..506
FT                   /note="Maturase K"
FT                   /id="PRO_0000143676"
SQ   SEQUENCE   506 AA;  60534 MW;  ADA44B25E92436E8 CRC64;
     MEEFKRNLEL DRSQQHDFIY PLIFQEYIYA LAHDRGLNRS IFLENTGYEN KSSLLIVKRL
     IIHLITQMYQ QNHFLFSGND SNQNKFLGYN TNLYSQMIFE GFAVVVEIPF YLRLLSFLEG
     KERVKSHNLR SIHSIFPFLE DKFSHLVYVL DILISHPIHL EIVIQTLRYW VKDASSLHLL
     RFFLHEYPIW NSLITPKKSS FSFSIRNQRF FLFLYNFHVC EYESIFVFLR NQSSHLRSIS
     SETFLERISF YRKIELEVFT KDFKAIIWVF KEPFLHYVRY RGKAILASKG TSLLMNKWKY
     YLVNFWQCYF YMWSQPRRIH INQLSNHSLD FLGYLSTVRL KPLMVRSQMI ENSFIIENAS
     KKFDTLMPIT PMIRSLSKAK FCNVLGHPMS KPVWAALSDS DIIERFGRIY RNLSHYYSGS
     LKKMSLYRIK YILRLSCART LARKHKSTVR AFLKRLGVGL LEEFFTEEEQ VFYLTFAKAS
     SNSGELYQRR VWYLDIICIN DLANYE