ID A0A0G0U4I6_9BACT Unreviewed; 633 AA.
AC A0A0G0U4I6;
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=UT91_C0017G0009 {ECO:0000313|EMBL:KKR54375.1};
OS Parcubacteria group bacterium GW2011_GWA2_40_23.
OC Bacteria.
OX NCBI_TaxID=1618816 {ECO:0000313|EMBL:KKR54375.1, ECO:0000313|Proteomes:UP000034534};
RN [1] {ECO:0000313|EMBL:KKR54375.1, ECO:0000313|Proteomes:UP000034534}
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:KKR54375.1}.
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DR EMBL; LBYP01000017; KKR54375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0U4I6; -.
DR STRING; 1618816.UT91_C0017G0009; -.
DR PATRIC; fig|1618816.3.peg.974; -.
DR Proteomes; UP000034534; 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:KKR54375.1}; 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..633
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 633 AA; 72249 MW; 38A7349CA6DCDA3A CRC64;
MKTSELRQLY LNFFAEKQHA VIPSASLIPE NDPTTLFTSA GMQPMIPYLM GEKHPAGTRL
VDSQKCFRTQ DIDSVGDNRH TTCFEMLGNW SLGDYFKIEQ INWMFDFLIN KTKLDPNRFY
VTCFRGMEEI GIPRDTEAAE KWQAKFKEVN VEAKIVDNAE TEGMQGGRIF YYNEKENWWS
RAGVTSKMPV GEPGGPDSEM FWDFDPKGEL QIHEKSDWKD APCHPACDCG RFVEIGNNVF
MQYVKTKNGF EPLKNKNIDF GGGLERMVAA MNDDSDIFNI DAFAKAKEKL EKLSGKKYGE
NKDEIQAFRV ILDHLRAATF LIADGAVPSN KDQGYFTRRL IRRSIRYANK LGISNKFCAD
LADTYIEVYK DVYTYFSTSR DKIVEELNAE EDKFSATLEN GLKVLKANVA SWEKNFKNIK
FNGGFSFLLY ESYGFPPEMT LEELLKYPEV AKQLDVEEYW AEFRNNLKQH QDLSRAGAEQ
KFKGGLADTS ETTARLHTAT HLLQAALRKV LGIHVEQRGS NITAERLRFD FTHGEKMTDE
QKKQVEDLVN EWIQKDFEVK CEELPYAEAK TKNVMGLFEN KYGDLVKVYT IGDVSGEICG
GPHANRTGEL GKFKISKEEA SSSGVRRIKA VLE
//
