SYAC_RAT
ID SYAC_RAT Reviewed; 968 AA.
AC P50475; A6IZ80; Q4G057;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 3.
DT 03-AUG-2022, entry version 133.
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=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
GN Name=Aars1; Synonyms=Aars;
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].
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.
RN [2]
RP PROTEIN SEQUENCE OF 456-476.
RC TISSUE=Liver;
RX PubMed=2040280; DOI=10.1111/j.1432-1033.1991.tb16002.x;
RA Dignam J.D., Dignam S.S., Brumley L.L.;
RT "Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori and Ratus ratus.
RT Existence of common structural features.";
RL Eur. J. Biochem. 198:201-210(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-968.
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
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. Interacts with ANKRD16; the interaction is direct.
CC {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 -!- PTM: ISGylated. {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; CH473972; EDL92558.1; -; Genomic_DNA.
DR EMBL; BC098738; AAH98738.1; -; mRNA.
DR PIR; S16073; S16073.
DR RefSeq; NP_001093987.1; NM_001100517.1.
DR RefSeq; XP_006255642.1; XM_006255580.3.
DR RefSeq; XP_006255643.1; XM_006255581.2.
DR RefSeq; XP_006255644.1; XM_006255582.3.
DR RefSeq; XP_006255645.1; XM_006255583.3.
DR AlphaFoldDB; P50475; -.
DR SMR; P50475; -.
DR IntAct; P50475; 1.
DR STRING; 10116.ENSRNOP00000025051; -.
DR iPTMnet; P50475; -.
DR PhosphoSitePlus; P50475; -.
DR jPOST; P50475; -.
DR PaxDb; P50475; -.
DR PRIDE; P50475; -.
DR Ensembl; ENSRNOT00000025052; ENSRNOP00000025051; ENSRNOG00000018404.
DR GeneID; 292023; -.
DR KEGG; rno:292023; -.
DR UCSC; RGD:1304832; rat.
DR CTD; 16; -.
DR RGD; 1304832; Aars.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000157335; -.
DR InParanoid; P50475; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; P50475; -.
DR TreeFam; TF300737; -.
DR PRO; PR:P50475; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000018404; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P50475; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IDA:RGD.
DR GO; GO:0016597; F:amino acid binding; IPI:RGD.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IPI:RGD.
DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IDA:RGD.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; ISO:RGD.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Ubl conjugation; Zinc.
FT CHAIN 1..968
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000075284"
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 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49588, ECO:0000255|HAMAP-
FT Rule:MF_03133"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT MOD_RES 876
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT CONFLICT 459
FT /note="G -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..476
FT /note="RAK -> ARA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 106790 MW; 10BF81F46F7AF546 CRC64;
MDSTLTAREI RERFINYFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTVDPS
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE
LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL ECRQIWQNLG LDEAKILPGN MKDNFWEMGD
TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT
GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDTDG IDMAYRVLAD
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV DVVVQSLGDA
FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDCQTIPGDT AWLLYDTYGF
PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRAKGLEA
TDDSPKYNYH SDSSGSYVFE CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG
QIFDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLRVGDQVR LFIDEPRRRP
VMSNHTATHI LNFALRSVLG DADQKGSLVA PDRLRFDFTA KGAMSTEQIK KTEEIVNGMI
EAAKPVYTLD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV
EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKSETL KKSLSAMEVK
VKAQSAPNKD VQKEIADLGE VLATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR
VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE ALQLATSFAQ
LRLGDVKN
