ID   SYA_PYRCJ               Reviewed;         896 AA.
AC   A3MXP1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   04-NOV-2026, entry version 90.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036};
GN   OrderedLocusNames=Pcal_1993;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC       domain. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP +
CC         diphosphate; 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_00036};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
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_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000561; ABO09408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MXP1; -.
DR   SMR; A3MXP1; -.
DR   STRING; 410359.Pcal_1993; -.
DR   KEGG; pcl:Pcal_1993; -.
DR   eggNOG; arCOG01255; Archaea.
DR   HOGENOM; CLU_004485_4_0_2; -.
DR   OMA; AAAKWMY; -.
DR   Proteomes; UP000001431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase activity; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00673; AlaRS_core; 1.
DR   FunFam; 2.40.30.130:FF:000010; Alanine--tRNA ligase; 1.
DR   FunFam; 3.30.930.10:FF:000056; Alanine--tRNA ligase; 1.
DR   FunFam; 3.30.980.10:FF:000004; Alanine--tRNA ligase, cytoplasmic; 1.
DR   Gene3D; 2.40.30.130; -; 1.
DR   Gene3D; 3.10.310.40; -; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 3.30.980.10; Threonyl-trna Synthetase, Chain A, domain 2; 1.
DR   HAMAP; MF_00036_A; Ala_tRNA_synth_A; 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; IPR022429; Ala-tRNA_lgiase_arc.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   NCBIfam; TIGR03683; A-tRNA_syn_arch; 1.
DR   NCBIfam; TIGR00344; alaS; 1.
DR   PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
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..896
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_1000074514"
FT   BINDING         599
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         603
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         707
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         711
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   896 AA;  100700 MW;  D44383DF1B4BA50E CRC64;
     MQKTQMLSAE IFRRRGHIRK QCPLCKSHFW TLRPDQEVCG DQPCTPYGFI GNPPTKVAVE
     SLRDVRERFL SFFERHGHAR IKRYPVVARW RDDVYLVGAS IYDFQPWVTS GAVPPPANPL
     TISQPSIRLT DVDKVGRSGR HLTGFEMMAH HAFNYPDKYV YWIDETTEYA YRFFTEELGI
     PPEEITFKES MWEGGGNAGE CFEVLVRGLE AATLVFMHYE VKDGKYVELP LKIVDTGYGL
     ERIYWLIKGT PTIYDAVFGP YLAKVRERLG VPEPPRDVMA KASIYFGQMD PEVISLDKAY
     DIIAEKIGVD GKWLREVVKP QEALYVLADH SRTVAWMIAD GVIPSNSGAG YLARLLIRRA
     LRGLMLAGVD APLVELFDLH LKELRYDYPE VWEARSLILE LVDMEEKKYR EVLKSAPAVV
     KRALEENRRR GKAGLDKEDL VTLYDSYGLP PEVVAEAAKS MGIEVKVPDD FYSLLASRHV
     RREKGREATL VEMAKVADLP RTRELFYEDA YMRTFKAKVL RVIDGKYVVL DQTAFYAEGG
     GQPADTGVLR HSGGVAKVVD VQRVGHVIVH VVEGDVPQEG SEVVGEVDWE RRYALMKMHT
     GTHVLIQSIR RVLGPHIWQA GAQKDIPFSR IDVTHYKLPT PEEVAKIERL ANDVVQRDLP
     VYVKVMPRNE AEAKYGFILY QGGVVPAREI RVVQIGPDDE PYDVQACGGT HLRRTGEIGL
     IKVHKVERIA DGVVRFIFTT GPHAVAYVQE LERQAAEAAA LGGGSKEELV EVVKRLLKRA
     EEAEKKARHY AELYAAALAE NLKAEAVGQR RLAVVELDDE ELAKRVALLA TKRDPDLVLV
     VKAGERVTIY TGGVDVGPIV KALREIGFRG GGSKTFAQGV YAGDVEKLKE AIRRAL
//