SYA_SULAC
ID SYA_SULAC Reviewed; 907 AA.
AC P35029; Q4J8V2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=Saci_1455;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-182.
RX PubMed=7966335; DOI=10.1006/jmbi.1994.1723;
RA Ramirez C., Shimmin L.C., Leggatt P., Matheson A.T.;
RT "Structure and transcription of the L11-L1-L10-L12 ribosomal protein gene
RT operon from the extreme thermophilic archaeon Sulfolobus acidocaldarius.";
RL J. Mol. Biol. 244:242-249(1994).
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; CP000077; AAY80776.1; -; Genomic_DNA.
DR EMBL; X59038; CAA41766.1; -; Genomic_DNA.
DR PIR; S53652; S53652.
DR RefSeq; WP_011278278.1; NC_007181.1.
DR AlphaFoldDB; P35029; -.
DR SMR; P35029; -.
DR STRING; 330779.Saci_1455; -.
DR PRIDE; P35029; -.
DR EnsemblBacteria; AAY80776; AAY80776; Saci_1455.
DR GeneID; 3473494; -.
DR KEGG; sai:Saci_1455; -.
DR PATRIC; fig|330779.12.peg.1399; -.
DR eggNOG; arCOG01255; Archaea.
DR HOGENOM; CLU_004485_4_0_2; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000001018; 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; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..907
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075276"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 907 AA; 103899 MW; 86807784D2351F3E CRC64;
MVKANENEYR LNFFLSRGYE RKICRSCSTP FWTLDKSKEN CSDVPCTDYY FFDIKIKSPP
LTVRESREKF LRFFEKRGHT IVPPKPVVAK WRDDLYLTIA SIVDFQPFVT SGLAKPPANP
LVVSQPCIRL EDVDNVGITF GRHLTTFEMA AHHAFNYPDK QIYWKDETVA FAKEFFTEEL
GIPEDQLNFK ESWWEGGGNA GPCFEVTVGG LELATLVFMQ YEIRGQDYVP LKLKIVDTGY
GVERIAWFTQ RTPTAFHAIY GNLVSSFYKK IGVGEVNNEL LKAAAIYAGR IDPDIKETIT
AHREHLAKQL GLDLKYVNEE LTRAARVFQV LDHTKTIALM LADGLVPSNS GEGYLGRLLI
RRALRVLRLL GSDVKLHELI KDQIDYWKED FPQMLKNKDY IVDAVINEEE KYNDTISKIP
SILSTLSKKS KVDLDELINI YDSNGISPDL ILDEARKRNI NINVEIPHNF YSIVAKKHQN
ALVRENRKDK IPKEVIDEIN NKKIEPTVPL YYKDQYLRTF NAKVLLNYKN FLVLDQTTFY
PEGGGQIGDT GIIRSIEGNK QAKVIDTQKY KGVIVHILDK DSPFIQGEQV YGEIDWQRRY
RIMKHHTVTH VILSATRRVL GEHAWQAGAE KTEYKGRLDV THYKLPTEEE IRKIEDFANY
IINDRRKVRP LYIERTEAEM KYGVSIYAGG IPEGSEIRLI EIENWDIEGC GGTHLINTGE
IGGVKIVNVE KLQDGVIRLE YVAGDMVSNY ARQQDEKLNE ISKLLNSPVS QINVRLKKHL
EEYENLQNLL DKYRKIVLDR IQEIAERISV NGITIYILRD FIDEQLIKEV MRKITSNNQN
IVISIRGKDT KNVEIATSKD IKVDKIVDEL RKIGGRGGGK GTYGSVSITV EEEKIIDTIR
SAITNGV
