ID A0A1F7J4N6_9BACT Unreviewed; 606 AA.
AC A0A1F7J4N6;
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=A3B50_02100 {ECO:0000313|EMBL:OGK50552.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_40_42.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802066 {ECO:0000313|EMBL:OGK50552.1, ECO:0000313|Proteomes:UP000178558};
RN [1] {ECO:0000313|EMBL:OGK50552.1, ECO:0000313|Proteomes:UP000178558}
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:OGK50552.1}.
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DR EMBL; MGAQ01000015; OGK50552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7J4N6; -.
DR Proteomes; UP000178558; 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 3..606
FT /note="Alanyl-transfer RNA synthetases family profile"
FT /evidence="ECO:0000259|PROSITE:PS50860"
SQ SEQUENCE 606 AA; 69695 MW; 91543851F03D3607 CRC64;
MKVTHQALRS LFADFWESKG HKEVPPIPLV PQNDPTTLFT GSGMQPLVPY LLGEPHPLGE
KLYNIQPCFR AQDIEEVGNN RHTTAFEMMG NWSLGTYFKK EQITWFHTFL TRIIKLDPSK
LHVTVFEGSR DIPKDEESAK LWRSLGIPKE RIYFYGTEKN WWSRSGKPEG MPAGEPGGPD
TEVFYDFGEE RKIHENSSFK DKKCHPNCDC GRFIEIGNSV FMQYQKQKDG SFKELPKKNV
DFGGGFERIL AAIYDDPDVF KSDLYEAIIA TIVDVSGKKY DEESNKQAIR IIADHLKASV
FLIVDGVTPS NKEQGYVLRR LLRRAAVKMR SLKGSLGKGE DFRRISESVL ETYGEVYFSK
AKDLKIIAGV IEDEITKFQK SLERGLREVQ KVKDINGKVA FDFYQTYGFP LELTEELFRE
RGQSVNHEQF QKEFENHKNL SRSASAGKFK GGLADHSDQV LKYHTATHLM HQALFDVLGE
GVKQEGSNIT KDRFRFDFSS LKKFTKEDVQ KTEDIINKKV KEELPMRFKI MTKDEAYEIG
ARSFFREKYP DKVKVYYLGG EDDKPETAYS KEFCGGPHVK NTKEIGKIKI YKFENIGSNL
YRLYAK
//
