SYAP_MICPC
ID SYAP_MICPC Reviewed; 899 AA.
AC C1MR42;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Alanine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03134};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03134};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03134};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03134};
DE Flags: Precursor;
GN ORFNames=MICPUCDRAFT_16345;
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545;
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(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_03134}.
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_03134};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03134};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03134};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03134}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03134}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03134}.
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_03134}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03134}.
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DR EMBL; GG663738; EEH57817.1; -; Genomic_DNA.
DR RefSeq; XP_003057866.1; XM_003057820.1.
DR AlphaFoldDB; C1MR42; -.
DR SMR; C1MR42; -.
DR STRING; 564608.C1MR42; -.
DR GeneID; 9683676; -.
DR KEGG; mpp:MICPUCDRAFT_16345; -.
DR eggNOG; KOG0188; Eukaryota.
DR OMA; DMEMENQ; -.
DR OrthoDB; 129373at2759; -.
DR Proteomes; UP000001876; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR HAMAP; MF_03134; Ala_tRNA_synth_plantC; 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; IPR027522; Ala_tRNA_synth_plant.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT CHAIN ?..899
FT /note="Alanine--tRNA ligase, chloroplastic/mitochondrial"
FT /id="PRO_0000402304"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
SQ SEQUENCE 899 AA; 95154 MW; 50631B1782D30122 CRC64;
MRDADGKDIS GAGIRRRFLE FYEARDHARL PSSSLVPEDP TVLLTIAGML QFKPVFMGQE
ERKVPTATTT QKCVRTNDIE NVGVTARHHT FFEMLGNFSF GDYFKKEAIA WAWEISTKEY
GLDASRIWIS VFREDDEAYA IWRDEIGIPE NRIKRMDEAD NFWAAGPTGP CGPCSELYWD
FHPERGVDGS EDLDDDSRFI EFYNLVFMES VRDTDGNMKP LKRKNIDTGM GLERMAQILQ
GKPNNYETDL IRPIIDAAAS MAGISYDDAD DATKLKLKVI GDHTRAVCYL ISDGVLPSNV
GRGYIVRRLL RRVVRCGRLL GVKAPDGAGA FTPAIARVAI GLSEACDANV LKSSQKICDE
LEREELRFAT TLGRGEEILA DMLAAAKTKD ANAPKLTGED AFTLYDTYGF PLDITTDVAT
EAGVDVDVDG FEKAMAAARD LSRDARVAVD VTVGDLLGAI ADELGEPTRF TGYGSVTEEG
VKVRALLKGG ERVASAGAGD TVEVVLDATP FYAEGGGQVG DEGEIILSDD RGKLVVGDCR
KAAGGRLFVH SCVVSEGVVG EGDAVTATVS AASRRRAKAN HTATHLLQSA LKMTIGEDVS
QAGSLVNFER LRFDFNAPSA PTPEELARVE SLVNGWIGDA IDLTAEEMAI SRAKEKGATA
MFGEKYGDVV RVVDVPGVSM ELCGGTHVKN TAEIGGFKIL SESGIAAGVR RIEAVSGPGV
VDLLQERDGT VKALAGSLRV PPEEIAGRVS ALMEDLKTSQ KEAEALRGEL AVAKATALAS
QAIDAPGGAK VLVARMDGVD PAALKAAAES LVAALGDDVA VVLGSGGDDG KVGLVASFTE
GVQKAGGLKA GVVLGATAKA CGGGGGGKPG FAQAGGRDAS ALDAALEDAK KTIVDALSK
