ID   SYA_LACP3               Reviewed;         881 AA.
AC   Q03B02;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
GN   Name=alaS; OrderedLocusNames=LSEI_0784;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000423; ABJ69620.1; -; Genomic_DNA.
DR   RefSeq; WP_003587396.1; NC_008526.1.
DR   RefSeq; YP_806062.1; NC_008526.1.
DR   AlphaFoldDB; Q03B02; -.
DR   SMR; Q03B02; -.
DR   STRING; 321967.LSEI_0784; -.
DR   EnsemblBacteria; ABJ69620; ABJ69620; LSEI_0784.
DR   KEGG; lca:LSEI_0784; -.
DR   PATRIC; fig|321967.11.peg.786; -.
DR   HOGENOM; CLU_004485_1_1_9; -.
DR   OMA; YHHTMFE; -.
DR   Proteomes; UP000001651; 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: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; IPR006195; aa-tRNA-synth_II.
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;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding.
FT   CHAIN           1..881
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347644"
SQ   SEQUENCE   881 AA;  97253 MW;  B490D0CFD51AE52C CRC64;
     MKKMSSGEIR QMFLDFFKSK GHAVEPSASL IPVDDPTLLW INSGVATLKK YFDGSVVPDN
     PRITNAQKSI RTNDIENVGK TARHLTFFEM LGNFSVGDYF KKEVIPWAWE LLTSPKWFGF
     DPKRLYVTVY PKDKVTKELW QKTGVPDDHI VEAEDNFWDI GEGPSGPDSE IFYDRGQQFN
     NVAEDDPENY PGGENSRYVE IWNIVFSELN HLPDGRFVEQ PHKNIDTGMG LERLVAVIQG
     TPTIFETDLF MPIIKATEKM SAGKRYGVSA QDDVSFKIIA DHARTVTFAI GDGALPSNEG
     RGYVLRRLIR RAVLNGKKLG IDHDFLYQLV PVVGEIMKSY YPQILANQQF IQKVIESEEA
     RFRQTLDAGV TLLNQIIADL KQDGKKEIPG ADAFKLFDTY GFPVEMTNEY AQDEGLQVDM
     AGFKKNMAAQ RDRARKARGD RQSMGSQDKV LMSITTPSKF TGWTELDHKH ASLQTIVVND
     QLQDSVSEGT AQLIFDETPF YAEMGGQVAD HGEIKAQDGT VLADVSDVQH APNGQNLHTV
     TVKGKLETGQ QYWLSVDPLR RKKVSLNHTA THLLDQALRD VLGEHTHQAG SLVEPDYLRF
     DFTNFGQVTP KQLRQVETIV NQKIWDALPI TWKEMPIEEA KKLGAIAMFG DKYGSVVRIV
     KIGDYNTEFD GGTHPTNSNA LGLFKITSES GIGAGIRRVE AVTSKEAYEY LTQQQDWLSE
     TAENLKIDQV KNVPSKVTQL QADLKAEQKT VAGLQAKLAA QAAAGIFDHP EEVGGLKLIA
     KQVQVAGMNE LRQLADKWKA KQASDILVLG TEVSGKANLL VAVNDTANQA GFKAGDLIKA
     IAPKVGGGGG GRPDMAQAGG KNPAGIPAAL SEAKTVISQK A