SYA_LYSSC
ID SYA_LYSSC Reviewed; 908 AA.
AC B1HUK4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
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=Bsph_3873;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACA41349.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP000817; ACA41349.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; B1HUK4; -.
DR SMR; B1HUK4; -.
DR PRIDE; B1HUK4; -.
DR EnsemblBacteria; ACA41349; ACA41349; Bsph_3873.
DR KEGG; lsp:Bsph_3873; -.
DR HOGENOM; CLU_004485_1_1_9; -.
DR Proteomes; UP000002164; 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; 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; 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..908
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347663"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 600
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"
FT BINDING 702
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 908 AA; 102334 MW; E9BC6A60929F5989 CRC64;
MGRQGLIHIV ILQYKLGGIY PMKAVDIRQM YLEFFKEKGH HHEPSAPLVP INDPSLLWIN
SGVATLKPYF DGRVIPDNPR ITNAQKSIRT NDIENVGKTA RHHTFFEMLG NFSIGDYFKK
EAIHYAWEFL TDKKWMGFDP ELLSITIHPE DQEAYDVWHQ EIGIPEERLI RLEGNFWDIG
EGPSGPNSEI FYDRGVEYGS DENDPEMYPG GENERYLEIW NLVFSQFNHN PDGTYTPLPK
QNIDTGMGLE RIVSVVQNVP TNFDTDLFMP IIEKIEEFAN RKYKRPSEVD LNEIFGSEED
INTPFKVIAD HIRTVAFAIG DGALPSNEGR GYVLRRLLRR AVRYAKQIGI EKPFMFELVP
TVGKIMEDFY PEVTEKCEFI QRVIKNEEIR FHETLDGGLA IFNEVAESQK AAGHDFIPGA
DAFRLYDTYG FPIELTEEYA EEVGMKVDHE GFETAMEEQR ERARAARQDV DSMQVQNEVL
ANLTVASEFV GFDTLVANTE IAAMIVNGQV EKVASEGQEA LVILAKTPFY AEMGGQIADS
GIISNDSFTA VVKDVQKAPN GQPLHTVIVE SGEMHVEDAV QAIVHRDDRN LIIKNHTATH
IMQRALKDVL GDHVNQAGSY VGPDRLRFDF SHFGQVTKEE LQQIERIVNE KVWDDIEVVI
EEMAIDQAKA KGAMALFGEK YGDVVRVVSI GDYSIELCGG IHVKRSSEIG FFKIVSEGGI
GAGTRRIEAV TGKVAYEVVK EEEALLNDAA ALLKANPKDI VTKVQALQGD YKELQRDNEA
LSQKIANAHS WGNCRCSTNN WRCHSSFYKS RSKDNNLLRQ MMDDLKALMP KAVIVLGAVD
GDLSDAMCRG ITIINRWQLP CWKYREIWCQ KLVVVIGGVR PDMAMAGAKD ASKLDEALLS
VYDYVKSI
