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SYA_THEVO
ID   SYA_THEVO               Reviewed;         876 AA.
AC   Q97AH7;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 105.
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=TV0833;
GN   ORFNames=TVG0850702;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB59975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000011; BAB59975.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_052268466.1; NC_002689.2.
DR   AlphaFoldDB; Q97AH7; -.
DR   SMR; Q97AH7; -.
DR   STRING; 273116.14325050; -.
DR   EnsemblBacteria; BAB59975; BAB59975; BAB59975.
DR   GeneID; 1441925; -.
DR   KEGG; tvo:TVG0850702; -.
DR   eggNOG; arCOG01255; Archaea.
DR   HOGENOM; CLU_004485_4_0_2; -.
DR   OMA; YHHTMFE; -.
DR   PhylomeDB; Q97AH7; -.
DR   Proteomes; UP000001017; 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 editing activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..876
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075280"
FT   BINDING         590
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         594
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         694
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         698
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   876 AA;  99775 MW;  F54597F617EEA500 CRC64;
     MEKQTGELDL KFFKNNGFEK KICRVCGSYF WTTDSRRETC GDTPCDEYTF IGNPPVPKKY
     TLSEMRKAFF DFFEKRGHKL LEPYPVVPRW REDVLLVNAS IYDFQPHVTS GIVKPPGNPI
     VMSQPSIRMN DVDLVGVTGR HLTSFEMLCH DAFNSKNDFV YWKEETVRYS YEFLTDGLGI
     DGSLITYKEK PWSGGGNAGN ALEVFVRGLE VATLVFMDMK EDQEGEVEIE GTRYTKMDMQ
     IVDTGYGLER LTWLSQGTPT VYQAIYPEII DYVLENSYVE SIDNEFLSDV VRVSVMREPY
     DEAFVLSTLG EKYPNALERF EKAKKVRDIF VLIDHARSLM HMFEAFVIPS NVKVGYLARL
     LIRRSIRAQK NIGFKGSLIN LIERNYNELK DIVKPLPIEF IKDVLSIEMQ KYSELEKRGQ
     QVIEKILKTK KSIDIDDLVL LYDSHGISPD VVAAMAAEKG LKVMIPPNFH AMVISRHEKK
     SALKKSAKVY PNIETRTLYY DDSTMREFTG LVMYSKGNEV ILDKTAFYPE GGGQPADHGY
     FEFKGKKINV LDVQKHGNAI VHKLDGEIPE GVRVKGVIDW ERRSRLMVHH TATHLLLGVL
     RDILGDHVWQ SGVQKDVSES HLDITHYKRI DEDTIKKIEH RIFELITEGR PVSVKNLDWY
     MAIGKYGFRL FEGGVPLSPK VRVVEIEGVD AEGCGGTHLK NISSIGVLKI KKIEAIQENI
     YRITFVAGVP ALELFEDSYD LAYRVSNISK KNIDQAGDFV ENTVRELSKI KRDLDSARTK
     LIEEEIRKSN SIKLGEKEIP AIEAETSDID IVSRIAHSKG IEVIIESRVG TKFRYTAISP
     SGKSKQILHD LLHTDAEGND KLSYVIVDHK ELSITR
 
 
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