ID A0A1G2I0W0_9BACT Unreviewed; 481 AA.
AC A0A1G2I0W0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
DE Flags: Fragment;
GN ORFNames=A3D35_01525 {ECO:0000313|EMBL:OGZ67698.1};
OS Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_02_FULL_34_9.
OC Bacteria; Candidatus Staskawiczbacteria.
OX NCBI_TaxID=1802206 {ECO:0000313|EMBL:OGZ67698.1, ECO:0000313|Proteomes:UP000176421};
RN [1] {ECO:0000313|EMBL:OGZ67698.1, ECO:0000313|Proteomes:UP000176421}
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:OGZ67698.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHOS01000033; OGZ67698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2I0W0; -.
DR STRING; 1802206.A3D35_01525; -.
DR Proteomes; UP000176421; 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 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 PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
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};
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..384
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
FT NON_TER 481
FT /evidence="ECO:0000313|EMBL:OGZ67698.1"
SQ SEQUENCE 481 AA; 55956 MW; 798AFDC15DDED7ED CRC64;
MNSVELRQKF LKFFKERGHE IIPSASLIPN KQDSTVLFNT AGMQPLVPFL MGEKHPKGTR
LVNYQKCIRT GDIEEVGDDT HLTFFEMLGN WSLGDYWKED SIKWSFEFLT KELRIPLEKL
AVSCFIGDDN VSKDEESAKI WESLGIKKER IAFLPKEDNW WGPVGETGPC GPDTEIFYWK
SSDPSPDKFN SEDKNWVEIW NNVFMQYNKT QGGKYELADQ KNVDTGMGLE RIVAVLNGKT
SVYETDLFLP IMEIFPGHFD ERKKRIVADH AKASIFLISD GIVPSNKDQG YVLRRLLRRM
MVYMRDFNKE ELFDPIKKCM EIYRDLYLLD ENKILEVIKE EADKFEKTLS EGLKVIEKMD
TVTGKEAFNL YETYGFPLEV LEEMRVVDNR EEFFEELKRH KELSRTASVG MFKGGLADHS
PETVRLHTAH HLLLAALQEL FSKEVKQRGS NINSERLRID FSFDRKLTDD EKKQLEDMVN
D
//
