MATK_RANMC
ID MATK_RANMC Reviewed; 507 AA.
AC A1XGL9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 37.
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 macranthus (Large buttercup).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae;
OC Ranunculeae; Ranunculus.
OX NCBI_TaxID=334596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17573971; DOI=10.1186/1471-2164-8-174;
RA Raubeson L.A., Peery R., Chumley T.W., Dziubek C., Fourcade H.M.,
RA Boore J.L., Jansen R.K.;
RT "Comparative chloroplast genomics: analyses including new sequences from
RT the angiosperms Nuphar advena and Ranunculus macranthus.";
RL BMC Genomics 8:174-174(2007).
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; DQ359689; ABC70737.1; -; Genomic_DNA.
DR RefSeq; YP_001004167.1; NC_008796.1.
DR AlphaFoldDB; A1XGL9; -.
DR GeneID; 4712200; -.
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_0000355961"
SQ SEQUENCE 507 AA; 60683 MW; 675BA755683F0173 CRC64;
MEELQRYLKM DRSRERDFLY SLLFQEYIYA LAHDFGLTKS IPYESMQILS YDNKYSSLIV
KRLIIRMYQQ KHLIILDNDS KNKNFLGHNK NLYSQMISEG FAVIVEIPFA LRLVSSYQGK
EIEKSINLGS IHSTFPFLED KFVHLNHVLN ILIPYPIHFE LIVQNLRCWI QDASFLHLLR
FFLYEYHNWN SFTTQKMKQN SLFLKENRRF FLFLYNFHVY ESESIFLFLR KKSYHLRSTS
SIAFLDRTHF FGKIEHLKVV FRNDFHTMLW LFKDPFMHYF RYQGKSIMSS KGTPLLMKKW
KYYLVNLWEC HFYFWSQPNR IHINQLSNIF LNFLGYLSSV RPNPSVVRNQ MLENAFIIDI
SRNKLSTLVP IIPLIGSLAK AKFCNLSGQP ISKPAWTDSL DSDIIDRFGR ICRNVSHYYS
GSSKKKTLYR IKYILRLSCA RTLARKHKST VRSFLKRLGS EFLEEFLIEE EQVLSFILPK
ISSSSQRLSK ERIWYFDIIR INDLMDL