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Database: UniProt
Entry: U3Q5C6_9FLAO
LinkDB: U3Q5C6_9FLAO
Original site: U3Q5C6_9FLAO 
ID   U3Q5C6_9FLAO            Unreviewed;       590 AA.
AC   U3Q5C6;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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   ORFNames=K645_2141 {ECO:0000313|EMBL:AGW86207.1};
OS   Blattabacterium sp. (Nauphoeta cinerea).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1316444 {ECO:0000313|EMBL:AGW86207.1, ECO:0000313|Proteomes:UP000016822};
RN   [1] {ECO:0000313|EMBL:AGW86207.1, ECO:0000313|Proteomes:UP000016822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nauphoeta cinerea {ECO:0000313|Proteomes:UP000016822};
RX   PubMed=24071059; DOI=10.1016/j.ygeno.2013.09.003;
RA   Kambhampati S., Alleman A., Park Y.;
RT   "Complete genome sequence of the endosymbiont Blattabacterium from the
RT   cockroach Nauphoeta cinerea (Blattodea: Blaberidae).";
RL   Genomics 102:479-483(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}.
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DR   EMBL; CP005488; AGW86207.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3Q5C6; -.
DR   STRING; 1316444.K645_2141; -.
DR   KEGG; blu:K645_2141; -.
DR   PATRIC; fig|1316444.3.peg.436; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_10; -.
DR   Proteomes; UP000016822; 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; 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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
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          472..590
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   590 AA;  69475 MW;  984CC10AEF69D073 CRC64;
     MLSMNDHLQS IEKIVIESIF VLYKIKSCPE LDFQYTKKEY PGDITLVLFS LSKKLKKPVE
     KIGKDIGNYV QNKLKGLIQF SIIRGFLNFI FEDDYYIYLL KKMLNTNFYD LKYPTKKIMV
     EYSSPNTNKP LHLGHIRNSL IGASLAEILK MVGHEIIRTQ IINDRGIHIC KSMIAWKRFG
     KGKTPDSAKM KGDHFVGKYY SLFDKISCKE IQELDNKSSK EDYNQYSILN QARELLKKWE
     LGDSEIRNTW RTMNQWVYNG FEETYKKLGI HFDKIEYESD IYKMGKEIVK KGLKKGIFFQ
     KKDGSIWIDL TKEGFDQKLL LRSDQTSVYI TQDIGTAVER FKKYNIDQII YIVGKEQDYH
     FQVLFNILKR LGYIWVNKLF HLSYEMVYLP SGRMKSREGN IVDADSIILE MYSIAKKNFS
     NKFIKKEEQK QSSEILGLGA LKYFFLKIDP RKKIIFHPEK SIDFKGKTGT YIQYTYSRIR
     SLERKFLNLC PLLNYHWSNI KFDIHEKNMI KILQKYPLVL KKSAIQLNPS LIANYIYEVS
     KIFNHLYQYK RLIDPLNVIH SNICMNIIHV TGNVLKSGMN LLGIKMLDRI
//
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