ID   AASD1_RAT               Reviewed;         412 AA.
AC   Q5XI97;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Alanyl-tRNA editing protein Aarsd1;
DE   AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1;
GN   Name=Aarsd1;
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 MRNA].
RC   TISSUE=Kidney;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC       incorrectly charged tRNA(Ala). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Alax-L subfamily. {ECO:0000305}.
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DR   EMBL; BC083790; AAH83790.1; -; mRNA.
DR   RefSeq; NP_001029281.1; NM_001034109.1.
DR   AlphaFoldDB; Q5XI97; -.
DR   SMR; Q5XI97; -.
DR   BioGRID; 565992; 1.
DR   STRING; 10116.ENSRNOP00000028047; -.
DR   iPTMnet; Q5XI97; -.
DR   PhosphoSitePlus; Q5XI97; -.
DR   jPOST; Q5XI97; -.
DR   PaxDb; Q5XI97; -.
DR   PRIDE; Q5XI97; -.
DR   Ensembl; ENSRNOT00000028047; ENSRNOP00000028047; ENSRNOG00000020658.
DR   GeneID; 619440; -.
DR   KEGG; rno:619440; -.
DR   UCSC; RGD:1561650; rat.
DR   CTD; 80755; -.
DR   RGD; 1561650; Aarsd1.
DR   eggNOG; KOG2105; Eukaryota.
DR   GeneTree; ENSGT00940000156241; -.
DR   HOGENOM; CLU_004485_7_0_1; -.
DR   InParanoid; Q5XI97; -.
DR   OMA; DREFKYD; -.
DR   OrthoDB; 910848at2759; -.
DR   PhylomeDB; Q5XI97; -.
DR   PRO; PR:Q5XI97; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000020658; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q5XI97; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; ISO:RGD.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006450; P:regulation of translational fidelity; ISO:RGD.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN           1..412
FT                   /note="Alanyl-tRNA editing protein Aarsd1"
FT                   /id="PRO_0000277467"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   412 AA;  45093 MW;  5723CBE2109E54C3 CRC64;
     MAFLCQRDSY AREFTTTVVS CCPAELQTDG NGSKKEVLSG FQVVLEDTLL FPEGGGQPDD
     RGTINDISVL RVTRRGAQAD HFTQTPLSPG SQVQVRVDWE RRFDHMQQHS GQHLITAVAD
     LLFGLKTTSW ELGKLRCVIE LDSPSVTAEQ VAAIEQSVNQ KIRDRLPVSV RELSLDDPEV
     EQVRGRGLPD DHAGPIRVVT IEGVDSNMCC GTHVNNLSDL QVIKILGTEK GKKNKSNLIF
     LAGNRVLKWM ERSHGSEKAL TSLLKCGAED HVEAVKKLQN ATKLLQKNNL NLLRDLAVHT
     AHTLRSSPAW GGVVTLHRKE GDSEFMNIIA NEIGSEETLL FLTVGDEKGA GLFLLAGPTE
     AVETLGPRVA EVLEGKGAGK KGRFQGKATK MSRRAEVQAL LQDYVSTQSA EE