SYA_ARATH
ID SYA_ARATH Reviewed; 1003 AA.
AC P36428; O04159; Q8GUG2; Q9SX40;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
DE Flags: Precursor;
GN Name=ALATS; Synonyms=ALARS; OrderedLocusNames=At1g50200; ORFNames=F14I3.17;
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] (ISOFORMS CYTOPLASMIC AND MITOCHONDRIAL).
RC STRAIN=cv. Columbia;
RX PubMed=8672889; DOI=10.2307/3870213;
RA Mireau H., Lancelin D., Small I.;
RT "The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-
RT tRNA synthetases.";
RL Plant Cell 8:1027-1039(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM CYTOPLASMIC).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 753-1003, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9669027; DOI=10.1038/cr.1998.12;
RA Ge S.J., Yao X.L., Yang Z.X., Zhu Z.P.;
RT "An Arabidopsis embryonic lethal mutant with reduced expression of alanyl-
RT tRNA synthetase gene.";
RL Cell Res. 8:119-134(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged tRNA(Ala) via its editing domain.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=P36428-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=P36428-2; Sequence=VSP_018903;
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. Developmental arrest of the
CC embryo at the globular stage. {ECO:0000305|PubMed:9669027}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50044.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z22673; CAA80380.1; -; mRNA.
DR EMBL; Z22673; CAA80381.1; -; mRNA.
DR EMBL; AC007980; AAD50044.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE32524.1; -; Genomic_DNA.
DR EMBL; BT002526; AAO00886.1; -; mRNA.
DR EMBL; BT008807; AAP68246.1; -; mRNA.
DR EMBL; Y12555; CAA73145.1; -; mRNA.
DR PIR; D96538; D96538.
DR RefSeq; NP_175439.2; NM_103905.4. [P36428-1]
DR AlphaFoldDB; P36428; -.
DR SMR; P36428; -.
DR BioGRID; 26667; 11.
DR STRING; 3702.AT1G50200.1; -.
DR iPTMnet; P36428; -.
DR PaxDb; P36428; -.
DR PRIDE; P36428; -.
DR ProteomicsDB; 228055; -. [P36428-1]
DR EnsemblPlants; AT1G50200.1; AT1G50200.1; AT1G50200. [P36428-1]
DR GeneID; 841442; -.
DR Gramene; AT1G50200.1; AT1G50200.1; AT1G50200. [P36428-1]
DR KEGG; ath:AT1G50200; -.
DR Araport; AT1G50200; -.
DR TAIR; locus:2011962; AT1G50200.
DR eggNOG; KOG0188; Eukaryota.
DR InParanoid; P36428; -.
DR OMA; DTEACCG; -.
DR PhylomeDB; P36428; -.
DR PRO; PR:P36428; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P36428; baseline and differential.
DR Genevisible; P36428; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Ligase; Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide;
KW tRNA-binding; Zinc.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT CHAIN 50..1003
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000035793"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 769
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:8672889"
FT /id="VSP_018903"
FT CONFLICT 194
FT /note="G -> R (in Ref. 1; CAA80380/CAA80381)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="V -> A (in Ref. 1; CAA80380/CAA80381)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="R -> Q (in Ref. 1; CAA80380/CAA80381)"
FT /evidence="ECO:0000305"
FT CONFLICT 985
FT /note="S -> F (in Ref. 5; CAA73145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 110489 MW; 0A85DA940C5BB308 CRC64;
MRLVKAASLL ISSTKPPSRV FYSSHLRRPF FSHFRFSSSS STSSSVAVMP GSEPSETQWP
AKRVRDTYVD FFRGKGHKFW PSSPVVPHND PTLLFANAGM NQYKPIFLGT ADPNTELSKL
SRACNTQKCI RAGGKHNDLD DVGKDTYHHT FFEMLGNWSF GDYFKKEAIE WAWELLTKVY
GLPTDRIYAT YFGGDEKAGL QPDNEARDIW LKVLPSGRVL PFGCKDNFWE MGDTGPCGPC
TEIHYDRIGN RDAASLVNND DPTCLEIWNL VFIQFNRESD GSLKPLPAKH VDTGMGFERL
TSVLQNKMSN YDTDVFMPIF DDIQKATGAR PYSGKVGPED VDRVDMAYRV VADHIRTLSF
AIADGSRPGN EGREYVLRRI LRRAVRYGKE ILKAEEGFFN GLVSSVIRVM GDVFTELKEH
EKKITDIIKE EEASFCKTLA KGIEKFRKAG QAVQGNTLSG DDAFILWDTY GFPLDLTQLM
AEERGLLVDV DGFNKAMEEA RERSRSAQNK QAGGAIVMDA DATSTLHKAG VSATDDSFKY
IWFQDHESEL KAIYTGSTFL ESSAASDNVG LVLGSTSFYA EQGGQIFDTG LIEGSFGTFN
VCNVQIFGGF VLHIGYLSKE TGEVSVGDKV ICKVDYERRK LIAPNHTCTH MLNYALKEVL
GDHIDQKGSI VLPEKLRFDF SHGKPVDPED LRRIESIVNK QIKDELDVFS KEAVLSEAKR
IKGLRAVFGE VYPDPVRVVS IGRKVEDLLA DPENNEWSLL SSEFCGGTHI TNTREAKAFA
LLSEEGIAKG IRRVTAVTTE CAFDALNAAS LLEREVEDAS RAEGSALEKK VSALKSRVDA
AIIPAAKKAD IRTKIASLQN EVRKAQKKIA EQNLKKSVKL ATEAAESAAS DGKTFCIIQL
DVGLDAAAVR EAVSKVMEKK GMSIMVFSTD ESTNKAVVCA GVPEKSDQFK PLDVTEWLTT
ALGPLKGRCG KGKGGLASGQ GTDASQVQAA LDMASSFASM KLN
