ID   MATK_ARUDI              Reviewed;         504 AA.
AC   Q8WJR4;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 55.
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   Aruncus dioicus (Goat's beard).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Spiraeeae; Aruncus.
OX   NCBI_TaxID=32220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Potter D., Gao F., Oh S.-H., Baggett S.;
RT   "Phylogenetic relationships among putative genes encoding polygalacturonase
RT   inhibitor proteins (PGIPs) in Rosaceae.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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; AF288094; AAL35988.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8WJR4; -.
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..504
FT                   /note="Maturase K"
FT                   /id="PRO_0000143258"
SQ   SEQUENCE   504 AA;  60202 MW;  5C59D4117987C05E CRC64;
     MEEFQGYLEI DGYQQHDFLY PLIFREYIYA LAHGLNRSIL LDNVGYDNKS SLLIIKRLIS
     RMYQQNHLII SANYYKQNKF FGYNKNLYSQ IISEGFAVIV EIPFSLRSVS SLEATEKEII
     KSYNLRSLHS LFPFLEDKFP HLNYVSDVLI PYPIHLEILV QTLRYWVKDS SSLHLLRLFL
     HEYYNWNSLI TPNKFIFSKS NQRLFLLLYN SHVCEYESIL LFLRNQSSHL PLTSYGIFFE
     KIHFYEKIKY PGDEVFSNDF MVSILWFFKD PFMHYVRYQG KSILASKDTP LMMNKWKYYL
     VNLWQCHYYV WSQPGRIYIN QLSKHSLYFL GYFASMQPNL SVVRSQMLEN SFIMDNAMKK
     LDTLVPIIPL IVSLAKVKFC NALGHPISKS TWTDSSDFDI IDRFVRICRN ISHYYSGSSR
     KKSLYRIKYI LRLSCVKTLA RKHKSTVRTF LKRLGSKLLE EFFTEEELIR SLIFPRTSYS
     LKKFYRGRIW YFDIFCINDL VNHE