MATK_BRACM
ID MATK_BRACM Reviewed; 502 AA.
AC Q6QHD9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
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 Brassica campestris (Field mustard).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Simonetti E., Martin J.P., Gonzalez L.M., Aguinagalde I.;
RT "Chloroplast DNA studies of wild 2n=18 Brassica oleracea relatives using
RT PCR-RFLP and sequencing techniques.";
RL Submitted (FEB-2004) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS48152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY541619; AAS48152.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q6QHD9; -.
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..502
FT /note="Maturase K"
FT /id="PRO_0000143289"
SQ SEQUENCE 502 AA; 59866 MW; A9B27C569AFA5DE3 CRC64;
MEKFQGYLEF DGARQQSFLY PLFFRDYIYV LAYDHGLNRL NRNRPIFLEN ADYDKKYSSL
IVKRLILRMY EQNRLIIPTK DLNKNLGHTN NFYYQMISVL FAVIVEIPFS LRLGSSIEGK
NVKKSYNLQS LHSIFPFLED KLSHFNYVLD VLIPYPIHLE ILVQTLRYRV KDASSLHFFR
FCLYEYCNWK NFDSKKKSIL NPRFLLFLYN SHVCEYESIF FFLRKQSSHL RSTSYDVFFE
RILFYGKIQH FFKVFVNNFS ALLGLLKDPF LHYVRYHGKY ILATKDTPLL MNKWKYYFVN
LWQCYFSVWF QSQKVNINQL SKDNLEFLGY LSSLRLNPLV VRSQMLENSF LIDNVRIKLD
SNIPISSIIG SLAKDKFCNV LGHPISKATW TDSSDSDILN RFVRICRNIS HYYSGSSNKK
NLYRIKYILR LCCVKTLARK HKSTVRAFLK RLGSGLLEEF LTGEDQVLSL IFPRSDYASK
RLYRVRVWYL DILYLNDLVN HE