SYAM_CAEEL
ID SYAM_CAEEL Reviewed; 793 AA.
AC Q23122; Q9U6B7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=AlaRS B;
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Flags: Precursor;
GN Name=aars-1 {ECO:0000255|HAMAP-Rule:MF_03133}; Synonyms=alas, ars-1;
GN ORFNames=W02B12.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=Bristol N2;
RX PubMed=9636067; DOI=10.1021/bi9804636;
RA Chihade J.W., Hayashibara K., Shiba K., Schimmel P.;
RT "Strong selective pressure to use G:U to mark an RNA acceptor stem for
RT alanine.";
RL Biochemistry 37:9193-9202(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 ECO:0000269|PubMed:9636067}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
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; AF188715; AAF05590.1; -; mRNA.
DR EMBL; Z66521; CAA91396.2; -; Genomic_DNA.
DR PIR; T26086; T26086.
DR RefSeq; NP_496444.1; NM_064043.5.
DR AlphaFoldDB; Q23122; -.
DR SMR; Q23122; -.
DR STRING; 6239.W02B12.6a; -.
DR EPD; Q23122; -.
DR PaxDb; Q23122; -.
DR PeptideAtlas; Q23122; -.
DR EnsemblMetazoa; W02B12.6a.1; W02B12.6a.1; WBGene00000196.
DR GeneID; 174749; -.
DR KEGG; cel:CELE_W02B12.6; -.
DR UCSC; W02B12.6a; c. elegans.
DR CTD; 174749; -.
DR WormBase; W02B12.6a; CE28096; WBGene00000196; aars-1.
DR eggNOG; KOG0188; Eukaryota.
DR HOGENOM; CLU_004485_5_1_1; -.
DR InParanoid; Q23122; -.
DR OMA; GEIAWML; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; Q23122; -.
DR PRO; PR:Q23122; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000196; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 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: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 1: Evidence at protein level;
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CHAIN ?..793
FT /note="Alanine--tRNA ligase, mitochondrial"
FT /id="PRO_0000402118"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 224..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 226
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 249
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 706
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
SQ SEQUENCE 793 AA; 89502 MW; 6A9F309B13D39A26 CRC64;
MGIGSKILEN NIQKSISLGF YHSHSELRKS FYEFFKSKNH EILRSSSVIP DENDGTLLFT
NAGMNQFKPL ILSSTESRRV ANIQKCIRAG GKHNDLDDVG KDLHHQTFFE MMGNWSFNDA
FSKEEACRYA WEYLVEILGI NADRLYVSYF GGIEKLGLPE DRECREIWKR IGVSSNRILP
FVAENFWEMG AAGPCGPCTE IHYDRIGGRD ASRLVNIDDS VVEIWNIVFM SSVRDSCGQI
RHLGKNHIDT GMGFERLLSV VQNKTSNFDT DVFTPILEKT SELAKKQYTG SLDSRQDATF
RLVADHIRAA TVAISDGAVP DGTGCGFIVR KMMRRAFLQG ISKLGIERYA MSELVPVVAS
TMKEVYPEIH DTSTHIRKIF NDEEAQFWKT VDKAKKMFDS VAAESKSPII SGRKAFNLFE
THGLPLAVTV ELARNIGREV DETEFERCRL EAQKVSQKAS QFKLPISADD FPSHSDKEKY
SYVFRNGKYE FPQVKTRILQ VYKDQQKAES LEANDRGFLV LEECQFYGEQ GGQTSDTGHL
LIDGREVFEV ENAKKIAGGA VTVLFGRALL PIRRDLRVEQ KLDETRREGV MRAHSATHLL
NWALQKLGVG SGQKGSSVDC DRFRFDYSTG DEDLSKEQRT ELLIKCEMKM REFIQNGGFT
EIIETSLEEA KKIENLQSDV KEDRIGGASV RVVALGSGAD VPVECCSGTH IHDVRVIDDV
AIMSDKSMGQ RLRRIIVLTG KEAAACRNYT KSIYEDLRST DPKERSKTGK NIDWKRVPIA
DQARISILLK QKK
