ID A0A1F4QI81_9BACT Unreviewed; 785 AA.
AC A0A1F4QI81;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
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=A2Z31_04410 {ECO:0000313|EMBL:OGB95694.1};
OS candidate division NC10 bacterium RBG_16_65_8.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1801657 {ECO:0000313|EMBL:OGB95694.1, ECO:0000313|Proteomes:UP000177292};
RN [1] {ECO:0000313|EMBL:OGB95694.1, ECO:0000313|Proteomes:UP000177292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGB95694.1}.
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DR EMBL; METG01000043; OGB95694.1; -; Genomic_DNA.
DR Proteomes; UP000177292; 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 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGB95694.1};
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..617
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT REGION 745..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGB95694.1"
SQ SEQUENCE 785 AA; 85258 MW; 6317BCCEBE309C86 CRC64;
VAYAWEFLRR DLGLPAERLW ATIHEGDVGM NIGPDEEARS LWRQYVPDER IVACSTKDNF
WAMGDTGPCG PCSEIIYDQG PAMGCGKPTC AVGCDCDRYL ELWNLVFMQF ERNAEGALSP
LPRPSIDTGA GLERLAAVLQ KVPSNFDTDL LRPIIGFMEE LSGKRYGGDP QADVSLRVIA
DHARSTTFLV ADGVLPSNEG RGYVLRRILR RGLRXXXGRM LGLDEPFMAK VTGHVVDLMQ
GAYPDLADAR EHVARVTLVE EERFGHTLRV GLRLAESLME EHRAKRQTLI SGADIFRLYD
TYGFPVDLLR DIATDAGLAL DEAGFERAMA EQRTRARESW VGSGELEIPA GLKDLTAAVK
VEALWYTALD ADARVVAILG GEERRPADAL PEGAAGEVVL DRTPFYPESG GQVGDVGALS
ADGLLAEIRD TTRPVPGLVL HRVRVKRGTL RIGQTVRAVV DAACRRMMAK NHTATHLLHA
AMRHTLGDHV KQAGSLVAPD RLRFDFTHFS PLTPQEIDRI EEAVNAQIWE NRGVATRVMS
LDEALATGAV ALFGEKYGER VRVVSVREFS TELCGGTHVG ATGEIGLFKI VSQGGVAAGV
RRIEAVTGPG AYQHVKREAH VLAETAARLK ARPLELVDRV DKLAEASRDL EREVQRLQAR
LLGGTLERLL QSASEVNGVR VVGALVEAAD SKGMRELGDR LRERLQSGVV ALAMQADGRV
TWVTMVTKDL VGRLHAGHLA RDLAKLTGGG GGGRPDMAEA GGKDPGRIPD ALAKLPELIS
GQLQA
//
