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Database: UniProt/SWISS-PROT
Entry: AASD1_DANRE
LinkDB: AASD1_DANRE
Original site: AASD1_DANRE 
ID   AASD1_DANRE             Reviewed;         412 AA.
AC   Q6DEJ5;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Alanyl-tRNA editing protein Aarsd1;
DE   AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1;
GN   Name=aarsd1; ORFNames=zgc:101066;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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; BC077118; AAH77118.1; -; mRNA.
DR   RefSeq; NP_001003572.1; NM_001003572.1.
DR   AlphaFoldDB; Q6DEJ5; -.
DR   SMR; Q6DEJ5; -.
DR   STRING; 7955.ENSDARP00000011878; -.
DR   PaxDb; 7955-ENSDARP00000011878; -.
DR   GeneID; 445178; -.
DR   KEGG; dre:445178; -.
DR   AGR; ZFIN:ZDB-GENE-040801-91; -.
DR   CTD; 80755; -.
DR   ZFIN; ZDB-GENE-040801-91; aarsd1.
DR   eggNOG; KOG2105; Eukaryota.
DR   InParanoid; Q6DEJ5; -.
DR   OrthoDB; 5490212at2759; -.
DR   PhylomeDB; Q6DEJ5; -.
DR   PRO; PR:Q6DEJ5; -.
DR   Proteomes; UP000000437; Chromosome 12.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.30.130; -; 1.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR   PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..412
FT                   /note="Alanyl-tRNA editing protein Aarsd1"
FT                   /id="PRO_0000277468"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  45517 MW;  4321F90E712F3200 CRC64;
     MAFQCQRDCY MQEFDSCVVS CVPAELKLEN NGRKEKLTGF NVKLKDTILF PEGGGQPDDH
     GTIGGVPVLR VLRQGPDAVH FVSSALEEGQ EVHIKLDWER RFDHMQQHSG QHLITALADT
     MFGYKTTSWD LGRQRSSIEL DTATVKPGEM EALETAVNEK IRAHVPVTVN LLSIDDPAVE
     KVRSRGLPDD HAGPIRIIDI EGVDANMCCG THVSNLSHLQ VIKILGTEKG KKNKTNLIFI
     AGNRVLKYAE KSYNIEKSLT VLLKTGADEH VDAVDKLQKT VKRLQKSNLT ILREMAVLIA
     QNFKSKPDRG HFFSLHNKDG DNEFMNIVAN EIGFQDTLIF MTVGDEKGAG LFLIAGPENI
     VTEVGPRVSE LLQGKGAGKA GRYQGKANSL VKRAEVEALL KERSYKCTAG DE
//
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