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MATK_RANLI
ID   MATK_RANLI              Reviewed;         508 AA.
AC   Q507Q9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 45.
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   Ranunculus lingua (Greater spearwort).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae;
OC   Ranunculeae; Ranunculus.
OX   NCBI_TaxID=105186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Paun O., Lehnebach C., Johansson J.T., Lockhart P., Hoerandl E.;
RT   "Phylogenetic relationships and biogeography of Ranunculus and allied
RT   genera (Ranunculaceae) in the Mediterranean region and in the European
RT   alpine system.";
RL   Taxon 54:911-932(2005).
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; AY954206; AAY21353.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q507Q9; -.
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..508
FT                   /note="Maturase K"
FT                   /id="PRO_0000143671"
SQ   SEQUENCE   508 AA;  60918 MW;  579184DAA8A91734 CRC64;
     MEELQRYLKM DRSRERDFLY PLIFQEYIYV LAHDFGLTKS IPYESMQILS YDNKYSSLIV
     KRLIIRMYQQ KHFLILDNDS NQKKFLGHNK NLYSQMISEG FAVIVEIPFA LRLVSSYQGK
     EIKKSINLRS IHSTFPFLED KFVHLNHVLD ILIPYPIHLE LLVQNLRCWI QDASFLHLLR
     FFLYEYHNWN SLTTQKTKQN SLFLKENRRF FLFLYNFHVY ESESIFLFLR KKSYHLRSTS
     SIAFLDRRRF YGKIEHFKVV FHNDFHTILW LFKDPFMHYF RYQGKSIMSS KGTLLLMKKW
     KYYLVNLWEC HFDFWSQPNR IHINQLSNRF LDFLGYLSGV RPNPSVVRNQ MLENAFIIDI
     AINKLDTIVP IIPLIGSLAK AKFCNLSGQP VSKPAWTDSP DSDIMDRFGR ICRNVSHYYS
     GSSKKKTLYR IKYIFRLSCA RTLARKHKST VRSFLKRLGS EFLEEFLIEE EEVLSFILPK
     ISSSSQRLSK ERIWYFDIIR INDLMDLS
 
 
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