SYAP_ORYSI
ID SYAP_ORYSI Reviewed; 996 AA.
AC B8B4H5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=OsI_22356;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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; CM000131; EEC80314.1; -; Genomic_DNA.
DR AlphaFoldDB; B8B4H5; -.
DR SMR; B8B4H5; -.
DR STRING; 39946.B8B4H5; -.
DR EnsemblPlants; BGIOSGA022618-TA; BGIOSGA022618-PA; BGIOSGA022618.
DR Gramene; BGIOSGA022618-TA; BGIOSGA022618-PA; BGIOSGA022618.
DR HOGENOM; CLU_004485_1_1_1; -.
DR OMA; DMEMENQ; -.
DR Proteomes; UP000007015; Chromosome 6.
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 /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT CHAIN ?..996
FT /note="Alanine--tRNA ligase, chloroplastic/mitochondrial"
FT /id="PRO_0000402305"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 779
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
FT BINDING 783
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03134"
SQ SEQUENCE 996 AA; 108149 MW; 9630D73DDFA65B1F CRC64;
MEAAALLSPT ATSRSPLPLL STAPAAHRLH VLLPLSGRRR RLCLRSSPRP RGSLGCAGDC
VVRSMGSSRE RGVLVKTSSS SASVESATQE VGAASSGEWS GDAIRRRFLD FYAARGHKIL
PSSSLVPDDP TVFLTIAGML QFKPIFLGKE PRRVPCATTS QKCIRTNDIE NVGRTSRHQT
FFEMLGNFSF GDYFKKEAIT WAWELTTKEF GLPPERLWIS VFQDDDEAFS IWHNEVGVPK
ERIKRLGEDD NFWTSGATGP CGPCSEIYYD FYPERGSSDA DLGDDSRFIE FYNLVFMQYN
KKDDGSLEPL KQKNIDTGMG LERMARILQK VPNNYETDLI FPIIEKAASM ALVSYTTADD
AMKTNLKIIG DHMRAVVYLI SDGVIPSNIG RGYVVRRLIR RVVRTGRLIG IRGDGHGNSE
GAFLPSLAEV AISLSTEIDP DVESRRKSIL GELQREELRF VQTLERGEKL LDELLDEALS
SAGNNGGKPC LSGKDVFLLY DTYGFPVEIT AEIAGERGVI VDMKGFDMEM ENQRKQSQAA
HNVVKLSVGN ETEIVKSIPD TEFLGYDSLS ATAVVKGLLV NGNSVNVVSE GSDVEIFLDR
TPFYAESGGQ VGDNGFLYVY GEEDAKQKAV IEINDVQKSL GNIFVHKGTI KQGSVEVGKE
IDAAVDAKLR QGAKAHHTAT HLLQSALKSI IGSETSQAGS LVAFDRLRFD FNFHRPLSEE
ELMKIESLVN QWVSSATHLE TKVMDLQDAK NAGAIAMFGE KYGEQVRVVE VPGVSMELCG
GTHVSNTAEI RGFKIISEQG IASGVRRIEA VAGDAFVEYV CARDNYMRCL CSSLKVKAED
VNGRVETILE ELRTTRNEVS SLRSKIAVLK AASLANKATT IDNTRVVVEN MGDVDADGLK
SAAEYLVDTL EDPAAVILGS SPGDGKVSLV AAFSPGVVKM GIQAGKFVGG IAKLCGGGGG
GKPNFAQAGG RKPENLPGAL EKARDEIVAA ISSKSS
