ID A0A1F5YJ81_9BACT Unreviewed; 619 AA.
AC A0A1F5YJ81;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE RecName: Full=alanine--tRNA ligase {ECO:0000256|ARBA:ARBA00013168};
DE EC=6.1.1.7 {ECO:0000256|ARBA:ARBA00013168};
GN ORFNames=A2Y99_03365 {ECO:0000313|EMBL:OGG00226.1};
OS Candidatus Gottesmanbacteria bacterium RBG_13_37_7.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798369 {ECO:0000313|EMBL:OGG00226.1, ECO:0000313|Proteomes:UP000178230};
RN [1] {ECO:0000313|EMBL:OGG00226.1, ECO:0000313|Proteomes:UP000178230}
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:OGG00226.1}.
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DR EMBL; MFIY01000018; OGG00226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5YJ81; -.
DR Proteomes; UP000178230; 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};
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..619
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 619 AA; 70658 MW; 22C8D00657062944 CRC64;
MSYPVLRKKF IDFFTAPPRN HKKIPSFPLI PENDPTVLFI TAGMHPLVPY LLGEPHPLGK
RLVDIQKSVR TDDIEEVGDL SHLTFFEMLG NWSLGDYFKK DAILWSFEFL TDKHWLGLDP
RRLYVSIFEG DKDAPCDSES ISYWQEAFNK IGISAEIGNP YTDNPNSKRI FPYPKNKNWW
GPAGLTGPCG PDSEMFFDTL LPLHNPSVHG RNCHINCSCG RFMEIWNDVF MEYYKNPDGT
YTILKQKNVD TGMGMERVVS LMEWLNGNIS EPDPFLTSLF QEIIEEIQKQ SKLSYAKEQK
PMRVIADHTR AATFLLADGI YPCNKERGYV LRKLIRRTIR FGNNIGIKHT FMSTLAEKAI
NIYAKYYPEL VARKKEIITQ IASEEERFQK TLALGLKEME KINLLTAKTA FDLYQNFGFP
WEMTLEIAKE KGQIIEKKLF EKEFQKHQKI SRTANKGIFK GGLQDRSEIT TKLHTATHLL
QQALIQILGK SVRQAGSHIT SERLRFDFTY AQKIEKTQLK KIEDQVNKII QKNLPITMKI
VNIKQAISQG ALTVPGVTYP EAVKVFTIES ITTSGKPYSM EVCGGPHVDF TGKLGLFKII
KEEGIAGGNR RIYAAVSTS
//