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MATK_BARAL
ID   MATK_BARAL              Reviewed;         510 AA.
AC   Q5I6K6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 38.
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   Bartsia alpina (Velvet bells).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Rhinantheae; Bartsia.
OX   NCBI_TaxID=46052;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15713237; DOI=10.1186/1471-2148-5-16;
RA   Young N.D., dePamphilis C.W.;
RT   "Rate variation in parasitic plants: correlated and uncorrelated patterns
RT   among plastid genes of different function.";
RL   BMC Evol. Biol. 5:16-16(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.
CC   -!- SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01390}.
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DR   EMBL; AY849600; AAW45733.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5I6K6; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-UniRule.
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   mRNA processing; Plastid; RNA-binding; tRNA processing.
FT   CHAIN           1..510
FT                   /note="Maturase K"
FT                   /id="PRO_0000143278"
SQ   SEQUENCE   510 AA;  60325 MW;  6CA35667A82FD00A CRC64;
     MEEIRRYLQL ERSQQHDFLY PLIFQEYIYA FAHDRGFSRS ILLENENPGY DNKSSLLVMK
     RLITRMYQQN HFLISPNDFN QKNPFFAHNK NLYSQIIAEG FAFIVEIPFS LRLISEGKKK
     KIVKSQNLRS IHSIFPFLED NFSYLNFVLD ILIPHPVHVE ILVQTLRYWV KDASSLHLLR
     FFLNKYWNSL ITPKKASSSF STRNQRLFVF LYNSHVSEYE SSFVFLRNQS SHLGSTPFGV
     LLERIYFYGK IERLVNVFVK VKDFRANLWL VKEPCIHYIR YQRKFILASK GTSLFMNKWK
     CYLITFWQWH FSLWFYPRRI YINQLSNHSF AFLGYLSSLR MNPSVVRSQS LENAFLINNA
     IKKVDTLVPI IPMIASLAKA KFCNVFGHPI SKPVRADLSD SNIIDRFGCI CRNFSHYYSG
     SSKKKSLYRI KYILRLSCAR TLARKHKSTV RTFLKKLGSE LLEEFLLSEE DVLFLTFPKA
     SPSLQGVYRS RIWYLDIISI NDLVDHKSKF
 
 
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