ID   SYA_PYRAE               Reviewed;         892 AA.
AC   Q8ZSV6;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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}; OrderedLocusNames=PAE3565;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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=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_00036};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; AE009441; AAL65007.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZSV6; -.
DR   SMR; Q8ZSV6; -.
DR   STRING; 178306.PAE3565; -.
DR   EnsemblBacteria; AAL65007; AAL65007; PAE3565.
DR   KEGG; pai:PAE3565; -.
DR   PATRIC; fig|178306.9.peg.2683; -.
DR   eggNOG; arCOG01255; Archaea.
DR   HOGENOM; CLU_004485_4_0_2; -.
DR   InParanoid; Q8ZSV6; -.
DR   OMA; YHHTMFE; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR   Gene3D; 3.30.930.10; -; 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   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; TIGR03683; A-tRNA_syn_arch; 1.
DR   TIGRFAMs; TIGR00344; alaS; 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..892
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075272"
FT   BINDING         594
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         598
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         702
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         706
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   892 AA;  100033 MW;  B677EF17883846E8 CRC64;
     MLSARVLKNT GFLRKQCPLC KSYFWTLRRD QEYCGDQPCV PYGFIGNPPT KISIDSLTEL
     RERFLRFFER RGHARIKRYP VVARWRDDVY LVGASIYDFQ PWVTSGAVPP PANPLVISQP
     SIRLTDVDKV GRSGRHLTGF EMMAHHAFNY PDKFIYWIDE TAEYAYEFFT KELGIPPEEI
     TFKESIWEGG GNAGECFEVL VRGLEVATLV FMHYEVKEGK YVELPLKIVD TGYGLERIYW
     LIRGTPTIYD AVFGPYLDKA RRSLGFPEPP SELMGKASVY FGQMDPEVIG LEKAYDIIAE
     KIGVDPKWLR EVFKPQEALY VLADHSRTVS WMIADGVIPS NSGAGYLARL LLRRILKNLK
     LVGVETPLVE LFDMHLKELK ADYPEVWEAR NLILELVDIE ERKYREILKS APGVVKKAYE
     EARRRGRAGF DAEDLVSLYD SFGLPPEIVA ETAKSLGVEV KIPDDFYSRL AARHAKREKQ
     PEKTLVEMAK IADLPRTREL FYEDPYMKSF KAKVLRVIDG KYVVLDQTAF YAEGGGQPAD
     IGILKHGGGA AKVVDVQRVG HVIVHVVEGE APPEGSEVVG EIDWDRRYAL MKMHTGTHVL
     IQSIRRVLGP HIWQAGAQKD IPASRIDVTH FKLPTAEEVA EIERLANSVV QANMPVHVKI
     LPRNEAEAKY GFILYQGGVV PAREIRVVQI GPDEAPYDVQ ACGGTHLKST GEIGLIKIQK
     VERIADGVVR FIFTTGLHAL KYVQEIERQV AEAASLAGGN RDNLVDSVRR LLQRAEEAER
     KAQRYTELYA AEFVKNLKAE PVGKYRLAVV ELEDEELAKK VAQIATGRDK ELVLLVVGGG
     RVTVYTGGAD VGPIVKALRE VGFRGGGSRT FAQGVYSGDV KTLIDAVKRA LA