SYAC_CAEEL
ID SYAC_CAEEL Reviewed; 968 AA.
AC O01541; Q17371;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alanine--tRNA ligase, cytoplasmic {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=AlaRS A;
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
GN Name=aars-2 {ECO:0000255|HAMAP-Rule:MF_03133}; Synonyms=ars-2;
GN ORFNames=F28H1.3;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-272.
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).
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: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.
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; FO081252; CCD70212.1; -; Genomic_DNA.
DR EMBL; U41660; AAA84420.1; -; mRNA.
DR PIR; T29466; T29466.
DR RefSeq; NP_491281.1; NM_058880.3.
DR AlphaFoldDB; O01541; -.
DR SMR; O01541; -.
DR BioGRID; 37458; 11.
DR IntAct; O01541; 1.
DR STRING; 6239.F28H1.3.3; -.
DR EPD; O01541; -.
DR PaxDb; O01541; -.
DR PeptideAtlas; O01541; -.
DR PRIDE; O01541; -.
DR EnsemblMetazoa; F28H1.3.1; F28H1.3.1; WBGene00000197.
DR EnsemblMetazoa; F28H1.3.2; F28H1.3.2; WBGene00000197.
DR GeneID; 171985; -.
DR KEGG; cel:CELE_F28H1.3; -.
DR UCSC; F28H1.3.1; c. elegans.
DR CTD; 171985; -.
DR WormBase; F28H1.3; CE09768; WBGene00000197; aars-2.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000157335; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; O01541; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; O01541; -.
DR PRO; PR:O01541; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000197; Expressed in adult organism 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; 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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..968
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000402113"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 214..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 216
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 239
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 728
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT CONFLICT 272
FT /note="K -> Q (in Ref. 1; AAA84420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 106782 MW; BE81FBDD0D3E2055 CRC64;
MKHLTASEVR STFINFFREK KEHTYVHSSS VIPHDDPTLL FANAGMNQFK PLFLGIADPN
SDLAKLKRAV NTQKCIRAGG KHNDLDDVGK DVYHHTYFEM LGNWSFGDYF KKEIITWAWE
LLTTVYGIPA ERLYVSVFGG DEANGVPADS EARDIWRSVG VPDERILNFG MKDNFWEMGD
VGPCGPCSEI HYDRIGNRDA SHLVNADDPM VVEIWNLVFI QFNREEGGVL KPLPAKHIDC
GLGLERLIAV MQDKTSNYDT DIFQPIFEAI HKGSGVRAYT GFIGDEDKDG VDMAYRVVAD
HVRTLTIALS DGGRPDNSGR GYVLRRILRR GVRYASEKLN AQPGFFASLV PVVISILGET
FPELSRDPVT VMDIINDEEK QFLKTLSRGR VLFQRAVQSL PEGTMTFPGD VSWRLYDTYG
FPADLTQLMA EEKGLSVDNT AFEEARRKAI ETSSAGTGKF RDTLDLDVHA LAELQQKGVP
TTDDSPKYAY TFTGEGSDAV YKFEPCVGKI LAIRRDGKFV DQLAAGEEGA ILLDRTNFYA
EQGGQIYDVG VLTKVNDESN EFNVSNCQVR GGYIVLVGSA EGSFSVGDQV NERFDEDRKQ
LIMKNHTGTH VLNYALRKVL ADSDQKGSLV APDRMRFDFT NKAGMTVQQV KKAEEYAQQL
IDTKGQVYAK NSPLGEAKKV KGLRAMFDET YPDPVRVVAV GTPVEQLLQN PDAEEGQNTT
VEFCGGTHLQ NVSHIGRIVI ASEEAIAKGI RRIVALTGPE AERAIARADR LTARLEEESK
HADKKDELLA NKDKFKALQK KIQEIVDEAN GAQLPYWRKD SIREKAKAIQ KTLDGYTKAQ
QAAVAEKVLG EAKELAAVAE QPTVLVHVFA ANANSKAIDN ALKLLKDTKA VMAFSVNEDS
GKVLCLAKVD KSLVSNGLKA NEWVNEVCTV LGGKGGGKDA NAQLTGENVD KLDAAVELAQ
KFALAAIN
