MATK_CYTSC
ID MATK_CYTSC Reviewed; 506 AA.
AC Q5YK00;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 48.
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 Cytisus scoparius (Scotch broom) (Spartium scoparium).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Cytisus.
OX NCBI_TaxID=3835;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND43661289;
RA Wojciechowski M.F., Lavin M., Sanderson M.J.;
RT "A phylogeny of legumes (Leguminosae) based on analysis of the plastid matK
RT gene resolves many well-supported subclades within the family.";
RL Am. J. Bot. 91:1846-1862(2004).
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; AY386902; AAQ91980.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YK00; -.
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_0000143354"
SQ SEQUENCE 506 AA; 60403 MW; 2D96B91E64CCD955 CRC64;
MEEYQVYLEL DISRQQHFLY PLIFREYIYG LAYGHDFNGS IFSENVDYDN KSSLLIVKRL
ITRMYQQNHL IISANDSKKN QFWGYNKNLY SQIISEGFAI VVEIPLSLQL NSSSEEAEII
KYYKNLRSIH SIFPFFEDKL TYLNYVSDAR IPYPIHLEIL VQVFRYWAKD APLFHLLRLF
LYEYCNWNNL ITPKKLISTF SKSNLRVFLF LYNFYVCEYE SIFLFLRNKS SHLQLTSFSV
LFERIYFYGK IEHFVEVFAK DFSSTLSFFK EPFIHYVRYQ GKSILASKNA SLLMNKWKNY
LIHLWQYHFD VWSQPRTIQI NQFSERSFHL LGYFSNVRLN LSAVRSQMLE NAFLIEIVMK
KLETIVPIIP LIRSLAKAKF CNVLGHPISK PVWADSSDFD IIDRFLRICR NLSHYYNGSS
KKKSLYRVKY ILRLSCIKTL ARKHKSTVRA FLKRLGSEKL LEEFFTEEEE ILSLVFQRAS
STLQGLYRGR IWYLDIIFIN DLINHE