SYA_RHOJR
ID SYA_RHOJR Reviewed; 890 AA.
AC Q0S0N7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=RHA1_ro07135;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG98899.1; -; Genomic_DNA.
DR RefSeq; WP_011598855.1; NC_008268.1.
DR AlphaFoldDB; Q0S0N7; -.
DR SMR; Q0S0N7; -.
DR STRING; 101510.RHA1_ro07135; -.
DR PRIDE; Q0S0N7; -.
DR EnsemblBacteria; ABG98899; ABG98899; RHA1_ro07135.
DR KEGG; rha:RHA1_ro07135; -.
DR PATRIC; fig|101510.16.peg.7188; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_11; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000008710; 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: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_B; Ala_tRNA_synth_B; 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; IPR023033; Ala_tRNA_ligase_euk/bac.
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; 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..890
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347755"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 890 AA; 95989 MW; 13A93960BB753D66 CRC64;
MQTHEIRRRF LDHFVKAGHT EVPSASLILD DPNLLFVNAG MVQFVPFFLG QQTPPYPRAT
SVQKCVRTLD IENVGITTRH NTFFQMAGNF SFGDYFKRDA IKHAWALLTS SVDDGGYGFD
PERIWVTVYL DDDDARDIWR DEVGVPESRI QRRGMADNYW SMGIPGPCGP CSEIYYDRGP
EYGKEGGPEA DEDRYIEIWN LVFMQNERGL GISKDNFEIL GPLPKQNIDT GMGVERVAFL
LQGVDNVYET DLVRPVIAKA EELSGRKYGA VHDDDVRFRV IADHARTAAM LIADGVNPGN
DGRGYVLRRL LRRIVRSAKL LGADKPSMRE FITVVRDTMA PSYPVLDTDF GRIETVAVGE
ETAFLKTLTS GSKLFEGAAE SVKASGKSTI GGDQAFALHD TYGFPIDLTL EMAAEAGLTV
DEEGFRTLMA EQRQRAKDDA QARKHAHADL TVYKELLDRG PTEFTGFHEL VSEAHVLALI
SQGQRVPVAT AGQDVEVILD RSPLYAEAGG QIADLGTLTG PGLRVKVNDV QKIAKKLWVH
KVTVQEGQLT EGDVVLAQVD AAWRKGATQG HSGTHMVHAA LRQVLGPNAV QAGSLNKPGY
LRFDFSWQGA LTEAQKQDIE VVANEAVAAD YSVNTFVTDL DKAKSMGAMA LFGENYGDEV
RVVEIGGPFS MELCGGTHVG SSSQIGNVTL LGEQSVGSGV RRVEAYVGLD SYRYLAKERA
LLAGLSSSLK VPSEEVPARV EALVERLRVA EKELEQTRAQ AVLAAAGTFV DKAQRVGPVL
LVADSAPAGV GGNDLRGLVT DIRGRFGTQP AVVALLGDVD GKVPFVVAVN KAAQELGLAA
GDLVKGFGPK IGGRGGGKAD MAQGSGSDTS GIAAALDAVR GQVADKVGSQ
