SYA_THET8
ID SYA_THET8 Reviewed; 882 AA.
AC P74941; Q5SH99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=TTHA1831;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9207019; DOI=10.1093/nar/25.14.2737;
RA Lechler A., Martin A., Zuleeg T., Limmer S., Kreutzer R.;
RT "A biologically active 53 kDa fragment of overproduced alanyl-tRNA
RT synthetase from Thermus thermophilus HB8 specifically interacts with tRNA
RT ala acceptor helix.";
RL Nucleic Acids Res. 25:2737-2744(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; Y08363; CAA69650.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71654.1; -; Genomic_DNA.
DR RefSeq; WP_011228945.1; NC_006461.1.
DR RefSeq; YP_145097.1; NC_006461.1.
DR AlphaFoldDB; P74941; -.
DR SMR; P74941; -.
DR STRING; 300852.55773213; -.
DR EnsemblBacteria; BAD71654; BAD71654; BAD71654.
DR GeneID; 3169868; -.
DR KEGG; ttj:TTHA1831; -.
DR PATRIC; fig|300852.9.peg.1802; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_0; -.
DR OMA; YHHTMFE; -.
DR PhylomeDB; P74941; -.
DR BRENDA; 6.1.1.7; 2305.
DR Proteomes; UP000000532; 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..882
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075234"
FT REGION 853..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT CONFLICT 179
FT /note="I -> T (in Ref. 1; CAA69650)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="G -> A (in Ref. 1; CAA69650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 882 AA; 97452 MW; C71E103DF619A648 CRC64;
MRTAEIREKF LSFFEGKGHL RLPSFSLIPE DDPSLLFTSA GMAPLKPYFL GAKPIFGGRE
WRRVTTCQEC LRVGDIENVG RTSRHNTYFE MLGNFSFGDY FKKEAILWAW EFLTEHLKLD
PGRLWVTVFE DDDEAYEIWR DLVGVPEERI GRFGEDENYW PGGAITHGPN GPSGPCSEIF
YDRGPAYGTP DETGPNTGSG DRFVEIWNLV FTQYDRQGPI PGPGILKPLP QKNIDTGMGL
YRVAAILQDV EDFYRTDTFF PIIQEVARMS GRPYEGKTSV SHRVIADHVR AVVAALSDGA
TFSNTGRGYV IRRLLRRALR HGYLLGLSDP FLHRLAPLVA ELLGDFYPEM RENLPAVEKQ
IRLEEERFLE TLEGGLKRLD ALLSGLKPGE VLPGKEAFRL YDTYGFPLDL TVEIAAERGY
GVDTEGFQKA MEEQQSRSRA AMAFEREIFK KGAQVLEELY AERGATEFLG YNALEAEAEV
LALLAGDQSL LEAGPGTEVQ VVLDKTPFYA EGGGQIGDFG LLEWPGGRAR VETTRKTERG
IFLHKARVEE GVLRVGERVR AVVDPRRRDT ERNHTATHLL HAALRAVLGP HVRQAGSLVA
PDRLRFDFTH PEPLKPEELE RVELLVNRWI MADFPVTWRY MPLEEARKEG AMALFGEKYG
EVVRVVRVEG SPLEGLESKE LCGGCHVRRT GEIGAFLIRS EEAVSAGVRR IEAVTGEEAI
RFARGSLNRL KALAERLEVG EAALEERLEK LLAELKEKER EVESLKARLV QAALGGGGGA
SLEEKGGLRW TVAELPGLDA KALRQAADDL VARGADVALV LSGGQAVLKL SPKAQGMGLE
AGALFRALAE KAGGRGGGKG ALAQGGGLDP RKAREALPGL LP
