ID W1U2V4_9FIRM Unreviewed; 842 AA.
AC W1U2V4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00017959};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032577};
DE Flags: Fragment;
GN ORFNames=Q612_NSC00210G0001 {ECO:0000313|EMBL:ETI88016.1};
OS Negativicoccus succinicivorans DORA_17_25.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Negativicoccus.
OX NCBI_TaxID=1403945 {ECO:0000313|EMBL:ETI88016.1, ECO:0000313|Proteomes:UP000018840};
RN [1] {ECO:0000313|EMBL:ETI88016.1, ECO:0000313|Proteomes:UP000018840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_17_25 {ECO:0000313|Proteomes:UP000018840};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain. {ECO:0000256|ARBA:ARBA00024779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001676};
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:ETI88016.1}.
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DR EMBL; AZMC01000210; ETI88016.1; -; Genomic_DNA.
DR AlphaFoldDB; W1U2V4; -.
DR Proteomes; UP000018840; 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:0016740; F:transferase activity; IEA:UniProt.
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; 2.40.30.130; -; 1.
DR Gene3D; 3.10.310.40; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 6.10.250.550; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 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; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00344; alaS; 1.
DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02272; DHHA1; 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 SUPFAM; SSF50447; Translation proteins; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ETI88016.1};
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..700
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT COILED 716..743
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 842
FT /evidence="ECO:0000313|EMBL:ETI88016.1"
SQ SEQUENCE 842 AA; 91997 MW; 9616A6F7FF6AC123 CRC64;
MKGNEIRERY LRFFEERGHL HLPSFPLIPK DDPSLLLIGA GMAPLKPFFT GKVEPPRHRV
VTCQKCMRTG DLENVGRTAR HHTFFEMLGN FSFGDYFKQD AIQWAWQFLT EELQLDPERL
YVTIHPEDKE AYALWHETVG LPDERIYKLE DNFWEIGEGP CGPCSEIFYD QGESFGTGPE
NAMGSDGDRF LEIWNLVFTQ YNRTKDGQYE PLAKKNIDTG AGLERLAAVL QKKRNNFETD
LIFPLIERAA ALAGTKYNTS AETDVALKVI ADHSRAVTAL IGDGVLPSNE GRGYVLRRIL
RRAVRQGKLL GINQPFMAEL VDLVIDLLGQ GLPDLFEKMA YIKKIAASEE ARFQKTLDQG
SLLLQEKIDA AKEQQKTSLS GEDVFQLYDT YGFPWELTEE IAAEAGLAID IDGFKTAMKT
QRERARQARA KVSAKVATPD TTRLAGAGKT ADETATASEI LMLGRDGVEI ESASDGESVL
IILATNPFHA EGGGQLGDIG ELQSATGKVE ITDTKKNPDG TIYLLGEVTE GTIERGAEVT
LAVDTERRHD MARNHTATHL LQAALRHVLG DHVTQAGSVV MPERLRFDFT HPEPLSADEL
KAVEAEVNER ILAGISTNIR ELPIEEAKAL GAIALFGEKY GNIVRVVEVP EVSIELCGGS
HVRNTGEIGS FRILSESGIG SGIRRIEAVT GHAAYRLAQQ DTNDLAQAAE LLKARPQELL
EKLEKLLAEK KELAQELSSL HQAQAKDQVG DLVKNAVTQD GLRIASGVVE VADVQELRAL
GDMLKARDDI QALVLGAQIG EKVNLVAMAD ATAVARGIHA GNAVTGAAKV AGGGGGGRPD
MA
//
