SYA_METJA
ID SYA_METJA Reviewed; 892 AA.
AC Q57984;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=MJ0564;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION IN EDITING ACTIVITY ON MISCHARGED TRNA(ALA).
RX PubMed=14663147; DOI=10.1073/pnas.2136934100;
RA Ahel I., Korencic D., Ibba M., Soll D.;
RT "Trans-editing of mischarged tRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003).
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) (By similarity). Also
CC functions in trans to edit the amino acid moiety from incorrectly
CC charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala). {ECO:0000250,
CC ECO:0000269|PubMed:14663147}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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; L77117; AAB98556.1; -; Genomic_DNA.
DR PIR; D64370; D64370.
DR RefSeq; WP_010870068.1; NC_000909.1.
DR AlphaFoldDB; Q57984; -.
DR SMR; Q57984; -.
DR STRING; 243232.MJ_0564; -.
DR PRIDE; Q57984; -.
DR DNASU; 1451429; -.
DR EnsemblBacteria; AAB98556; AAB98556; MJ_0564.
DR GeneID; 1451429; -.
DR KEGG; mja:MJ_0564; -.
DR eggNOG; arCOG01255; Archaea.
DR HOGENOM; CLU_004485_4_0_2; -.
DR InParanoid; Q57984; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 7896at2157; -.
DR PhylomeDB; Q57984; -.
DR Proteomes; UP000000805; 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; IDA:UniProtKB.
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 1: Evidence at protein level;
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..892
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075264"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 892 AA; 102851 MW; 409A542E72C8188B CRC64;
MKHNYKVKLF DELGFVRKKC KKCGQWFWTL DEERETCGDA PCDIYSFIGK PITKKPYTYK
EMVKEFINFF KEHGHEPIKR APVTARRWRD DILLTIASIA VFQPWITKGI VKPKANPLVI
AQPCIRLNDI DNVGRTGRHL TCFTMGGHHA FNREDDFKYW QDETVELCFN FFKKLGIDEK
SITFIESWWE GGGNAGPCYE VITHGVELAT LVFMQYEKVG DNYKEIPLKI VDTGYGIERF
VWASTGEPTI YDAIFKNIVN KLKEDAGVKD IDKEILAKIT EVAGLMDVKD VGDLRKLREE
VANKVNIPVE ELDKLISPYE DIYAIVDHTR ALAFMLGDGI VPSNVKDGYL VRMLIRKTLR
HMDRLNLSTP ITEIVAMQLN ELKDLYPELL DMEDYIMEIL EIETNKYRQT IERGKGIVER
LLKSKKEIDL ENLIELYDSH GLPPEIVKDV AKSLGKDVKI PDNFYTIVAE RHENKKEVKE
KIKLPEVNVD KTELLFYEYP KMKEFEAKIL RIVDDYVILD RTAFYPEGGG QKADTGYIIK
GDKKFRVVDV QKENNIVYHK IENLNDELKE GDIVKGVIDW KRRLSLMRNH TATHIINAAA
QKVLGRHVWQ AGSDVDVDKA RLDITHYKRI SREELKDIER VANEIVLNNY NIKSIFMDRN
EAEEKFGFRI YQGGVVPGNV LRIVIIEDEN GNIVDVQACG GTHCQNTGEV GFIKIIKTER
VQDGVERLIY SSGLSALKAV QEMEDILEES AEILRCPTEE LPKVIKRFFE EWKEQRKKIE
ELEKKIGELK KFELINKFET IGNYKVLVEK VEANPKEMLN IADNLATENA IVVLLNDKGN
ILCKRGENVD IKMNELIRYI AKGGGREHLA QGKYEGDVEE IKKKVIEFIK NK
