SYA_ECOLI
ID SYA_ECOLI Reviewed; 876 AA.
AC P00957; P78279;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Alanine--tRNA ligase;
DE EC=6.1.1.7 {ECO:0000269|PubMed:7005211};
DE AltName: Full=Alanyl-tRNA synthetase;
DE Short=AlaRS;
GN Name=alaS; Synonyms=lovB; OrderedLocusNames=b2697, JW2667;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7005898; DOI=10.1073/pnas.77.11.6531;
RA Herlihy W.C., Royal N.J., Biemann K., Putney S.D., Schimmel P.R.;
RT "Mass spectra of partial protein hydrolysates as a multiple phase check for
RT long polypeptides deduced from DNA sequences: NH2-terminal segment of
RT alanine tRNA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:6531-6535(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-876.
RX PubMed=7025207; DOI=10.1126/science.7025207;
RA Putney S.D., Royal N.J., de Vegvar H.N., Herlihy W.C., Biemann K.,
RA Schimmel P.;
RT "Primary structure of a large aminoacyl-tRNA synthetase.";
RL Science 213:1497-1501(1981).
RN [6]
RP PROTEIN SEQUENCE OF 2-12, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=7005211; DOI=10.1016/s0021-9258(19)70119-7;
RA Putney S.D., Sauer R.T., Schimmel P.R.;
RT "Purification and properties of alanine tRNA synthetase from Escherichia
RT coli A tetramer of identical subunits.";
RL J. Biol. Chem. 256:198-204(1981).
RN [7]
RP PROTEIN SEQUENCE OF 163-173.
RX PubMed=8292605; DOI=10.1021/bi00169a019;
RA Musier-Forsyth K., Schimmel P.;
RT "Acceptor helix interactions in a class II tRNA synthetase: photoaffinity
RT cross-linking of an RNA miniduplex substrate.";
RL Biochemistry 33:773-779(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 799-876.
RC STRAIN=KP4714;
RX PubMed=8604133; DOI=10.1006/jmbi.1996.0103;
RA Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T.,
RA Sekimizu K., Miki T.;
RT "Evidence for involvement of Escherichia coli genes pmbA, csrA and a
RT previously unrecognized gene tldD, in the control of DNA gyrase by letD
RT (ccdB) of sex factor F.";
RL J. Mol. Biol. 256:483-502(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 866-876.
RC STRAIN=K12;
RX PubMed=8393005; DOI=10.1128/jb.175.15.4744-4755.1993;
RA Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.;
RT "Identification and molecular characterization of csrA, a pleiotropic gene
RT from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis,
RT cell size, and surface properties.";
RL J. Bacteriol. 175:4744-4755(1993).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=6256345; DOI=10.1016/s0021-9258(19)70120-3;
RA Putney S.D., Melendez D.L., Schimmel P.R.;
RT "Cloning, partial sequencing, and in vitro transcription of the gene for
RT alanine tRNA synthetase.";
RL J. Biol. Chem. 256:205-211(1981).
RN [11]
RP ZINC-BINDING, AND MUTAGENESIS OF CYS-179; CYS-182; GLU-184; ASP-188;
RP HIS-189; ASP-191 AND HIS-192.
RX PubMed=1712632; DOI=10.1021/bi00242a023;
RA Miller W.T., Hill K.A.W., Schimmel P.;
RT "Evidence for a 'cysteine-histidine box' metal-binding site in an
RT Escherichia coli aminoacyl-tRNA synthetase.";
RL Biochemistry 30:6970-6976(1991).
RN [12]
RP FUNCTION IN AMINOACYLATION OF TMRNA.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7524073; DOI=10.1073/pnas.91.20.9223;
RA Komine Y., Kitabatake M., Yokogawa T., Nishikawa K., Inokuchi H.;
RT "A tRNA-like structure is present in 10Sa RNA, a small stable RNA from
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9223-9227(1994).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP FUNCTION IN TRNA EDITING, AND MUTAGENESIS OF HIS-564; HIS-568; GLN-584;
RP CYS-666 AND HIS-670.
RX PubMed=12554667; DOI=10.1093/emboj/cdg065;
RA Beebe K., Ribas De Pouplana L., Schimmel P.;
RT "Elucidation of tRNA-dependent editing by a class II tRNA synthetase and
RT significance for cell viability.";
RL EMBO J. 22:668-675(2003).
RN [15]
RP FUNCTION IN TRNA EDITING, AND MUTAGENESIS OF GLN-584 AND CYS-666.
RC STRAIN=K12;
RX PubMed=18723508; DOI=10.1074/jbc.m805943200;
RA Chong Y.E., Yang X.L., Schimmel P.;
RT "Natural homolog of tRNA synthetase editing domain rescues conditional
RT lethality caused by mistranslation.";
RL J. Biol. Chem. 283:30073-30078(2008).
RN [16]
RP DOMAIN EDITING, AND MUTAGENESIS OF ARG-693.
RX PubMed=18172502; DOI=10.1038/nature06454;
RA Beebe K., Mock M., Merriman E., Schimmel P.;
RT "Distinct domains of tRNA synthetase recognize the same base pair.";
RL Nature 451:90-93(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [18]
RP FUNCTION IN TRNA-BINDING VIA C-ALA DOMAIN, AND DOMAIN EXCHANGE EXPERIMENTS.
RX PubMed=19661429; DOI=10.1126/science.1174343;
RA Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.;
RT "The C-Ala domain brings together editing and aminoacylation functions on
RT one tRNA.";
RL Science 325:744-747(2009).
RN [19]
RP FUNCTION, AND MUTAGENESIS OF THR-567; SER-587 AND CYS-666.
RX PubMed=28362257; DOI=10.7554/elife.24001;
RA Pawar K.I., Suma K., Seenivasan A., Kuncha S.K., Routh S.B.,
RA Kruparani S.P., Sankaranarayanan R.;
RT "Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a
RT cellular defense against glycine mischarging by AlaRS.";
RL Elife 6:0-0(2017).
RN [20] {ECO:0007744|PDB:3HXU, ECO:0007744|PDB:3HXV, ECO:0007744|PDB:3HXW, ECO:0007744|PDB:3HXX, ECO:0007744|PDB:3HXY, ECO:0007744|PDB:3HXZ, ECO:0007744|PDB:3HY0, ECO:0007744|PDB:3HY1}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-442 WITH AND WITHOUT CHARGED
RP CORRECT AND INCORRECT AMINO ACID, AND MUTAGENESIS OF ASP-236 AND GLY-238.
RX PubMed=20010690; DOI=10.1038/nature08612;
RA Guo M., Chong Y.E., Shapiro R., Beebe K., Yang X.L., Schimmel P.;
RT "Paradox of mistranslation of serine for alanine caused by AlaRS
RT recognition dilemma.";
RL Nature 462:808-812(2009).
CC -!- FUNCTION: Catalyzes the attachment of L-alanine to tRNA(Ala) in a two-
CC step reaction: L-alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). AlaRS also
CC incorrectly activates the sterically smaller amino acid glycine as well
CC as the sterically larger amino acid L-serine; generates 2-fold more
CC mischarged Gly than Ser (PubMed:28362257). These mischarged amino acids
CC occur because the of inherent physicochemical limitations on
CC discrimination between closely related amino acids (Ala, Gly and Ser)
CC in the charging step. {ECO:0000269|PubMed:28362257}.
CC -!- FUNCTION: Edits mischarged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not
CC incorrectly charged Ser-tRNA(Thr) (PubMed:12554667, PubMed:18723508).
CC Dtd edits Gly-tRNA(Ala) 4-fold better than does AlaRS
CC (PubMed:28362257). {ECO:0000269|PubMed:12554667,
CC ECO:0000269|PubMed:18723508, ECO:0000269|PubMed:28362257}.
CC -!- FUNCTION: Attaches Ala to transfer-messenger RNA (tmRNA, also known as
CC 10Sa RNA, the product of the ssrA gene). tmRNA plays a major role in
CC rescue of stalled ribosomes via trans-translation.
CC {ECO:0000269|PubMed:7524073}.
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:0000269|PubMed:7005211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12541;
CC Evidence={ECO:0000305|PubMed:7005211};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit; it is not clear where this binding
CC occurs. {ECO:0000269|PubMed:1712632};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7005211}.
CC -!- INTERACTION:
CC P00957; P00957: alaS; NbExp=2; IntAct=EBI-544061, EBI-544061;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
CC -!- DOMAIN: The editing domain removes incorrectly charged amino acids,
CC i.e. Ser-tRNA(Ala) or Gly-tRNA(Ala) become uncharged tRNA(Ala) and the
CC amino acid. It is specific for the acceptor stem of tRNA(Ala).
CC -!- DOMAIN: The C-terminal C-Ala domain, along with tRNA(Ala), serves as a
CC bridge to cooperatively bring together the editing and aminoacylation
CC centers thus stimulating deacylation of misacylated tRNAs. This C-Ala
CC domain can be replaced in vitro by the corresponding domain of Aquifex
CC aeolicus or man. Recognition of tRNA(Ala) by the 2 domains is
CC independent, that is one enzyme recognizes the same tRNA(Ala) in 2
CC different manners. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75739.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16559.1; -; Genomic_DNA.
DR EMBL; J01581; AAA03208.1; -; Unassigned_DNA.
DR EMBL; L07596; AAA71918.1; ALT_SEQ; Unassigned_DNA.
DR EMBL; D44453; BAA21554.1; -; Genomic_DNA.
DR EMBL; Z28405; CAA82247.1; -; Genomic_DNA.
DR PIR; E65049; SYECAT.
DR RefSeq; NP_417177.1; NC_000913.3.
DR RefSeq; WP_000047184.1; NZ_LN832404.1.
DR PDB; 3HXU; X-ray; 2.10 A; A=2-442.
DR PDB; 3HXV; X-ray; 1.93 A; A=2-442.
DR PDB; 3HXW; X-ray; 1.93 A; A=2-442.
DR PDB; 3HXX; X-ray; 2.11 A; A=2-442.
DR PDB; 3HXY; X-ray; 2.27 A; A=2-442.
DR PDB; 3HXZ; X-ray; 1.99 A; A/B/C/D=2-442.
DR PDB; 3HY0; X-ray; 1.90 A; A/B=2-442.
DR PDB; 3HY1; X-ray; 2.79 A; A/B=2-442.
DR PDBsum; 3HXU; -.
DR PDBsum; 3HXV; -.
DR PDBsum; 3HXW; -.
DR PDBsum; 3HXX; -.
DR PDBsum; 3HXY; -.
DR PDBsum; 3HXZ; -.
DR PDBsum; 3HY0; -.
DR PDBsum; 3HY1; -.
DR AlphaFoldDB; P00957; -.
DR SMR; P00957; -.
DR BioGRID; 4261283; 55.
DR BioGRID; 851507; 1.
DR DIP; DIP-9080N; -.
DR IntAct; P00957; 21.
DR STRING; 511145.b2697; -.
DR MoonProt; P00957; -.
DR iPTMnet; P00957; -.
DR SWISS-2DPAGE; P00957; -.
DR jPOST; P00957; -.
DR PaxDb; P00957; -.
DR PRIDE; P00957; -.
DR EnsemblBacteria; AAC75739; AAC75739; b2697.
DR EnsemblBacteria; BAA16559; BAA16559; BAA16559.
DR GeneID; 947175; -.
DR KEGG; ecj:JW2667; -.
DR KEGG; eco:b2697; -.
DR PATRIC; fig|1411691.4.peg.4046; -.
DR EchoBASE; EB0033; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_6; -.
DR InParanoid; P00957; -.
DR OMA; YHHTMFE; -.
DR PhylomeDB; P00957; -.
DR BioCyc; EcoCyc:ALAS-MON; -.
DR BioCyc; MetaCyc:ALAS-MON; -.
DR BRENDA; 6.1.1.7; 2026.
DR EvolutionaryTrace; P00957; -.
DR PRO; PR:P00957; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IDA:EcoCyc.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IDA:EcoCyc.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7005211"
FT CHAIN 2..876
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075113"
FT REGION 2..461
FT /note="Catalytic"
FT REGION 553..705
FT /note="Editing"
FT REGION 699..808
FT /note="Important for oligomerization"
FT REGION 766..875
FT /note="C-Ala domain"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 179
FT /note="C->S: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 182
FT /note="C->S: No inactivation."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 184
FT /note="E->Q: No inactivation."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 188
FT /note="D->N: No inactivation."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 189
FT /note="H->Q: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 191
FT /note="D->N: No inactivation."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 192
FT /note="H->Q: Inactivates the enzyme."
FT /evidence="ECO:0000269|PubMed:1712632"
FT MUTAGEN 236
FT /note="D->A,N: Decreases affinity for alanine without
FT improving discrimination against serine."
FT /evidence="ECO:0000269|PubMed:20010690"
FT MUTAGEN 238
FT /note="G->A: Greatly decreases affinity for alanine with
FT only small changes in affinity for serine and glycine, in a
FT 2-442 residue construct."
FT /evidence="ECO:0000269|PubMed:20010690"
FT MUTAGEN 564
FT /note="H->A: No effect on tRNA editing."
FT /evidence="ECO:0000269|PubMed:12554667"
FT MUTAGEN 567
FT /note="T->F: Complete loss of tRNA editing; when associated
FT with W-587 and F-666."
FT /evidence="ECO:0000269|PubMed:28362257"
FT MUTAGEN 568
FT /note="H->A: No effect on tRNA editing."
FT /evidence="ECO:0000269|PubMed:12554667"
FT MUTAGEN 584
FT /note="Q->H: Loss of mischarged tRNA editing activity; when
FT associated with A-666."
FT /evidence="ECO:0000269|PubMed:12554667,
FT ECO:0000269|PubMed:18723508"
FT MUTAGEN 587
FT /note="S->W: Complete loss of tRNA editing; when associated
FT with F-567 and F-666."
FT /evidence="ECO:0000269|PubMed:28362257"
FT MUTAGEN 666
FT /note="C->A: Loss of mischarged tRNA editing activity; when
FT associated with H-584 the effect is more pronounced."
FT /evidence="ECO:0000269|PubMed:12554667,
FT ECO:0000269|PubMed:18723508, ECO:0000269|PubMed:28362257"
FT MUTAGEN 666
FT /note="C->F: Complete loss of tRNA editing; when associated
FT with F-567 and W-587."
FT /evidence="ECO:0000269|PubMed:28362257"
FT MUTAGEN 670
FT /note="H->A: No effect on tRNA editing."
FT /evidence="ECO:0000269|PubMed:12554667"
FT MUTAGEN 693
FT /note="R->K: Reduces specificity of editing activity for
FT tRNA(Ala), allows editing of tRNA(Thr)."
FT /evidence="ECO:0000269|PubMed:18172502"
FT CONFLICT 29..33
FT /note="LVPHN -> RYPIT (in Ref. 4; no nucleotide entry and
FT 5; AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> N (in Ref. 4; no nucleotide entry and 5;
FT AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="D -> G (in Ref. 5; AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="Q -> R (in Ref. 5; AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="D -> G (in Ref. 5; AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="G -> D (in Ref. 5; AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="Q -> H (in Ref. 5; AAA03208)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="Q -> L (in Ref. 5; AAA03208)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3HY0"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3HXU"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 89..101
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3HY0"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 170..188
FT /evidence="ECO:0007829|PDB:3HY0"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 205..221
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3HY1"
FT STRAND 227..240
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 279..296
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 305..324
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 353..368
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:3HY0"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:3HY0"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:3HY0"
FT HELIX 422..440
FT /evidence="ECO:0007829|PDB:3HY0"
SQ SEQUENCE 876 AA; 96032 MW; 73F69C69FCF8C08C CRC64;
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV FLGLDKRNYS
RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKHDAIQF AWELLTSEKW
FALPKERLWV TVYESDDEAY EIWEKEVGIP RERIIRIGDN KGAPYASDNF WQMGDTGPCG
PCTEIFYDHG DHIWGGPPGS PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG
LERIAAVLQH VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM
PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK RQQAQVEQVL
KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD TYGFPVDLTA DVCRERNIKV
DEAGFEAAME EQRRRAREAS GFGADYNAMI RVDSASEFKG YDHLELNGKV TALFVDGKAV
DAINAGQEAV VVLDQTPFYA ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG
SLKVGDAVQA DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH
NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD ERVRVLSMGD
FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG EGAIATVHAD SDRLSEVAHL
LKGDSNNLAD KVRSVLERTR QLEKELQQLK EQAAAQESAN LSSKAIDVNG VKLLVSELSG
VEPKMLRTMV DDLKNQLGST IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG
GKGGGRPDMA QAGGTDAAAL PAALASVKGW VSAKLQ
