SYA_RICAH
ID SYA_RICAH Reviewed; 878 AA.
AC A8GQ73;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=A1C_06625;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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; CP000847; ABV75548.1; -; Genomic_DNA.
DR RefSeq; WP_012150177.1; NC_009881.1.
DR AlphaFoldDB; A8GQ73; -.
DR SMR; A8GQ73; -.
DR STRING; 293614.A1C_06625; -.
DR EnsemblBacteria; ABV75548; ABV75548; A1C_06625.
DR KEGG; rak:A1C_06625; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_5; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000006830; 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; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..878
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347762"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 878 AA; 99191 MW; 57E859144B41DBC7 CRC64;
MTKFTTEEVR SKFITYFKTN NHTHVPASSL IPHNDPSLMF VNSGMVQFKN VFTGQTKRPY
HTAVTSQKSV RAGGKHNDLE NVGYTARHHT FFEMLGNFSF GDYFKEQAIY YAWNLLTKEF
ELPKDKLYAT IYHTDDEAAS CWKKIAGFGD DRIIKIKTND NFWSMGDTGP CGPCSEIFYD
HGEQIYGGLP GTKYEDGDRF IEIWNMVFMQ YEQIDKDTRI ELPQKSIDTG MGLERMTAVL
QHVSNNYDID LFQEIINFTE NIVKVKIEGE AKFSYRVIAD HLRASSFLIA DGVIPSNEGR
GYVLRRIMRR AMRHAHMLGS QEPLMYKLLP KLVDLMGSVY PELKRAESFI SRILEQEEIR
FKTTLERGLK LLTEETETLK KGNELSGEIA FKLYDTYGFP LDLTEDILKN RDISIDHKGF
EEQMLAQKER ARKAWLGSGE SKTDQLWFDI KEQHGSTEFL GYTLNEAECK IIALIKDNNL
VNDIKKIDTQ FLLISNQTPF YGESGGQMGD IGTIFAKDSD IEVIDTLKYL GSIIAHKCIL
KKGQINVGDS ANFSIDIKYR QNLRIHHSAT HILHAVLHEV LGQHVTQKGS LVAPTYLRFD
ISHSKAVTHE EITSIEDKVN EIIRDNHEVN TTLMTTEDAV KQGVMALFGE KYDSEVRVVK
MGETSLELCG GTHVRRTGDI GSFKITSESA IAAGVRRIEA VCGEFVIKLI REKDSLLKSI
ENSLKTNKNE LVTKVNNTLE RNKELEKELE KTHLARLDLS IEQIEKQAED IKGVKLIYRH
IENLDNKVLR QAAANLTNKV EDLIVVYITG NNDKLSITVA VSKAITDKYN ACIIAKELSL
FLGGSGGGGQ ASLAQAGGSD IGKLTNIHEK LYSFITAS
