MATK_LATTI
ID MATK_LATTI Reviewed; 506 AA.
AC Q8MCR8;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
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 Lathyrus tingitanus (Tangier pea).
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 NPAAA clade; Hologalegina; IRL clade; Fabeae; Lathyrus.
OX NCBI_TaxID=3862;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Steele K.P., Wojciechowski M.F.;
RT "Phylogenetic analyses of tribes Trifolieae and Vicieae based on sequences
RT of the plastid gene matK (Papilionoideae: Leguminosae).";
RL (In) Klitgaard B.B., Bruneau A. (eds.);
RL Advances in legume systematics - part 10, pp.355-370, Royal Botanic
RL Gardens, Kew (2003).
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; AF522087; AAM82079.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MCR8; -.
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_0000143460"
SQ SEQUENCE 506 AA; 60898 MW; 6187B6AE73C9D564 CRC64;
MKEYQVYLER ARSRQQDFLY PLLFREYIYG LAYSHNLNRS IFLENVGYDN KYSLLIVKRL
ITRMYQQNHL IISANDSNKN TLGGYNPILD SQIISEGFAI VVEIPFLRQL SSSLEEEKIL
QSYKNLRSIH SIFPFLEDKF TYLHYVSDIR IPYPIHLEIL VQILRYWVKD APFFHLLRLF
LYNFCNWNSF FTTKKWISTF SKSNPRLFLF LHNFYVCEYE SIFVFLRTKS SHLRLKSFSV
FFERIFFYAK REHLVKVFSK DFSYTLTFLK DPNIHYVRYQ GKCILASKNA PFLMNKWKHY
FIHLWQCFFD LWSQPRMINI NPLSEHSFQL LGYFLNVRLN RSVVRSQMLQ NTFLIEMVIQ
NLDIIVPIIP LIRSLAKAKF CNILGEPISK PVWADSSDFD IIDRFLRICR NLSHYYNGSS
KKKSLYRIKY ILRLSCIKTL ACKHKSTVRA FLKRSGSEEL LQEFFTEEQE ILSFIFPRDS
STWQRLHRNR IWYLDILFSN DLVHDE