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MATK_PROLU
ID   MATK_PROLU              Reviewed;         500 AA.
AC   Q7YKM5;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   11-DEC-2019, entry version 47.
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   Proboscidea louisiana (Louisiana Devil's-claw) (Proboscidea louisianica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Martyniaceae; Proboscidea.
OX   NCBI_TaxID=9786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15248131; DOI=10.1055/s-2004-817909;
RA   Mueller K.F., Borsch T., Legendre L., Porembski S., Theisen I.,
RA   Barthlott W.;
RT   "Evolution of carnivory in lentibulariaceae and the Lamiales.";
RL   Plant Biol. 6:477-490(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; AF531809; AAP87869.1; -; 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..500
FT                   /note="Maturase K"
FT                   /id="PRO_0000143650"
SQ   SEQUENCE   500 AA;  58766 MW;  BCF693F525AB884B CRC64;
     MEEIQRYLQL ERSQQHDFLY PLIFQEYIYT FAHDHGFSRS IWSKNRGYDN KSSLLIVKRL
     ITRMYQQNHF LISLNDSNQN PFWARNKNLY SQIISEGFAF IVEIPFSIRL ISCLEGKKIV
     KSQNLRSIHS IFPFLEXNFS HLNFVLDILI PHPVHVEILD ASSLHLLRFF LNEYCNWNSL
     ITPKKASSSF SKINQRLFLF LYNSHVCEYE SIFVFLRNQS SHLRSTSSGV LLERIYFYGK
     IEHLVNVFVT VKDFQANLWL VKEPCMHYIR YQRKSILASK GTSLFMNKWK CYLVTFWQWH
     FSLWFHPSRI YINQLSNHSL EFLGYLSSVR MNPSVVRSQI LENAFLINNA IKKFDTLVPI
     IPLIASLAKA KFCNVLGHPI SKPVRADLSD SNIIDRFGCI CRNLSHYHSG SSKKKSLYRI
     KYILRLSCAR TLARKHKSTV RAFLKRLGSE LLEQFLMSEE DVLFXTFXKA SSTLRGVNNS
     RIWYVDIISI NDLAXHKSKF
 
 
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