SYA_THEKO
ID SYA_THEKO Reviewed; 917 AA.
AC Q5JIL7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=TK1567;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85756.1; -; Genomic_DNA.
DR RefSeq; WP_011250518.1; NC_006624.1.
DR AlphaFoldDB; Q5JIL7; -.
DR SMR; Q5JIL7; -.
DR STRING; 69014.TK1567; -.
DR PRIDE; Q5JIL7; -.
DR EnsemblBacteria; BAD85756; BAD85756; TK1567.
DR GeneID; 3235147; -.
DR KEGG; tko:TK1567; -.
DR PATRIC; fig|69014.16.peg.1527; -.
DR eggNOG; arCOG01255; Archaea.
DR HOGENOM; CLU_004485_4_0_2; -.
DR InParanoid; Q5JIL7; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 7896at2157; -.
DR PhylomeDB; Q5JIL7; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_A; Ala_tRNA_synth_A; 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; IPR022429; Ala-tRNA_lgiase_arc.
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; TIGR03683; A-tRNA_syn_arch; 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..917
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075275"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 917 AA; 104882 MW; DC7869EBC54F5AA1 CRC64;
MSMDMTTRMF KEEGWIRKKC PKCGKYFWTL DPDRETCGDP PCDEYQFIGK PGIPKKYTLD
EMREKFLSFF EKHESYPHGR VKRYPVLPRW RDDVLLVGAS IMDFQPWVIS GEADPPANPL
TISQPSIRFT DIDNVGITGR HFTIFEMMAH HAFNYPGKPI YWMDETVELA FEFFTKELKM
KPEDITFKEN PWAGGGNAGP AFEVLYRGLE VATLVFMQYK KAPADADPSQ VVEIKGDYYV
PMETRVVDTG YGLERLVWMS HGTPTAYDAV LGYVIEPLKK MAGVEKIDER ILMENSRLAG
MFDIEDMGDL RYLREQVAKR VGISVEELEK AVRPYELIYA IADHTKALTF MLADGVIPSN
VKAGYLARLL IRKSIRHLRE LGLEIPLAEI VAMHIKELSP TFPEFKEMED VILDIINVEE
KRYAETLRRG SDLVKREIAK LKKKGINELP LEKLILFYES HGLTPEIVAE VAEKEGIKVN
IPDNFYTLVA KEAEKQAEKK EAAEYVVDFE LVKDLPDTRT LYYEDPFMKE FDARVLKVIA
DWVVLDQTAF YPEGGGQPYD TGVLEVNGEK VKVTNVQKVG KVILHKVEKP ELFKEGVTVH
GRLDWDRRIQ HMRHHTGTHV LMGALVRVLG KHVWQAGSQL HTDWARLDIS HYKRITEEEL
REIERLANRV VMENRKVTWE WLPRTEAEMK YGFRLYQGGV VPGRVIRVLK IEDWDVQACG
GTHLPNTGLI GPIKILRTER IQDGVERIIF AAGEAAINWM QETERLLKRT AEIFRVPPEK
VPETAERFFN EWKEARKEVE KLRKELAKLL VYELQEKVEK VGNVEFIGAV VEGTIDDLRE
AANRLRKENR VVVLISREGH FVVAVGDGLD LKAGELAKVI TSVAGGGGGG RKELAQGRIK
NPLKAEEAIE EVKKMLG
