ID   MATK_AMOPO              Reviewed;         512 AA.
AC   Q8MEE6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, 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   Amorphophallus paeoniifolius (Whitespot giant arum) (Amorphophallus
OS   campanulatus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Thomsonieae;
OC   Amorphophallus.
OX   NCBI_TaxID=174187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND23294517;
RA   Grob G.B.J., Gravendeel B., Eurlings M.C.M., Hetterscheid W.L.A.;
RT   "Phylogeny of the tribe Thomsonieae (Araceae) based on chloroplast matK and
RT   trnL intron sequences.";
RL   Syst. Bot. 27:453-467(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; AF387410; AAM46585.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MEE6; -.
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..512
FT                   /note="Maturase K"
FT                   /id="PRO_0000143230"
SQ   SEQUENCE   512 AA;  60674 MW;  1C905D09F427EAF7 CRC64;
     MEELKGYLKK SRSKQQHFLY PLLFQEYIYA FAHDHGLNVN GSFFYEPAEI SGYDKKFSSL
     LVKRLITRMY QQNYLINSVN DSNQNRFVGH NKNLYSQMIS EVFAVIVEIP FSLRLVSFLA
     EKKEIPKSQN LRTIHSIFPF FEDKLSHLNC VSDILIPYPV HLEILVQILQ CRIQDVPSLH
     LLRFFFHEYH NWNNLITPKK SNYYGFSKEN PRLFLFLYNS YVVECESIFV FLRKQSSYLR
     STSSGTFLER AHFYEKIEQH LVVLCCNDFQ KTLWLFKDPF MHYVRYQGKS ILASKGTHLL
     MKKWKSYFVN FWQCHFHFWS QPCRIHINQF SKFSFYFLGY LSSVPINPSA VKSQMLENSF
     LVDTVTKKFE TIVPIIPMIG ALSKAKFCNV SGNPISKPVW ADLSDSDIID RFGRTCRNLS
     HYYSGSSKKQ SLYRIKYILR LSCARTLARK HKSTVRAFLQ RLGSEFLEEF FTEEEKALSL
     ILPRISYPLD KLYRERIWYL DIIRINDLVN HL