ID   MATK_PRUPE              Reviewed;         506 AA.
AC   Q8WJP1;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 56.
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   Prunus persica (Peach) (Amygdalus persica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760;
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; AF288117; AAL36011.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8WJP1; -.
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_0000143654"
SQ   SEQUENCE   506 AA;  60176 MW;  E1F83F0D2C909AEF CRC64;
     MEEFQGYLEL DRYQQHDFLY PLIFREYIYA LAHDHGLNRS ILLDNVGYDN KSSLLIIKRL
     ISRMYKHNHF FISANASNQK KKLGYNKNLY SQKISEGFTV IVEISFSLRL VSSLEATETV
     KSYNLRSIHS IFPFLEDKFP HLNYVSDVLI PYPIHLEILV QTLRYWVKDA SSLHLLRLFL
     HEYYNWNSLI TSNNFFFSKS NPRLFLLLYN SHVCEYEFIL LFLRNQSSHL QLTSSGIFFE
     RIHFYEKIKY PVEKVFANDF PASILWFFKD PFMHYVRYQG KSILASKDTP LLMNKWKYYL
     VNLWQCHSYV WSQPGRIYIN KLSKHSLDFL GYFSSIRPNL SVVRSQMLEN SFITDNAMKK
     LDTLVPIIPL IGSLAKVKFC NALGHPISKS TWADSSDFDI IDRFLRICRN LSHYYSGSSR
     KKSLYRIKYI LRLSCLKTLA RKHKSTVRTF LKRLGSKLLE EFFTEEEQIL SLVFPRASYT
     FTFKKLYRGR IWYLDIFCIN DLINYE