ID T1CRM1_9ZZZZ Unreviewed; 333 AA.
AC T1CRM1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Arginyl-tRNA synthetase {ECO:0000313|EMBL:EQD71900.1};
DE EC=6.1.1.19 {ECO:0000313|EMBL:EQD71900.1};
DE Flags: Fragment;
GN ORFNames=B1A_05574 {ECO:0000313|EMBL:EQD71900.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD71900.1};
RN [1] {ECO:0000313|EMBL:EQD71900.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD71900.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:EQD71900.1}.
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DR EMBL; AUZX01004070; EQD71900.1; -; Genomic_DNA.
DR AlphaFoldDB; T1CRM1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EQD71900.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EQD71900.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 2..37
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03485"
FT DOMAIN 46..133
FT /note="Arginyl-tRNA synthetase catalytic core"
FT /evidence="ECO:0000259|Pfam:PF00750"
FT NON_TER 333
FT /evidence="ECO:0000313|EMBL:EQD71900.1"
SQ SEQUENCE 333 AA; 37085 MW; 3D6E4AF3230D2580 CRC64;
MRQPPREVAA QLIAALPSSS LIDRVELAGP GFINIFLTAQ ARQEVVHEIL RHGPLFGSSQ
KGSGRRVQVE FVSSNPTGPL HVGHGRGAAY GASVANLLCK AGYQVHREYY VNDAGRQMDI
LTVSTWLRAL QQSGKLKSLP FPNNGYQGDY VETMARETAQ RFSGLVVSEE SLLSTLRLPH
TDDLIVISPE EEEHHMDALI AAAKELLGPT YLALHHFVLT EQLDDCREDL EEFGVIFDEW
FSEQSLFDSG AVALVVSRLE NAGHLYTEKG ARWFRSSAFG DEKDRVVQRE NGLYTYFASD
IAYHAGKFER GYDLIVDIWG ADHHGYIPRV RAA
//
