SYAP_OSTTA
ID SYAP_OSTTA Reviewed; 976 AA.
AC Q015G2; A0A090M7L5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Probable 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 OrderedLocusNames=Ot07g01880 {ECO:0000312|EMBL:CEF98677.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595;
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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; CAID01000007; CEF98677.1; -; Genomic_DNA.
DR AlphaFoldDB; Q015G2; -.
DR SMR; Q015G2; -.
DR STRING; 70448.A0A090M7L5; -.
DR PRIDE; Q015G2; -.
DR eggNOG; KOG0188; Eukaryota.
DR InParanoid; Q015G2; -.
DR OrthoDB; 129373at2759; -.
DR Proteomes; UP000009170; Chromosome 7.
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; 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: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 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..54
FT /note="Chloroplast and mitochondrion"
FT CHAIN 55..976
FT /note="Probable alanine--tRNA ligase,
FT chloroplastic/mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT /id="PRO_0000402308"
FT REGION 71..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 104285 MW; 1DC125E90AD04A01 CRC64;
MPRPGFAHAT APALAHARAR ISPVARRRVV VMRTRVDGAA KSLVTQLRLA LGSTASRASS
IASARRRVRA LGTATNDQST GTRANPNAEG KDNSGRGIRR RFLEFYEARG HSRQPSASLV
PEDPTVLLTI AGMLQFKPVF MGQREREMPR ATTTQKCVRT NDIENVGVTA RHHTFFEMLG
NFSFGDYFKR EACEWAWELA TNEFGLNPER VWVSVFREDD EAFAIWRDVV GVPESRIKRM
DEKDNFWAAG PTGPCGPCSE LYYDFHPERG LDGADLDDDS RFIEFYNLVF MELNRDADGG
IKPLKNKNID TGMGLERMAQ ILQGVSNNYE TDLIRPIIDK AASMAGLDYA SCSATQKQQL
KVIGDHTRAV TYMISDGVFA SNIGRGYIVR RLLRRVVRNG RLLGIKPADG QSAFTPSIAE
VAISMSEECD PQVVKNTARI LAELEREELS FQKTLGRGEE MLAELIEKAK DSKSGLSGKD
AFTLYDTYGF PLDITTDVAS EAGIAVDLEG FEKAMAEQRS MSQAAHQTVD VTAGNALAQV
ADELGAMSEF IGYDNISSDV SNVLAIVSGG ESVEEASGGA RVDVVLDVTP FYAESGGQVG
DNGFLHSADG AVLKVTDVQK AGGGRIIVHS ATVVKGSIKK GSQVSANVDE NARRRARNNH
TATHLLQSAL KKVLGDDVSQ AGSLCGFDRL RFDFNCPKAV TEAQLLEVET LVNGWISQSA
DLTAEEMPIA AAKEKGATMM FGEKYGDVVR VVDVPGISME LCGGTHVSNT AEIGGFKIIS
EAGIASGIRR IEAVAGAGVV ELLQQRDAVV KQLASTLRVP PEEIASRVSG MQKDLVAAQK
LAESLRGELA VAKANALVSE ARAVGESKVL VARLDGVDPG ALKVAAENLA TQLGDGAAVI
LGSANGDNVG LVALFDTKVQ KDGDLKAGQV LGAAAKRCGG GGGGKPGFAQ AGGRDATQLD
AALDEALQTL TTALDK
