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SYA_DESAP
ID   SYA_DESAP               Reviewed;         880 AA.
AC   B1I370;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, 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=Daud_0912;
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Candidatus Desulforudis.
OX   NCBI_TaxID=477974;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000860; ACA59425.1; -; Genomic_DNA.
DR   RefSeq; WP_012302011.1; NC_010424.1.
DR   AlphaFoldDB; B1I370; -.
DR   SMR; B1I370; -.
DR   STRING; 477974.Daud_0912; -.
DR   EnsemblBacteria; ACA59425; ACA59425; Daud_0912.
DR   KEGG; dau:Daud_0912; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_9; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000008544; 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; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..880
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347585"
FT   BINDING         563
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         665
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         669
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   880 AA;  97049 MW;  863F8027A3F87FDB CRC64;
     MNSSEIRKRY LEFFAARGHR VIPSASLIPG NDPTLLWTSA GMVPFKPYFT GVATPEFRRV
     VTCQKCLRTP DIEMVGRTAR HHTFFEMLGN FSFGDYFKER AIPWAWEFVT RDLGLAPEHL
     WISVYLDDNE AFDHWRGLGV PAERIVRLGR DTNFWEIGVG PCGPCSEVYY DRGPAYGCES
     ASCGPGCDCD RWLEIWNLVF IQYFRNEAGD YSPLESPGID TGMGLERVAS VLQGVNTNFD
     TDLFRGLIDY TAGVLGVRYG DDPAGDAALK VIADHGRAIT FAIADGVLPS NEGRGYVIRR
     LLRRAVRKAL LLGREKPFLE GVALAVIEQM AGAYPELETA RDSVRKVVRF EEERFRQTLT
     QGNEIIGRLI AEARAEKRST LEGAAAFQLY DTYGFPLELT REICAEQGLA VDEAGFEAAL
     KAQQQKARSS RRETRYVEER ETFFRNLRDE IGLTRFVGYE QLEADAGVRA LIRDGQRVPA
     AGSGEQVSLV VDTTPCYAES GGQVGDHGLI EGENVRGRIT DTFAPVEGLH VHEVVVEAGV
     LEEGARIRIL VDGSRRRKIC RNHTATHLLH RTLKAVLGTH VNQAGSLVAP ERLRFDFTHI
     QPLSEAELAE VESRINEIVL SNLRVESFQT SFDRARELGA VALFGEKYGD LVRVVQIDGV
     SMELCGGTHV LSTAEIGPVK ITAESSVGAG LRRLEAVTGM EALAFLNSRN EQLHRIAQAV
     RVPVSELVVH VERLLDHQKK LQRENEQLQD RLQVYEVKEL LDRASTHEGV RILATSVRAR
     DMAELRSMLD LLRERLGSAV IVLGSAVNGK VSLVASVSRD LVARGLHAGA IIKEAAAVAG
     GGGGGRPEMA QAGGKNPEKL TEALEKARQV VLRRVDGGSA
 
 
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