ID   MATK_AVIGE              Reviewed;         506 AA.
AC   Q7YKQ9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 50.
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   Avicennia germinans (Black mangrove) (Bontia germinans).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Acanthaceae; Avicennioideae; Avicennia.
OX   NCBI_TaxID=41378;
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; AF531771; AAP87831.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YKQ9; -.
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_0000143271"
SQ   SEQUENCE   506 AA;  60045 MW;  121AC037006DB643 CRC64;
     MEEIKRYLQR NRSHHQDFLY PLIFQEYIYA FAHYRGFSQS ILSENPGYDN KSSLLLVKRL
     ITRMYQQNHF LIFPNDSNQN PFFARNKNLY SQIIPEGFAF IVEIPFSLRL ISCLEGKKIV
     KSQNLRSIHS IFPFLENNFS HFHFVLDVLI PHPVHVEILV QTLRYWLKDA SSLHLLRFFL
     NEYCNWNSCI LPKKAGSSFS KRTQRLFLFV YNSHVWEYES IFVFLRNQSA HLRSISSGVL
     LERIYFYGKM ERLVNVFVKV KDFRSNPGLI KEPCMHYIRY QRKSILASKG TSLFMNKWKC
     YLVTLWQWHF SLWFHPRRIY INQLANHSLE FLGYLSSVRM NPSVIRSQIL ENAFLINNAI
     KKFDTLVPII PLIMSLAKAQ FCTVLGHPIS KPVWADLSDS NIIDRFRRIS RNLSHYHSGS
     STKKSLYRIK YILRLSCVRT LARKHKRTVC VFLKRSGSEL LEEFLMSEEG VPFFTFQKGF
     STLRGIYRSR VWYLDIFSIN DLANHK