ID   ALAXL_PYRHO             Reviewed;         404 AA.
AC   O57734;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Alanyl-tRNA editing protein AlaX-L;
DE            Short=AlaX-L;
DE   AltName: Full=Alanyl-tRNA deacylase AlaX-L;
GN   Name=alaXL; OrderedLocusNames=PH1969;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC       mischarged charged tRNA(Ala). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Editing domain AlaX-L subfamily. {ECO:0000305}.
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DR   EMBL; BA000001; BAA31096.1; -; Genomic_DNA.
DR   PIR; A71213; A71213.
DR   RefSeq; WP_010886033.1; NC_000961.1.
DR   AlphaFoldDB; O57734; -.
DR   SMR; O57734; -.
DR   STRING; 70601.3258413; -.
DR   EnsemblBacteria; BAA31096; BAA31096; BAA31096.
DR   GeneID; 1442815; -.
DR   KEGG; pho:PH1969; -.
DR   eggNOG; arCOG01254; Archaea.
DR   OMA; IACQHTA; -.
DR   OrthoDB; 40337at2157; -.
DR   Proteomes; UP000000752; Chromosome.
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; IEA:UniProt.
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:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
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   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   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Zinc.
FT   CHAIN           1..404
FT                   /note="Alanyl-tRNA editing protein AlaX-L"
FT                   /id="PRO_0000391650"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  46804 MW;  A86DBEBCA8A95C22 CRC64;
     MVERVYYKDP YLREIDAKIV DVRKEKDRVE VVLDRTIFYP EGGGQPGDRG VIKGNDFEIM
     VEDTIEKNGE IFHIGKLRGE IPKEGEKVKL YLDWEWRYGN MQMHTGQHIL SAVLKKLYDL
     DTTGFNIFRD YAKIEVNGEV NWDMIERAEL EVNKIIINDL PVVIEEYDKL PEEIALKLRK
     NVTKVKEKIR IVKIGDVDVT PCGGTHVKST REVGIIKVLR FYKKSKNLWR IEFTCGYRAI
     SKMNEILRDY WGSLDLMPNK NPPLIERINE VLRTVNSLEN RIEELRREIW EWKGKALLKE
     GVKVGNYTVI THVENWNMKD AQAFAIDFVK KNSNTILLLA NEKYVLFAKN EGVPVSMREL
     LKEVIDELGG KGGGTDNLAR GRVEAKPEEI FDVALEKLRS HLQV