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SYA_FRATN
ID   SYA_FRATN               Reviewed;         865 AA.
AC   A0Q604;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=FTN_0778;
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA   Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA   Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA   Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA   Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA   Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary events
RT   associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(2007).
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; CP000439; ABK89669.1; -; Genomic_DNA.
DR   RefSeq; WP_003038961.1; NZ_CP009633.1.
DR   AlphaFoldDB; A0Q604; -.
DR   SMR; A0Q604; -.
DR   EnsemblBacteria; ABK89669; ABK89669; FTN_0778.
DR   KEGG; ftn:FTN_0778; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   BioCyc; FTUL401614:G1G75-811-MON; -.
DR   Proteomes; UP000000762; 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: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_B; Ala_tRNA_synth_B; 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; IPR023033; Ala_tRNA_ligase_euk/bac.
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; 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..865
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347614"
FT   BINDING         554
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         558
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         656
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         660
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   865 AA;  96042 MW;  7618493349077BEE CRC64;
     MITTKELRNK FINYFESKNH SHQPSSSLIP FGDDTLLFTN AGMVQFKDVF LGIEKKDFSR
     AVTVQKCLRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKKDAISFA WEFLTKEIKL
     PIEKLWVTIY ASDDEAFDVW HKHIGLAKER IIRIDSSDNF WSMGDTGPCG PCTEIFYDHG
     EDVAGGLPGT PEQDGDRYIE IWNIVFMQYN RHADGSTTDL PKPSVDTGMG LERISAVLQN
     VHSNYEIDLF QALIKKAQQV THAKDINSPS LKVIADHIRA CAFLIADGVL PANEGRGYVL
     RRIIRRAIRH GNKVGAKEIF FYKLVAELVN QMGEAYSQLI DKRELIEKTL IKEEELFLKT
     IENGIKIFDA EIENLKDNTI SGEVAFKLYD TYGFPFDLTA DMAREKGLKV DEQAFLAQMQ
     IQKQRSKEAG KFNVDYNSLI NSQVKSEFRG YSTLIEDAKV LEIYQDGQLV ASTSEQVPAV
     VVLDKTPFYA ESGGQVGDKG ILEGVGFEFV VEDVQKSGEA ILHIGKLVKG RLNLNDELTA
     RVSDQPRLAT AANHSATHLL HKALKLVLGG HAEQKGSLVD ENRLRFDFTH DKAISRSEIE
     QIELLVNQQI RANYPVTTIE TSQQKAKSLG AEALFGEKYG DIVRVISMGD FSIELCGGTH
     VAYTGDIGLF KIISEGGIAS GVRRIEAVTA DKAIRHTFTN ENKIIAIKDS LKANDANLID
     KIKSMLEQIK NQEKQIAKLK KELLSGSSND IKETNIGDIK VVVANVDGVD VKTLRDKIDD
     YKSKNTKVIA VLTTTNADKV QFVIGVSNAI TTLIKAGDIA KELSSHIDGK GGGRADMAQG
     GGNNSANIDQ ALSQVEKFIL NNIKE
 
 
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