GenomeNet

Database: UniProt
Entry: I0RBT6_9FIRM
LinkDB: I0RBT6_9FIRM
Original site: I0RBT6_9FIRM 
ID   I0RBT6_9FIRM            Unreviewed;       590 AA.
AC   I0RBT6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
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:EIC97144.1};
GN   ORFNames=HMPREF9970_1091 {ECO:0000313|EMBL:EIC97144.1};
OS   Lachnoanaerobaculum saburreum F0468.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnoanaerobaculum.
OX   NCBI_TaxID=1095750 {ECO:0000313|EMBL:EIC97144.1, ECO:0000313|Proteomes:UP000005039};
RN   [1] {ECO:0000313|EMBL:EIC97144.1, ECO:0000313|Proteomes:UP000005039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0468 {ECO:0000313|EMBL:EIC97144.1,
RC   ECO:0000313|Proteomes:UP000005039};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (MAR-2012) 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:EIC97144.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJGH01000006; EIC97144.1; -; Genomic_DNA.
DR   RefSeq; WP_008752836.1; NZ_AJGH01000006.1.
DR   AlphaFoldDB; I0RBT6; -.
DR   PATRIC; fig|1095750.3.peg.133; -.
DR   eggNOG; COG0018; Bacteria.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000005039; 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   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; 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:SF11; ARGININE--TRNA LIGASE, MITOCHONDRIAL-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.
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}; Cytoplasm {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          2..87
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          471..590
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   590 AA;  66990 MW;  93B32DB8A4F3562F CRC64;
     MKTIIELISD ELKSAFVKLS YDEKYGKVNI SNRPDLCEYQ CNGAMAAAKV FKKKPIDIAN
     EVVELLKESD SFDKIEAVMP GFININISNS FIEKYIKDMS NAPKYGIEFD SPAKKIIIDY
     GGANVAKPLH IGHLRSAIIG ESLKRMGRFF GNEMIADVHL GDWGLQIGLI IEELRERKPD
     LVYFKENYDG EFPKEAPFTL NDLEELYPAA SKKSKVDEGF RQRAQEATLE LQNGYKPYRA
     IWRHIMNLSI EDLKKNYGSL LVDFDLWKGE SDADPYIPDL IKDLEDRKIA RVSEGALVVD
     IAMEGDKKEL PPCIIRKSDG AALYATSDLG TLIEREKLYS PDEYIYIADK RQELHYTQFF
     RVAKIAGIVP DNHVLKYIGF GTINGKDGKP LKTRDGGVVR LETVIKDIED AVFAKIKETR
     DEVSDEEARN TAKIVGLAAI KYADLSNQAA KDYIFDIDRF TSFEGNTGPY ILYTIVRIKS
     ILEKYYESGN EKVSLNDLTI PKEDIHKKLY MELAGYNEIM RAAWTELAPH KICQFIYSVS
     NTFNSFYHEI KILSESDEKK KKGYLATILL TKKILESAIN LLGIEAPDKM
//
DBGET integrated database retrieval system