ID   E3PTE1_ACESD            Unreviewed;       402 AA.
AC   E3PTE1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Alanyl-tRNA synthetase related protein {ECO:0000313|EMBL:CBH22145.1};
GN   OrderedLocusNames=CLOST_2025 {ECO:0000313|EMBL:CBH22145.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH22145.1, ECO:0000313|Proteomes:UP000007041};
RN   [1] {ECO:0000313|Proteomes:UP000007041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC   {ECO:0000313|Proteomes:UP000007041};
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; FP565809; CBH22145.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PTE1; -.
DR   STRING; 1511.CLOST_2025; -.
DR   KEGG; cst:CLOST_2025; -.
DR   eggNOG; COG2872; Bacteria.
DR   HOGENOM; CLU_004485_7_2_9; -.
DR   BioCyc; CSTI499177:GJE9-2089-MONOMER; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.30.130; -; 1.
DR   Gene3D; 3.10.310.40; -; 1.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR   PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CBH22145.1};
KW   Ligase {ECO:0000313|EMBL:CBH22145.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007041}.
FT   DOMAIN          1..252
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
SQ   SEQUENCE   402 AA;  45538 MW;  D457007ABB93AABB CRC64;
     MNNELNDFFE VDIATLNPTN KLYYFNPYMI EASSNIVAIL KDKEFYKIVL DETIFYPEGG
     GQPSDRGEIE EIPVFDVKEK DGIVYHYVNE LPKNSKVKSK IDFNRRFDFM QQHSGEHALS
     GVILKLFGGA NKGFHIGEQF VTIDINIKDM TEEMLIEAEN ETNRYIFENQ KVDQIVTDTE
     GLKAYPIRKE ITAEEDIRVV SMGEADCCAC CGTHVRNLGE VGIIKIIKAE SYKGMTRISF
     LCGYRALNDY KEKNDIIKSL KKELSSEESM ILTKVQKQRE DISALKKQSD IIRKDLAKNI
     SLNIKADETI AIIFDDVDFL TLVHIESILL EKSNTVILAT TVDNKITAVT KNDAINLGQF
     FKENIKSYNG KGGGSKDKAQ GSFETKEEII AFYTSLMSKI VN
//