ID A0A1W9P3L8_9BACT Unreviewed; 351 AA.
AC A0A1W9P3L8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
DE Flags: Fragment;
GN ORFNames=B5M54_08135 {ECO:0000313|EMBL:OQX52810.1};
OS Candidatus Aminicenantes bacterium 4484_214.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1968529 {ECO:0000313|EMBL:OQX52810.1, ECO:0000313|Proteomes:UP000192734};
RN [1] {ECO:0000313|Proteomes:UP000192734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:OQX52810.1}.
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DR EMBL; MZGL01000054; OQX52810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9P3L8; -.
DR Proteomes; UP000192734; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02938; GAD; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55261; GAD domain-like; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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}.
FT DOMAIN 28..310
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQX52810.1"
SQ SEQUENCE 351 AA; 38998 MW; 0CA2BB4D3E1DAFED CRC64;
ARLKTSSSST STSISPVASR GLHKCGARRR TFPRLSYEEA LARYGTDKPD LRLKATLEDL
TALVPRLGSQ VLERAVEAGG RVIGLCVPGG QAFSRTQLSK LTRRVQDWGA KGLIWVKKKD
PGWQASLPLP QENIALLWQT AKAEEDSLLL LVAGPENQTR EIMGRLRLEL CPPDPELKDT
FQCLWITDFP LFEWSEEENR LVSMHHPFTA PHEEDLELLT DDPLKVRAKA YDLVCNGYEI
GGGSIRIHKQ DLQEKIFDLL GLSPAEVEQK FGFFLEALRY GTPPHGGIAL GFDRIVMLLA
GETSIREVIP FPKTTSSLCL LTGAPSPVRP EQLRELGLIL ADKPLDEDEE A
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