MATK_ROBPS
ID MATK_ROBPS Reviewed; 507 AA.
AC Q9TKP9;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 11-DEC-2019, entry version 57.
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 Robinia pseudoacacia (Black locust).
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; robinioid clade; Robinieae; Robinia.
OX NCBI_TaxID=35938;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10719003; DOI=10.2307/2656638;
RA Hu J.-M., Lavin M., Wojciechowski M.F., Sanderson M.J.;
RT "Phylogenetic systematics of the tribe Millettieae (Leguminosae) based on
RT chloroplast trnK/matK sequences and its implications for evolutionary
RT patterns in Papilionoideae.";
RL Am. J. Bot. 87:418-430(2000).
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; AF142728; AAD52899.1; -; Genomic_DNA.
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_0000143681"
SQ SEQUENCE 507 AA; 60668 MW; FE092A065FB4DE99 CRC64;
MEEHQVYLEL DRSRQQDFLY PLVFREYIYG LAYGHDLNRS IFAENVGYDN KSSLLIVKRL
ITRMYQQNHL IISANDSKKN TFLRYNNNIY SQIISEGFAV VVEIPFSLQL SSSLEEAEIL
KSYNNLQSIH SIFPFFEDKF TYLNYLSDIR IPYPIHLEIL VQILRYWVKD VPFFHLLRLF
LYDYCNSNSL ITPKKWISTF SKSNPRFFFF LYNFYVCEYE SIFYFLRNKS SHLRLKSFSV
FFERIFFYAK RKHLVEVVAK DFLSTLTFFK DPFIHYVRYQ GKSILASKNA PLLMNKWKYY
FIHLWQCHFD LWAQPGTIHI NLLSEHSFHF LGYFLNVRLN RSVVRSQMLQ NAFLIEMVIK
KLDIIVPIIP LIRSLAKANF CNGLGNPISK PVWADSSDFD IIDRFLRICR NLSHYYNGSS
KKKSLYRIKY ILRLSCIKTL ACKHKSTVRA FLKRLGSEKL LEEFFIEEQE IVSLIFPRAS
XTLQRLHRNR IWYLDILFFS NDLVNHE