ID I3AWD0_BIFLN Unreviewed; 620 AA.
AC I3AWD0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123,
GN ECO:0000313|EMBL:EIJ23423.1};
GN ORFNames=HMPREF1314_0109 {ECO:0000313|EMBL:EIJ23423.1};
OS Bifidobacterium longum subsp. longum 35B.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1161904 {ECO:0000313|EMBL:EIJ23423.1, ECO:0000313|Proteomes:UP000004446};
RN [1] {ECO:0000313|EMBL:EIJ23423.1, ECO:0000313|Proteomes:UP000004446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35B {ECO:0000313|EMBL:EIJ23423.1};
RX PubMed=23682142;
RA Shkoporov A.N., Efimov B.A., Khokhlova E.V., Chaplin A.V., Kafarskaya L.I.,
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Sutton G., Weibel D.B.,
RA Nelson K.E., Smeianov V.V.;
RT "Draft Genome Sequences of Two Pairs of Human Intestinal Bifidobacterium
RT longum subsp. longum Strains, 44B and 1-6B and 35B and 2-2B, Consecutively
RT Isolated from Two Children after a 5-Year Time Period.";
RL Genome Announc. 1:E00234-E00213(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000256|ARBA:ARBA00001766,
CC ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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:EIJ23423.1}.
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DR EMBL; AJTI01000100; EIJ23423.1; -; Genomic_DNA.
DR RefSeq; WP_007057494.1; NZ_AJTI01000100.1.
DR AlphaFoldDB; I3AWD0; -.
DR PATRIC; fig|1161904.3.peg.1532; -.
DR Proteomes; UP000004446; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00123; Arg_tRNA_synth; 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; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00456; argS; 1.
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; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
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:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}.
FT DOMAIN 4..98
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 480..620
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 147..157
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 620 AA; 67264 MW; 05A79761A32784FF CRC64;
MSPEALSELI SSIAHNLVAA GQAGALTDEL IPPVDKLAVM RPKDRAHGDW ASNIAMQLAK
KAGMKPRDLA EPFAAALAEA DGIAKVEVAG PGFINITLDS ASAAAVVDTV LAAGAVTDAD
KHLNKVNEYG RNDHLGGQTL NLEFVSANPT GPIHIGGTRW AAVGDAMARV LEANGAKVVR
EYYFNDHGEQ INRFAKSLVA AWAEANNLGE AGYQTETPCD GYKGAYINEI AARVQAEAES
DGVDLTALAH QDRGLNDDGE PLGEADTEVR EEFRKRAVPM MFDEIQKSMK DFRVNFDVWF
HENSLYADGK VDAAIEELKS RGDIFDKDGA TWFESTKHGD DKDRVIIKSN GEFAYFAADI
AYYWDKRHRA ENSADVAIYM LGADHHGYIG RMMAMCAAFG DEPGKNMQIL IGQLVNVMKD
GKPVRMSKRA GNVVTIDDLV SVVGVDAARY SLARSDYNQN FDIDLALLAS HTNDNPVYYV
QYAHARSKNV DRNAAAAGIS YEGADLALLD TEADGEVLAA LAQFPSVLAT AADDRQPHKV
ARYLEELAAT YHKWYNVERV VPMALTDPET RGDDEARKAL EIAKNPEPAR AAARLKLNDA
VQQVIANGLD LLGVTAPEKM
//
