SYA_SACS2
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 03-AUG-2022, entry version 129.
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=SSO0341;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; 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=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; 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 STRING; 273057.SSO0341; -.
DR EnsemblBacteria; AAK40671; AAK40671; SSO0341.
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 OMA; YHHTMFE; -.
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: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; 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; 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
