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SYMM_ARATH
ID   SYMM_ARATH              Reviewed;         616 AA.
AC   Q9M2T9; O23761; Q9ASP8;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Methionine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE            EC=6.1.1.10 {ECO:0000305};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000305};
DE            Short=AtcpMetRS {ECO:0000303|PubMed:9724821};
DE            Short=MetRS {ECO:0000305};
DE   AltName: Full=Protein OVULE ABORTION 1 {ECO:0000303|PubMed:16297076};
DE   Flags: Precursor;
GN   Name=OVA1 {ECO:0000303|PubMed:16297076};
GN   OrderedLocusNames=At3g55400 {ECO:0000312|Araport:AT3G55400};
GN   ORFNames=T22E16.60 {ECO:0000312|EMBL:CAB75898.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=9724821; DOI=10.1073/pnas.95.18.11014;
RA   Menand B., Marechal-Drouard L., Sakamoto W., Dietrich A., Wintz H.;
RT   "A single gene of chloroplast origin codes for mitochondrial and
RT   chloroplastic methionyl-tRNA synthetase in Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11014-11019(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA   Berg M., Rogers R., Muralla R., Meinke D.;
RT   "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT   development in Arabidopsis.";
RL   Plant J. 44:866-878(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17433818; DOI=10.1016/j.jmb.2007.03.015;
RA   Pujol C., Marechal-Drouard L., Duchene A.M.;
RT   "How can organellar protein N-terminal sequences be dual targeting signals?
RT   In silico analysis and mutagenesis approach.";
RL   J. Mol. Biol. 369:356-367(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17433818, ECO:0000269|PubMed:9724821}.
CC       Mitochondrion {ECO:0000269|PubMed:17433818,
CC       ECO:0000269|PubMed:9724821}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According EST sequences.
CC         {ECO:0000305};
CC       Name=1;
CC         IsoId=Q9M2T9-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC       {ECO:0000269|PubMed:16297076}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; Y13943; CAA74281.1; -; mRNA.
DR   EMBL; AL132975; CAB75898.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79379.1; -; Genomic_DNA.
DR   EMBL; AF367354; AAK32940.1; -; mRNA.
DR   EMBL; AY133597; AAM91427.1; -; mRNA.
DR   PIR; T47679; T47679.
DR   PIR; T50641; T50641.
DR   RefSeq; NP_191100.1; NM_115398.3. [Q9M2T9-1]
DR   AlphaFoldDB; Q9M2T9; -.
DR   SMR; Q9M2T9; -.
DR   STRING; 3702.AT3G55400.1; -.
DR   PaxDb; Q9M2T9; -.
DR   PRIDE; Q9M2T9; -.
DR   ProteomicsDB; 234126; -. [Q9M2T9-1]
DR   EnsemblPlants; AT3G55400.1; AT3G55400.1; AT3G55400. [Q9M2T9-1]
DR   GeneID; 824706; -.
DR   Gramene; AT3G55400.1; AT3G55400.1; AT3G55400. [Q9M2T9-1]
DR   KEGG; ath:AT3G55400; -.
DR   Araport; AT3G55400; -.
DR   TAIR; locus:2099966; AT3G55400.
DR   eggNOG; KOG0436; Eukaryota.
DR   InParanoid; Q9M2T9; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 788159at2759; -.
DR   PhylomeDB; Q9M2T9; -.
DR   BRENDA; 6.1.1.10; 399.
DR   PRO; PR:Q9M2T9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M2T9; baseline and differential.
DR   Genevisible; Q9M2T9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IDA:TAIR.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast;
KW   Ligase; Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..616
FT                   /note="Methionine--tRNA ligase,
FT                   chloroplastic/mitochondrial"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433535"
FT   REGION          582..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           78..88
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000305"
FT   MOTIF           366..370
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000305"
FT   BINDING         369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        99
FT                   /note="A -> S (in Ref. 1; CAA74281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="E -> G (in Ref. 4; AAK32940/AAM91427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="M -> I (in Ref. 1; CAA74281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="I -> V (in Ref. 1; CAA74281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        547
FT                   /note="T -> S (in Ref. 1; CAA74281)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   616 AA;  69274 MW;  1E6A0B4DE127B4DC CRC64;
     MAARINTSLH NALSFLKPFN TPLNTKPFSF RRNSFRFSKK LPYYSQFSSG KRALYCTSSS
     QESTVDEGET FVLTTPLYYV NAPPHMGSAY TTIAADSIAR FQRLLGKKVI FITGTDEHGE
     KIATSAAANG RNPPEHCDLI SQSYRTLWKD LDIAYDKFIR TTDPKHEAIV KEFYARVFAN
     GDIYRADYEG LYCVNCEEYK DEKELLENNC CPVHQMPCVA RKEDNYFFAL SKYQKPLEDI
     LAQNPRFVQP SYRLNEVQSW IKSGLRDFSI SRALVDWGIP VPDDDKQTIY VWFDALLGYI
     SALTEDNKQQ NLETAVSFGW PASLHLIGKD ILRFHAVYWP AMLMSAGLEL PKMVFGHGFL
     TKDGMKMGKS LGNTLEPFEL VQKFGPDAVR YFFLREVEFG NDGDYSEDRF IKIVNAHLAN
     TIGNLLNRTL GLLKKNCEST LVVDSTVAAE GVPLKDTVEK LVEKARTNYE NLSLSSACEA
     VLEIGNAGNT YMDQRAPWFL FKQGGVSAEE AAKDLVIILE VMRVIAVALS PVAPCLSLRI
     YSQLGYTEDQ FNSITWSDTK WGGLKGGQVM EQASPVFARI ELNPEKEEDE KKPKVGKKTG
     KAKVKVVEQT PTVAEA
 
 
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