MATK_HEDHE
ID MATK_HEDHE Reviewed; 505 AA.
AC Q8WH60; Q8WH57; Q8WH58;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 07-OCT-2020, entry version 52.
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 Hedera helix (English ivy).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Hedera.
OX NCBI_TaxID=4052;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sample 13HH01, Sample 20HH01, and Sample 26HH05;
RA Grivet D., Petit R.J.;
RT "Phylogeography of the common ivy (Hedera sp.) at the European scale: is
RT the native European liana following the standards recolonization pathway.";
RL Submitted (SEP-2001) 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; AJ319068; CAD01146.1; -; Genomic_DNA.
DR EMBL; AJ319070; CAD01148.1; -; Genomic_DNA.
DR EMBL; AJ319072; CAD01150.1; -; 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..505
FT /note="Maturase K"
FT /id="PRO_0000143417"
FT VARIANT 40
FT /note="N -> S (in sample 26HH05)"
FT VARIANT 85
FT /note="L -> R (in sample 20HH01)"
SQ SEQUENCE 505 AA; 59655 MW; 3E480CF4E167E952 CRC64;
MEEFQRYLEL DRSQQHYFLY PLIFQEYIYX XAHDHGLNRN RSILLENAGY DNKFSLLIVK
RLITRMYQYQ QNHLILSTND SNQNLFLRRN KNLYSQMISE GFAVIVEIPF SLQLISSLES
KGIVKSHNLR SIHSIFPFLE DKISHFIYVL EILIPYPVHL EILVQTLRYW VKDASSLHLL
RFFLHEYCNW NTPNKAGSSF SKRNQRLFFF LYNSHLCEYE SIFIFLRNQS SHLRSTSSGT
LLERIYFYGK IKYLVKVFVK AFQVNLLLLK DPFMHYVRYQ GKSILASKGT PFLMKKWTYY
FVNLWQCHFY LWSQPGRICI NQLYNHSLDL LGYLSSARLN PSMVRGQMLE NSFLIDNAIN
KFDTIVPIIP LIGSLAKAKF CNVLGHPISK AVWTDLSDSD IIDRFGRICR NLSHYHSGSS
QKKSLYRIKY ILRLSCARTL ARKHKSTVRA FLKRLGSGLL EEFFTAEEQV LYLTLPRASS
ASQRLYRRRI WYLDIICIND LANHE