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MATK_OXYPI
ID   MATK_OXYPI              Reviewed;         506 AA.
AC   Q5D1B9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 43.
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   Oxytropis pilosa (Woolly milkvetch) (Astragalus pilosus).
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; Galegeae; Oxytropis.
OX   NCBI_TaxID=83865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wojciechowski M.F.;
RT   "Astragalus (Leguminosae): a molecular phylogenetic perspective.";
RL   Submitted (FEB-2005) 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; AY920452; AAX14920.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5D1B9; -.
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_0000143564"
SQ   SEQUENCE   506 AA;  60439 MW;  6AE52DD01273C89B CRC64;
     MKEYQVLLER DRSRQQDFLY PLIFREYVYG LAYSHDFNRS TFVENVGYDK KYSLLIVKRL
     ITRMYQQNHL IISANDSKKN PFLGYNKNFY SQIISEGFAI VVEIPFFLQF SSSLEEADIV
     KSYKNLRSIH SVFPFLEDKF PYLNYVSDIR IPYPIHLEIL VQILRYWVKD APFFHLLRLF
     LYNFCNRNSF LTPKKSISTF SKSNPRLFLF LYNFYVCEYE SIFLFLRKKS SHLRLKSFSV
     FFERIFFYAK REHLVEVFAK DFSSTVTFFK DPLFHYVRYQ GKSILASKNA PLLMNKWKHY
     FIHLWECFFD VWSQPGTIHI KQLSEHSFYL LGYFSNVRLN RSVVRSQMLQ NTFLIEIVSK
     KLDTIVPIIP IIRSLAKAKF CNVLGHPISK AVWADSSDFD IIERFLRICR NLSHYYNGSS
     KKKSLYRIKY ILRLSCIKTL ACKHKSTVRA FLKRSGSEEL LEEFFTEEEE ILSLIFPRAS
     CTLQKLHGNR IWYLDILFSN DLVNHE
 
 
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