ID A0A0L0LNG0_9BACT Unreviewed; 647 AA.
AC A0A0L0LNG0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN Name=alaS {ECO:0000313|EMBL:KND51947.1};
GN ORFNames=ABA06_01655 {ECO:0000313|EMBL:KND51947.1};
OS Parcubacteria bacterium C7867-001.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659195 {ECO:0000313|EMBL:KND51947.1, ECO:0000313|Proteomes:UP000037027};
RN [1] {ECO:0000313|EMBL:KND51947.1, ECO:0000313|Proteomes:UP000037027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-001 {ECO:0000313|EMBL:KND51947.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KND51947.1}.
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DR EMBL; LFCK01000001; KND51947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LNG0; -.
DR STRING; 1659195.ABA06_01655; -.
DR PATRIC; fig|1659195.3.peg.324; -.
DR Proteomes; UP000037027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00673; AlaRS_core; 1.
DR Gene3D; 3.30.54.20; -; 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; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KND51947.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 1..647
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 647 AA; 71763 MW; 114D74B74A77AE97 CRC64;
MTVSEVRKRY LAFMQSRGHV IIPSAPIVPG NDPTTLFTSS GMQPLVPYLL GKDHPEGKRI
ANSQMSFRAG DIEEVGDNRH TTFFEMLGNW SLGDYFKKEQ LPWFFEFLTS KEEGLGLDPN
KLYVTVFAGD PESGMSEDME AVEIWKELFK SKGVDAEFSN IGSEVQGYEK GMGANDRIFA
YDAKKNWWSR AGVPSKMPAG EPGGPDSEVF YDFGLPHDPK WGANCHPNCD CGRFVEIGNS
VFMQFVKNED GSFSNLPKQN VDFGGGLERL TFATLGTPDA FLIDVFDAAR GVLEARSGKT
YGEDDSTTKA MRIILDHMRA ASFMLAEGVL PSNTEAGYVL RRLIRRAIVQ ADRLGIKDAI
LAEVADGYAA AYVEHYPHVQ SSAAKIHAEL AKEEEQFRKT LANGMREFEK FFTATINGAL
MAKDLDSDAV FKLVTTDGFP FELVKEVAAE RGLGVNEIEF EKRMKVHQET SRAGGAQRFA
GGLADHAEQT VRYHTTHHIL LKALQMVLGD EVKQRGSNIT SERLRIDFSS PAKMTDEQKA
DVEKIVNDII YQDLPVTRTV MPRTEAEKLG AQMEFGVKYP DTVSVYSVGP IDATEADPKI
PQAFSLEFCG GPHVSNTKEI HEGGKRFRIQ KEEAVASGIR RIKGILD
//
