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MATK_ARAHA
ID   MATK_ARAHA              Reviewed;         504 AA.
AC   Q9GF51;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 55.
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   Arabidopsis halleri.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Koch M., Mitchell-Olds T.;
RT   "Evolutionary analysis of plastidic maturase K and nuclear chalcone
RT   synthase and their utility for phylogenetic reconstructions within the
RT   Brassicaceae.";
RL   Submitted (APR-1999) 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}.
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DR   EMBL; AF144341; AAG43310.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9GF51; -.
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..504
FT                   /note="Maturase K"
FT                   /id="PRO_0000143243"
SQ   SEQUENCE   504 AA;  60299 MW;  109F4AF5C24940DD CRC64;
     MEKFQGYLEF DGARQQSFLY PLFFREYIYV LAYDHGLNRL NRNRSIFLEN TDYDKKYSSL
     IVKRLILRMY EQNRLIIPTK DLNQNSFLGH TSLFYYQMIS VLFAVIVEIP FSLRLGSSFQ
     GKQLKKSYNL QSIHSIFPFL EDKLAHFNYV LDVLIPYPIH LEILVQILRY WVKDASSLHF
     FRFCLYEYCN CKNFYIKKKS ILNPRFFLFL YNSHVCEYES IFFFLRKRSS HLRSPSYEVL
     FERIFFYGKI QHFFKVFINN FPAILGLLKD PFIHYVRYHG RCILATKDTP LLMNKWKYFF
     VNLWQCYFSV WFQSQKVNIN QLSKDNLEFL GYLSSLRLNP LVVRSQMLEN SFLIDNVRIK
     LDSKIPISSI IGSLAKDKFC NVLGHPISKA TWTDSSDSDI LNRFVRICRN ISHYYSGSSK
     KKNLYRIKYI LRLCCVKTLA RKHKSTVRAF LKRLGSGLLE EFLTGEDQVL SLIFPRSYYA
     SKRLYRVRIW YLDILYLNDL VNNE
 
 
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