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SYA_IGNH4
ID   SYA_IGNH4               Reviewed;         901 AA.
AC   A8A8X8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Igni_0196;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU81380.1; -; Genomic_DNA.
DR   RefSeq; WP_011998232.1; NC_009776.1.
DR   AlphaFoldDB; A8A8X8; -.
DR   SMR; A8A8X8; -.
DR   STRING; 453591.Igni_0196; -.
DR   PRIDE; A8A8X8; -.
DR   EnsemblBacteria; ABU81380; ABU81380; Igni_0196.
DR   GeneID; 5562184; -.
DR   KEGG; iho:Igni_0196; -.
DR   eggNOG; arCOG01255; Archaea.
DR   HOGENOM; CLU_004485_4_0_2; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 7896at2157; -.
DR   PhylomeDB; A8A8X8; -.
DR   Proteomes; UP000000262; 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; 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   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..901
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347881"
FT   BINDING         600
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         604
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         704
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         708
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   901 AA;  102865 MW;  6509AE2C91A903DB CRC64;
     MENEYRLRFF EEEGLKRKRC KVCGSYFWTK GEHEVCGDSP CQEYEFFDVP TKVKLSLRDA
     KREFIKFFEE KGHVPVEPRP VVARWRDDLF LTIASIVVFQ PHVTKGLVPP PANPLVIVQP
     CIRLEDIDNV GLTLGRHMTG FHMGGHHAFN YPDNWVYWKE ETVKLAYEFF TERIGIPEEL
     LNFKESWWEG GGNAGPSFEV TVAGLELATL VFMQYDVVEE NGQKKYVPMK LKVVDTGYGI
     ERIAWFTQKT PTAFHAVYGE LLHEFHKRLG VEEPPDELLY ELVRSAGLMD PERPETLERV
     YKRASEKLGM RVDEIREIHS RASLVYQVLD HTRTLMWMLA DGIVPSNVGE GYLARLVIRR
     TLRALKKLKA DVPLSELLEL QINYWKDDYP RAWKNKDYIL DVVEFEQKKF EETLKKGRNI
     VIRLIKKKKQ ITLDDLVELY DSHGIPPDIV SEIAKEMGVR VEVPHNFYSI VASRHQKTVH
     KVKGAEEKGK LPPEIIEWAK GFPPTRRLFH EDPYMKEFDA QVIGSNRNYV ILDKTAFYPE
     GGGQAADTGV IASGDESYRV VDVQKVGDVI VHVLDRDYSG GKVVVGRIDW ERRYRLMRHH
     TGTHLLLGAL RKVLGDHVWQ AGAEKTPEKA RFDFTHHKPL TREEVRKIEE VANKVIDERR
     KIRAFTLPRN EAEARYWFSI YQGGVPMSKD IRLVEIEGWD VEACFGTHLS NTGEVGSLKI
     ISTRKIQDGV VRVEFVAGTR VAEEAAKMED LIREASEKLS TNPEMLVKRI DALQKELENV
     KKTVAEYRKR LVSEYLKAAK ALDGIKYVKL DLRDPELVQE VLRALSSDSP AAVIVDGRVE
     LAAPKGVDVG KAVREVVREV GCKGGGKGNR ATVVCESEEK VVELLSKLAA KLTSQPSGRR
     G
 
 
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