ID   MATK_CAMRA              Reviewed;         511 AA.
AC   Q7YKQ5;
DT   21-JUN-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   Campsis radicans (Trumpet creeper) (Bignonia radicans).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Tecomeae; Campsis.
OX   NCBI_TaxID=83937;
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; AF531775; AAP87835.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YKQ5; -.
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..511
FT                   /note="Maturase K"
FT                   /id="PRO_0000143305"
SQ   SEQUENCE   511 AA;  60391 MW;  D88137EBCB564437 CRC64;
     MEEIQRYLQL ERSHHQDFLY PLIFQEYIYA FAHDRGFSRS ILSENPGYDN KFSLLIVKRL
     ITRMYQQNHF LISSNDYDSN QNLFWARNKN FDFQIISEGF AFIVEIPFYL RLISCLEGKK
     IVKSQNLRSI HSIFPFLEDN FSHLNFVLDI GIPHPVHVEI LVQILRYWVK DPSSLHLLRF
     LLNEYCNWTS LITPKKASSS FSKRNQRLFL FLYNSHVCEY ESVFVFLRNQ SSHLRSTSSG
     VLLERIYFYG KIESLVNVFG KVKDFQANLW LVKEPCMHYI RYQRKSLLAS KGTSLFMNKW
     KCYLVTFWQW HFSLWFHPRR IYINQLSNYS LEFLGYLSNV RINPSVVRSQ IVEKSFLINN
     AIKKFDTLVP IIPLIASLAK GKFCNVLGHP ISKPVRADLS DSNIIDRFGR ICRNLSHYHS
     GSSKKKNLYR IKYILRLSCA RTLARKHKST VRAFLKRLGS ELLEEFLMSE EDVLYLTLPK
     ASSALWGVYR SRIWYLDIIS INDLANHKSK L