ID   MATK_ACECA              Reviewed;         512 AA.
AC   Q8SM90;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 52.
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   Acer campestre (Field maple) (Hedge maple).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Sapindaceae; Hippocastanoideae; Acereae; Acer.
OX   NCBI_TaxID=66205;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=24/2 AC 01;
RA   Bittkau C., Mueller-Starck G.;
RT   "Chloroplast DNA variation of Acer campestre, A. monspessulanum and related
RT   species in Europe.";
RL   Submitted (MAR-2002) 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; AJ438795; CAD27639.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8SM90; -.
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_0000143199"
SQ   SEQUENCE   512 AA;  61003 MW;  8D262BA2C3063A0D CRC64;
     MKEYQIHLEL DRSQQNNFLY PLLFREYIYA LAHDHGLNRS TIPLENGGYD NKSSSLSVKR
     LISRTYQRIH LSIYAKDSNP NQFIGHNNKF YSQMISEGFS VIVEIPFSLR LVAFLEGKEM
     AKSQNFQSIH SIFPFFENNF SHLHYVLDVL IPYPIRPEIL VRTFRYWVKD ASSLHLLRFF
     LHEYFNWNSL ITPKKSNSIF STRNPRFFLF LYNSHVYEYE SIFFFLRNQS SHLRSTSSGL
     LFERISFYGK VEDLVQVFVN DFQDNLWLFK HPIMHYVRYQ GKSVLASKDM PLLMNKWKYY
     LVNLWQWHFH VWSQPGRIHI NHLYKDYIDF LGYLSRGRLN TLVVRSQMLE NAFLIDNAMK
     QFETTVPIIP LIGSLTTARF CNSLGHPISK PTWADSSDSY IIDRFMRICR NLSHYHSGSS
     KKKSLYRIKY ILRVSCVKSL VRKHKSTVRV FLKRLGSEFL EEFFTEEEHV LSLIFPRALF
     TSRRLYRGRV WYLDIICIND LVNHDKLEIV PN