MATK_AMPBR
ID MATK_AMPBR Reviewed; 507 AA.
AC Q6PSE2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 51.
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 Amphicarpaea bracteata (American hog peanut) (Glycine bracteata).
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; indigoferoid/millettioid clade; Phaseoleae; Amphicarpaea.
OX NCBI_TaxID=45679;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND43667961; DOI=10.1600/0363644042451035;
RA Thulin M., Lavin M., Pasquet R., Delgado-Salinas A.;
RT "Phylogeny and biogeography of Wajira (Leguminosae): a monophyletic
RT segregate of Vigna centered in the horn of Africa region.";
RL Syst. Bot. 29:903-920(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; AY582971; AAS94270.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6PSE2; -.
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..507
FT /note="Maturase K"
FT /id="PRO_0000143232"
SQ SEQUENCE 507 AA; 61637 MW; 82EB1EA2F6EF410A CRC64;
MEEYRAYLEL HRSRHQDTLY PLFFREYIYG LACGHGSILV ESVGYNNKFS LLIVKRLITR
MYQQTHFIIF ANDSNKNPFR GYNNHFYSQI ILEGFVVVVE IRFSLQLFIS SLRELEIIKS
YNNLRSIHSI FPFFEDKLIY LNLESDIRIP YPIHLEILVQ ILRYWIKDVS FFHLLRLFFS
YYYNRNNLFT PKKWISTFFS KSNPSFFLFL YNLYVQEYES IFIFLRNKSS QLRLKYFRVF
FERIFFYEKI EHLVEVSVKD CSYTFSFFKD TFIHYVRYQG KSILVSKNTP LFINKWKYYF
IYLWQCHFDI WSRPGTIHIN QLSRHSFHFL GYFLSIRLNF SVVRSQMLQN SFLIKIVMKK
LDTIVPIISL IRSLAKAKFC NVFGHPISKP VWANLSDFDI IDRFLRICRN FYHYYNGSAK
KKSLYQIRYI LRLSCIKTLA RKHKSTARTF LKRLGSEKLL EEFFTEEEDI FSLIFPIPKT
SFTVQRLYRG RIWYLDILFR NDFVNHL