ID SYA_SACS2 Reviewed; 900 AA. AC P96041; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 02-SEP-2026, entry version 143. 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}; GN OrderedLocusNames=SSO0341; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174. RX PubMed=9252104; DOI=10.1016/s0167-4838(97)00073-3; RA Geiger M., Groebner P., Piendl W.; RT "Nucleotide sequence of a gene cluster encoding NusG and the L11-L1-L10-L12 RT ribosomal proteins from the thermophilic archaeon Sulfolobus RT solfataricus."; RL Biochim. Biophys. Acta 1340:170-177(1997). 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=tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + CC diphosphate; 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; Evidence={ECO:0000255|HAMAP- CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE006641; AAK40671.1; -; Genomic_DNA. DR EMBL; U85262; AAB99528.1; -; Genomic_DNA. DR PIR; H90176; H90176. DR RefSeq; WP_009990629.1; NC_002754.1. DR AlphaFoldDB; P96041; -. DR SMR; P96041; -. DR FunCoup; P96041; 221. DR STRING; 273057.SSO0341; -. DR PaxDb; 273057-SSO0341; -. DR EnsemblBacteria; AAK40671; AAK40671; SSO0341. DR GeneID; 1455481; -. DR GeneID; 44129312; -. DR KEGG; sso:SSO0341; -. DR PATRIC; fig|273057.12.peg.332; -. DR eggNOG; arCOG01255; Archaea. DR HOGENOM; CLU_004485_4_0_2; -. DR InParanoid; P96041; -. DR PhylomeDB; P96041; -. DR Proteomes; UP000001974; 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:0002161; F:aminoacyl-tRNA deacylase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central. DR CDD; cd00673; AlaRS_core; 1. DR FunFam; 2.40.30.130:FF:000010; Alanine--tRNA ligase; 1. DR FunFam; 3.30.54.20:FF:000004; Alanine--tRNA ligase; 1. DR FunFam; 3.30.930.10:FF:000056; Alanine--tRNA ligase; 1. DR FunFam; 3.30.980.10:FF:000004; Alanine--tRNA ligase, cytoplasmic; 1. DR Gene3D; 2.40.30.130; -; 1. DR Gene3D; 3.30.54.20; -; 1. DR Gene3D; 6.10.250.550; -; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 3.30.980.10; Threonyl-trna Synthetase, Chain A, domain 2; 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 NCBIfam; TIGR03683; A-tRNA_syn_arch; 1. DR NCBIfam; TIGR00344; alaS; 1. DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1. DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1. DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1. DR SUPFAM; SSF50447; Translation proteins; 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..900 FT /note="Alanine--tRNA ligase" FT /id="PRO_0000075277" 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; 102980 MW; 6CB15A31210E153F CRC64; MKASEEEYKL NFFIKNDFKR KICKSCQTPF WTKDDKKEYC SDIPCTDYYF FDINIKSQPL TVKEAREKFL SFFEKRGHTR IPPKPVLARW REDLYLTIAS IVDFQPHVTS GLVPPPANPL VVSQPSIRLE DIDNVGVTFG RHLTTFEMAA HHAFNYPDRY VYWKDETTAY ATEFFTKELG IPEEELNFKE SWWEGGGNAG PCLEVTVGGL ELATLVFMQY KITDNGDYIP LKLKIVDTGY GVERIAWVTQ KTPSAFHAIY GNLVYKFFDK IGVAYIDETL LKVASRFAGK IDPDNPDTIK IHRQMVSKEL GIDIKNVEEE LDRAAKVFQI LDHTKTIMLM LADGLVPSNS GEGYLGRLVI RRALKVLRLL KSDVRLYELV KEQIGFWKED FPQVLKNKDY ILDAVELEQQ RFEKILEKVP SIASTLARKS EITTEDLIQV YDSNGVPPDL LEEELKKKRV KFELPRNFYA LVAKRHQTST IKNVYDKVKL PKDLLEYITT LQPTEKLYYK DQYMRSFEGK VLGIYKNYLI LDKTTFYPEG GGQLGDTGLI IDEKSSKRYE VVDTQKVNDV IIHVLKEEPS TIKVGDNVRG EINWERRYRL MRHHTVTHVI LAAAKKVLGD HIWQAGAEKT PEKGRLDITH HKALTEEEVK LIENYANSVI SDRRPVKPLE MNRMEAEMKY GVSIYEGGVP NSATIRLLEI KDWDIESCGG THVSNTSEIG AVKIINVERI QDGIIRLEYV AGPALVDYIR ETEAKIAEAS KIIGTSPDQL PSRLRRILNE VEKKNNLIIQ YRRIVETELL NSLKPYEING NKIYIIEGLN DEEENKEILR KLTSTDNTIA ISISDNRLQI ATSKNMRVDK IVEELLKGGG KGGGKGTFAN VILSSKKSKE EIIDIVRKSL //