SYA_PYRNV
ID SYA_PYRNV Reviewed; 892 AA.
AC B1YDH4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Tneu_0900;
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001014; ACB39837.1; -; Genomic_DNA.
DR AlphaFoldDB; B1YDH4; -.
DR SMR; B1YDH4; -.
DR STRING; 444157.Tneu_0900; -.
DR EnsemblBacteria; ACB39837; ACB39837; Tneu_0900.
DR KEGG; tne:Tneu_0900; -.
DR eggNOG; arCOG01255; Archaea.
DR HOGENOM; CLU_004485_4_0_2; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000001694; 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..892
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347893"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 702
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 706
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 892 AA; 99923 MW; 18FE54A67E3CC487 CRC64;
MLSAKILQSS GFHRKQCPLC KSYFWTRRAD QIYCGDQPCV PYGFIGNPPA RASVESLADL
RERFLRFFER NSHVRIRRYP VVARWRDDVY LVGASIYDFQ PWVTSGAVPP PANPLAISQP
SIRLTDVDKV GRSGRHLTGF EMMAHHAFNY PDKYVYWIDE TTQYAYEFFT RELGIPPDEI
TFKESMWEGG GNAGECFEVL IRGLEVATLV FMHYEVKDGR YVELPLKIVD TGYGLERIYW
LLKGTPTVYD AVFGPYLAKA RQRLGVPEPP AEVMGKASVY FGQMDPEVIG LEKAYDIIAE
KIGVDPKWLR EVVRPQEALY VLADHSRTVS WMIADGVIPS NTGAGYLARL LIRRILKNLR
LAGVDAPLVE LFDMHLAELK REYPEVWEAR GLILELVDME ERRYREVLKS APAAVKKALE
EARRRGRAGL DADDLVALYD SQGIPPEVAA EVAKSLGTEV KVPDDFYAKL AARHVKREKK
PESSPVEMGK VADLPRTREL FYEDSYMRSF KARVLRVIDG RYVVLDQTAF YPEGGGQPAD
RGVLKFQGGE AKVVDVQRVG HVVVHVVEGQ PPPEGAEVVG EVDWERRYSL MKMHTGTHVL
IQSIRRVLGS HIWQAGAQKD IPSSRIDVTH HRLPTAEEVA RIEELANRAV QADLPVYAKI
MPRNEAEAKY GFVLYQGGVV PAREIRVLQI GPDEQPYDVQ ACGGTHLRST GEIGLIKIQK
VERIADGVVR FVFTTGMHAL AYVQELERRA AEAASIAGGS RDELVEAVRR LAQRAEEADR
RARRYAELYA AALAENLKAE QVGRHRLAVV ELDDEELARK IALAATSRDR DLVLVFVGGG
RATVYTGGVD VAPIVKALRE VGFRGGGSKT FAQGQYKGDI QTLKEAIRRA LA
