ID A0A0G1ZJC9_9BACT Unreviewed; 655 AA.
AC A0A0G1ZJC9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=UY63_C0013G0030 {ECO:0000313|EMBL:KKW19459.1};
OS Parcubacteria group bacterium GW2011_GWA2_51_10.
OC Bacteria.
OX NCBI_TaxID=1618855 {ECO:0000313|EMBL:KKW19459.1, ECO:0000313|Proteomes:UP000034456};
RN [1] {ECO:0000313|EMBL:KKW19459.1, ECO:0000313|Proteomes:UP000034456}
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:KKW19459.1}.
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DR EMBL; LCQS01000013; KKW19459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1ZJC9; -.
DR STRING; 1618855.UY63_C0013G0030; -.
DR PATRIC; fig|1618855.3.peg.562; -.
DR Proteomes; UP000034456; 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:KKW19459.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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..655
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 655 AA; 73560 MW; 2A2846D391F0EC0D CRC64;
MTANEIRAAF LDFFQRRDHI VIPSASLVPE NDPTTLFTGS GMQPLVPYLL GKDHPAGNRL
ANSQKCFRAM DIDEVGDNRH TTFFEMLGNW SLGNYFKKEQ LSYFFEFLVD VIHLDPRRLY
VTVFIGDEKT GIPKDDESAA IWKELFSQRG IAAKEVSLGS GEEGSRTGMQ DGRIFYYGAE
KNWWSRAGTP DQMPAGEPGG PDSEVFYDFG TAHDIRFGTY CHPNCDCGRF LEIGNSVFMQ
YMKSSDGSFA LLPKLNVDFG GGLERITAAA GGNPDIFRID LFADIIALLQ HYADEKQYDD
PKHTKSFRII ADHIRAAVFM IADGVRPSNT DRGYMLRRLL RRAAHHAIAL GAAQGQEENN
ELVRCAMLVV EKYKEAYPEL DGENVYKKIW ETIWEEEKQF ARALDMGKRA FDKIVSAEGA
LSGKSATMLV TTYGLPLETA IDLARERGID VDEREITETH KRLMDEHREV SRAGVTQKFK
GGLADSSEKT TRLHTAHHLL LAALQLILGR AVKQRGSNIT QDRLRIDFSF ERKVSDEELK
EVERIVNEKI HEELPVIRTL MSKSEAEKLG AQQEFGAKYP DQVSVYSIGP ETATDDDPKF
EKAFSLEFCG GPHVNNTREL ASIIHPDGPD RKGSFKIVKE EAVASGIRRI KAVLL
//