ID A0A0G0CTU0_9BACT Unreviewed; 618 AA.
AC A0A0G0CTU0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-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 ORFNames=UR78_C0009G0003 {ECO:0000313|EMBL:KKP79721.1};
OS Candidatus Moranbacteria bacterium GW2011_GWF2_35_39.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618721 {ECO:0000313|EMBL:KKP79721.1, ECO:0000313|Proteomes:UP000034839};
RN [1] {ECO:0000313|EMBL:KKP79721.1, ECO:0000313|Proteomes:UP000034839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKP79721.1}.
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DR EMBL; LBQM01000009; KKP79721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0CTU0; -.
DR PATRIC; fig|1618721.3.peg.434; -.
DR Proteomes; UP000034839; 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 ECO:0000313|EMBL:KKP79721.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
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..618
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 372..399
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 618 AA; 70258 MW; CEE917B98297DE15 CRC64;
MTASELRTKY LEFFKEQGHQ IVPSGSLIPE NDPTTLFTGS GMQPMIPYLM GEKHPLGGRI
ADSQKSFRSG DIEEVGDNRH TTFFEMLGNW SLGDYFKKEQ IGWMFEFLTK EIGLNPEKIY
VTVFRGDESL KIPRDNESVV YWQKLFKSIK VEALAVDNAE IGGMQNGRIF FYPVEKNWWS
RAGVPNNMPL GEPGGPDSEM FWDFGAELKI HENSIWRNKP CHVNCDCGRF LEIGNNVFMQ
YIKTQAGFEI LKQQNVDFGG GLERILAATN GNPDIFLTDI FAKAKLEIEK LSGKKYEDNK
EAFQIILDHL RAATFLIADG AYPGNKDQGY FVRRLIRRAV RFAHKLEIEK NFCSDIAKIY
IKYYQDAYPD LLEKSKNIFE ELEKEENKFR KTLEKGLKEF EKTVSSEQGT VINGKAVFDL
YATYGFPLEL TEELAKENNL EIDKKGFEEE LGKHQELSRT ASAGKFKGGL ADHSEKITQL
HTATHLMLAG LRKILGENVH QKGSNITEER IRFDFSHSDK MTEEQKKVVE EYVNLAINSK
TDVVMEEMTL SEAREKGAEG AFENKYGERV KVYSIAGFSN EICGGPHVQN TGDIKGVFKI
KKEESSSAGV RRIKAVVE
//
