SYA_SULIY
ID SYA_SULIY Reviewed; 900 AA.
AC C3N7E3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=YG5714_1881;
OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=439386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.G.57.14 / Yellowstone #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001403; ACP46137.1; -; Genomic_DNA.
DR RefSeq; WP_012716389.1; NC_012622.1.
DR AlphaFoldDB; C3N7E3; -.
DR SMR; C3N7E3; -.
DR PRIDE; C3N7E3; -.
DR EnsemblBacteria; ACP46137; ACP46137; YG5714_1881.
DR GeneID; 7807284; -.
DR KEGG; siy:YG5714_1881; -.
DR HOGENOM; CLU_004485_4_0_2; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000002308; 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:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
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_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; 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; 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; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..900
FT /note="Alanine--tRNA ligase"
FT /id="PRO_1000202051"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 712
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 900 AA; 103090 MW; AE89FEAD497CB69C CRC64;
MKASEEEYRL NFFIKNDFKR KICKSCKTPF WTRDEKKEYC SDIPCTDYYF FDINIKSQPL
TVKEAREKFL SFFEKRGHTR ISPKPVLARW REDLYLTIAS IVDFQPHVTS GLVPPPANPL
VVSQPSIRLE DIDNVGITFG RHLTTFEMAA HHAFNYPDHY VYWKEETTAY ATEFFTKELG
IPEEELNFKE SWWEGGGNAG PCLEVTVGGL ELATLVFMQY KITDNGNYTP LKLKIVDTGY
GVERIAWITQ KTPSAFHAIY GNLVYKFFNK IGVAYIDETL LKVASRFAGK IDPDNPDTIK
IHRQMVSKEL GIDIKAVEEE LDRAAKVFQI LDHTKTIMLM LADGLVPSNS GEGYLGRLVI
RRALKVLRLL KSDVRLYELV KEQIDFWKED FPQVLKNKDY ILDAVELEQQ RFEKILEKVP
SIASTLARKS EITTEDLIQV YDSNGIPPDL LEEELKKKSV KFELPRNFYA LVAKRHQTST
IKSAYDKVKL PKDMLEYITA LQPTEKLYYK DQYMRSFEGK VLGVYKNYLI LDKTTFYPEG
GGQLGDTGLI IDEKSSKRYE VIDTQKVNDV IVHILKEEPS TIKVGDNVRG EINWERRYRL
MRHHTVTHVI LAAAKKVLGE HVWQAGAEKT PEKGRLDITH HKTLTEEEVK LIENYANSVI
SDRRQVKPLE MNRMEAEMKY GVSIYEGGVP NSATIRLLEI KDWDIESCGG THVSNTSEIG
AVKIINVERI QDGVIRLEYV AGPALVDYIR ETQAKIVEAS KIIGTSPDQL TSRLRRILNE
IEEKNNLIIQ YRRIIETELL NNLKPYEINS NKIYIIEGLG DEEENKEILR KLTSTDNTIA
ISISDNRLQI ATSKNMRVDK IVEELLKGGG KGGGKGTFAN VILNSKKSKE EIIEIVRKSL
