SYAM_RAT
ID SYAM_RAT Reviewed; 985 AA.
AC D3ZX08;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Alanine--tRNA ligase, mitochondrial {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=Aars2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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.
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 -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
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DR EMBL; CH473987; EDM18733.1; -; Genomic_DNA.
DR RefSeq; NP_001100361.1; NM_001106891.1.
DR AlphaFoldDB; D3ZX08; -.
DR SMR; D3ZX08; -.
DR IntAct; D3ZX08; 3.
DR STRING; 10116.ENSRNOP00000037568; -.
DR PaxDb; D3ZX08; -.
DR PeptideAtlas; D3ZX08; -.
DR PRIDE; D3ZX08; -.
DR GeneID; 301254; -.
DR KEGG; rno:301254; -.
DR UCSC; RGD:1310617; rat.
DR CTD; 57505; -.
DR RGD; 1310617; Aars2.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; D3ZX08; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; D3ZX08; -.
DR TreeFam; TF300737; -.
DR PRO; PR:D3ZX08; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 9.
DR Genevisible; D3ZX08; RN.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; ISO:RGD.
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; IBA:GO_Central.
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; ISO:RGD.
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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
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; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; Transit peptide; tRNA-binding; Zinc.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CHAIN 24..985
FT /note="Alanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000402117"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 235..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 237
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 260
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
SQ SEQUENCE 985 AA; 107806 MW; A019BF4379DCADC7 CRC64;
MAASVAAAAG RLRRAIGRSC PWQRFSTEPH PPHGAAVRDA FLSFFRDRHG HRLVPSASVR
PRGDPSLLFV NAGMNQFKPI FLGTVDPRSE MAGFRRVANS QKCVRAGGRH NDLEDVGRDL
SHHTFFEMLG NWAFGGEYFK KEACSMAWEL LTQVYGIPED RLWVSYFSGD SKTGLDPDLE
TRDIWLSLGV PASRVLSFGL QENFWEMGDT GPCGPCTEIH YDLAGGMGPP QLVELWNLVF
MQHYREADGS LHLLPQQHVD TGMGLERLVA VLQGKHSTYD TDLFSPLLDA IHQSCRVPPY
SGRVGAADEG RIDTAYRVVA DHIRTLSVCI ADGVSPGMSG APLVLRRILR RAVRYSTEVL
QAPPGFLGNL VPVVVATLGA AYPELQKNSV KVLIWEIANL VSEDEAAFLA SLQRGRRIID
RTVKRLGPSD LFPAEVAWSL SLSGNLGIPL DLVQLMLEEK GVKLDTAGLE QLAQKEAQHR
AQQAEAAQEE GLCLDVHALE ELHRQGIPTT DDSPKYNYSL RPNGDYEFGL CEAQVLQLYS
ETGTAVASVG EGQRCGLLLD RTNFYAEQGG QASDRGYLIR TGQQDVLFPV ARAQVCGGFI
LHEAMAPECL QVGDRVQLYV DKAWRMGCMV KHTATHLLNW ALRQTLGPTT EQRGSHLNPE
RLRFDVATQT PLTTEQLRTV ESYVQEAVGQ DKPVYMEEVP LAHTARIPGL RSLDEVYPDP
VRVVSVGVPV AQALAPASQA ALQTSVELCC GTHLLSTGAV GDLVIIGDRQ LVKGITRLLA
ITGEQAQQAR EVGQSLSQEV EVASERLSRG SRDLLEAHRL SKDIGRLIEF TESAVIPQWQ
RQEQQTTLKM LQRRANTAIR KLEKSQATEK SQELLKRHSE GPLIVDTVSA QSLSVLVKVV
RQLCKQAPSM SVLLLSPQPT GSVLCACQVA QGATPTFTAE AWALAVCSHM GGKAWGSPVI
AQGTGHTADL EAALRTARAY ALNQL
