SYA_ONYPE
ID SYA_ONYPE Reviewed; 864 AA.
AC Q6YQR8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=PAM_305;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04390.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YQR8; -.
DR SMR; Q6YQR8; -.
DR STRING; 262768.PAM_305; -.
DR EnsemblBacteria; BAD04390; BAD04390; PAM_305.
DR KEGG; poy:PAM_305; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_14; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR BioCyc; OYEL262768:G1G26-364-MON; -.
DR Proteomes; UP000002523; 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..864
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075165"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 639
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 864 AA; 99723 MW; E4E05034F6ECC716 CRC64;
MTSFEIRQMW LKFFASKNHH IAKSSSLIPR NEANLLWVNA GITPLKKYFD GTQTPPFRRI
TNVQKCIRTN DIKNVGKTSR HHTFFEMLGN FSIGNYFKKE AIHYAFELLT SPKWFAFPLE
KLYITYFFQD QDTYQYWLDL GVEKNHLIPL KSNFWQIGPG PSGPCTEIFF DRGKTFDPRN
KELIIQDLEN DRFIEIWNIV FSQYNCDPKL PIEKYQELPS KNIDTGAGLE RLACILQNTK
TNFETDLFFP LIKALEKMTQ IKYTGQESFK IIADHLKTLV FAINDGAVLT NEKRGYVLKK
LLRRAANEGK KLGLDKPFLH QLVPPTAAMM KDFYKELCTN QEIIAKVLLQ QENIFEQTLK
TAEKTFLQHL TQNTLSGQNF FKLYDTYGIP EDLILDYAKK KNITTDYQKF QELLHDHQNL
SKQNQTSQIH MNKQEESFLQ FLTPSEFIGY TNFTCKTKVI KVFDKGIVLE KTPFYANMGG
QIEDEGWIDN TKVTKITKLP NGQILHEVQG NFCEGQEVYA CIEKTKRNQI SYHHTATHLL
EAVLQKQLGS HLKKQGSSVG FSSLRYDFNH FEKITPQTLL QIEKEVNQLI QKSVPVKIEQ
LSIPDAQKKY ATLLEQNQKA KYKDKVRIVS IDTFSVDLCG GTHATNTKDL EHFTILSCES
ISSGIYRIEA VCNNNCQESL NAKLVPYQND LHQLTQKAKS LQTQNLIFDV KNFPPITQSY
QDILNYQKHI KAQQQALVLF EKKVLEYHQK NMVQAESNFL PPQITKKMML TIEEEKPLEV
LKFFMNHIFD KYHLEVLFLS YVQPEKIVFL CKSKTLHAGN LIKEAVSLVC GSGGGNASLA
QGGTKKTKNL EQVLNFVKTK LEIN
