ID   MATK_IBILU              Reviewed;         509 AA.
AC   Q7YKQ2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 49.
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   Ibicella lutea (Yellow unicorn-plant) (Martynia lutea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Martyniaceae; Ibicella.
OX   NCBI_TaxID=204345;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15248131; DOI=10.1055/s-2004-817909;
RA   Mueller K.F., Borsch T., Legendre L., Porembski S., Theisen I.,
RA   Barthlott W.;
RT   "Evolution of carnivory in lentibulariaceae and the Lamiales.";
RL   Plant Biol. 6:477-490(2004).
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; AF531778; AAP87838.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YKQ2; -.
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..509
FT                   /note="Maturase K"
FT                   /id="PRO_0000143431"
SQ   SEQUENCE   509 AA;  60149 MW;  8919D9D67F5D22C5 CRC64;
     MEEIQRYLQL ERSQQHDFLY PLIFQEYIYT FAHDRGFSRS ILSENPGYDN KSSLLIVKRL
     ITRMYQQNHF IISPNDSNQN PFWARNKNLY SQIISEGFAF IVEIPFSIRL ISCLEGKKIV
     KSQNLRSIHS IFPFLEDNFS HLNFVLDILI PHSVHVEILV QTLRYWVKDA SSLHLLRFFL
     NEYCNWNSLI TPKKASSSFS KRNQRLFLFL YNSHVCEYES IFVFLRNQSS HLRSTSSGVL
     LERIYFYRKI ERLVNVFVKV KDFQANLWFV KEPCMHYIRY QRKSILASKG TSLFMNKWKC
     YFVTFWQWHF SLWFHPSRIY INQLSNHSLE FLGYLSSVRI NPSVVRSQIL ENAFLINNAI
     KKFDTLVPII PLIASLAKAK FCNVLGHPVS KPGRADLSDS NIIDRFGCIC RNLSHYHSGS
     SKKKSLYRIK YILRLSCART LARKHKSTVR AFLKRLGSEF LEQFLMSEED VLFLTFQKAS
     STLRGVYRSR IWYLDIISIN DLANHKSKF