ID A0A0G1KUH0_9BACT Unreviewed; 586 AA.
AC A0A0G1KUH0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=UW53_C0004G0004 {ECO:0000313|EMBL:KKT59992.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWA1_44_25.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618645 {ECO:0000313|EMBL:KKT59992.1, ECO:0000313|Proteomes:UP000034087};
RN [1] {ECO:0000313|EMBL:KKT59992.1, ECO:0000313|Proteomes:UP000034087}
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:KKT59992.1}.
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DR EMBL; LCIR01000004; KKT59992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KUH0; -.
DR PATRIC; fig|1618645.3.peg.360; -.
DR Proteomes; UP000034087; 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:KKT59992.1};
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 3..586
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 586 AA; 66070 MW; 2B3987C7E9B4AD3A CRC64;
MIMSASELRE KFLDFFKEHG HKIVPSSSLI PDDPSVLLTT AGMQQFKPYF LGKADPIKDF
GGKRATSIQK CFRTSDIDEV GDESHLTFFE MLGHFSFGDY FKKETIAWTY ELLTEIFNIA
PERISATVFA GDEKIPFDKE SYNAWAEFLP SERIRKGSRA DNMWGPAGPE GPCGAANEVY
VDNLEVATLV FMEYFCAKDQ SLTPLPQKGV DVGWGFERLA MIVQGTKTIF ETDLFEPIAQ
LIKDNSGSED VKGIRIVADH VRAATFMIAD GIKPSNTDRG YILRRLLRRA RYYYNSLGAY
DKALGELVDH VVPIYKETNY GLNGKIPIID EIITSEEMTF SAHLGFGKKL LEKIIKNDGR
ISGENAFLLH STYGYPFELI LDIAKENNME VDENGFQEKQ KAHQEISRAG VEKKFGGHGL
LLDNGELKAA NEEELKKVTR LHTATHLLQA ALRKVLGEGV KQAGSDITAE RTRFDFTFER
KLTDEEIKKV EDSVNFAISQ KYDVQKKEMP HEDAIKSGAL HFFKEKYPPM VNVYSVGNFK
TDPPEIFSRE LCGGPHVKNT SEIGRFKILK QEPVGSGLRR LRATVY
//
