ID   MATK_METGY              Reviewed;         509 AA.
AC   Q9MST4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, 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   Metasequoia glyptostroboides (Dawn redwood) (Sequoia glyptostroboides).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC   Metasequoia.
OX   NCBI_TaxID=3371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10898782; DOI=10.2307/2657004;
RA   Gadek P.A., Alpers D.L., Heslewood M.M., Quinn C.J.;
RT   "Relationships within Cupressaceae sensu lato: a combined morphological and
RT   molecular approach.";
RL   Am. J. Bot. 87:1044-1057(2000).
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; AF152203; AAF25756.1; -; Genomic_DNA.
DR   PRIDE; Q9MST4; -.
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..509
FT                   /note="Maturase K"
FT                   /id="PRO_0000143519"
SQ   SEQUENCE   509 AA;  61272 MW;  A9FF15C5C5F63105 CRC64;
     MDEFQRNENK HRSWQQFFLY PLFFREDLYA IAHDHHLDRS GSSEPTEILV SHFFSFLTVK
     RSIRRIRKQN NSISLLRNCD RNQFSECKKN XCSKSLLEGL TVVLEVSFAM RSKHFIEGMD
     GWNSIRSIHC IFPLMEDKLT HSNYISDIRV PYSIHPEILV RIFRRWIRDT PSLHLLRSIL
     HEWQNSFSRD NLQKAIITPR ENTRFSLFLW NSYVHECESF LVPLVKRFFN SQSLLYGSFP
     DRTHFDKKMK HIVILXXRQI STKKIWLLKD SFMHYVRYGE RSLIALKGTH LEVKKWRYHL
     FHFWQYYFHL WFQPYRIRSL ELSKTYSSFL GYFLHVKMRP LVVRAKMLDN LFITDLITNE
     LKLIAPIRSI LFFLAKEKFC DISGWPISKL SWTSLSDDDI LDRFDRIWIN LFHYYSGSMN
     QDGLYHIKYI LLLSCAKTLA CKHKTTIRVV REQLGSELFT KSFSKEREFI SSSFSKNRLK
     RERIWNSEIS QINPLANFWQ NMQNKQIEN