ID T2N958_PORGN Unreviewed; 597 AA.
AC T2N958;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:EOA10818.1};
GN ORFNames=A343_0437 {ECO:0000313|EMBL:EOA10818.1};
OS Porphyromonas gingivalis JCVI SC001.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1195243 {ECO:0000313|EMBL:EOA10818.1};
RN [1] {ECO:0000313|EMBL:EOA10818.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA10818.1};
RX PubMed=23564253; DOI=10.1101/gr.150433.112;
RA McLean J.S., Lombardo M.J., Ziegler M.G., Novotny M., Yee-Greenbaum J.,
RA Badger J.H., Tesler G., Nurk S., Lesin V., Brami D., Hall A.P., Edlund A.,
RA Allen L.Z., Durkin S., Reed S., Torriani F., Nealson K.H., Pevzner P.A.,
RA Friedman R., Venter J.C., Lasken R.S.;
RT "Genome of the pathogen Porphyromonas gingivalis recovered from a biofilm
RT in a hospital sink using a high-throughput single-cell genomics platform.";
RL Genome Res. 23:867-877(2013).
RN [2] {ECO:0000313|EMBL:EOA10818.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA10818.1};
RA McLean J., Yee-Greenbaum J., Durkin A.S., Lasken R.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOA10818.1}.
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DR EMBL; APMB01000137; EOA10818.1; -; Genomic_DNA.
DR AlphaFoldDB; T2N958; -.
DR PATRIC; fig|1195243.10.peg.552; -.
DR HOGENOM; CLU_006406_6_1_10; -.
DR Proteomes; UP000016542; Chromosome.
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 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 5..88
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 478..597
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 125..135
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 597 AA; 67473 MW; D0DEFDC31CEF9071 CRC64;
MSILQKLENS AAAAVKALYG TDPMEGQIQL QKTKREFKGH LTLVVFPFVK MSRKSPEATA
TEIGEWLLAN ESAVSAIEVV KGFLNLTIAP RVWLELLNEI RADINFGHKV ATEDSPLVMV
EYSSPNTNKP LHLGHVRNNL LGYSLSEIMK ANGYRVVKTN IVNDRGIHIC KSMLAWQKWG
DGVTPEKAGK KGDHLIGDFY VLFDKHYKAE LNSLMAEGKS KEEAEAASTL MAEAREMLRL
WEAGDEKVVD LWRTMNQWVY DGFDATYKMM GVDFDKIYYE SETYLVGKEE VLRGLEEGLF
VKHSDGSVWA DLTKDGLDEK LLLRADGTSV YMTQDIGTAK MRFNDYPINR MIYVVGNEQN
YHFQVLSILL DRLGFEFGKG LVHFSYGMVE LPEGKMKSRE GTVVDADDLM DEMIRTAAEI
AAEAGKAAEM DEEESHEVAR IVGLGSLKYF ILKVDPRKNM TFNPKESIDF NGNTGSFVQY
TYARIRSLMR RAEAAGYDIP SQLPTDLPLS EKEEALIQKV SEYAEVVSEA GHSYSPALIA
NYIYDLVKEY NQFYHDFSVL KEEDERIRAF RLALSEVVAL TMRKGFALLG IEMPERM
//
