GenomeNet

Database: UniProt
Entry: A0A0F4KV58_9LACO
LinkDB: A0A0F4KV58_9LACO
Original site: A0A0F4KV58_9LACO 
ID   A0A0F4KV58_9LACO        Unreviewed;       571 AA.
AC   A0A0F4KV58;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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:KJY49106.1};
GN   ORFNames=JG29_05550 {ECO:0000313|EMBL:KJY49106.1};
OS   Bombilactobacillus mellis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Bombilactobacillus.
OX   NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY49106.1, ECO:0000313|Proteomes:UP000033695};
RN   [1] {ECO:0000313|EMBL:KJY49106.1, ECO:0000313|Proteomes:UP000033695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hon2 {ECO:0000313|EMBL:KJY49106.1,
RC   ECO:0000313|Proteomes:UP000033695};
RA   Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA   Vasquez A.;
RT   "Comparative genomics of the lactic acid bacteria isolated from the honey
RT   bee gut.";
RL   Submitted (DEC-2014) 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:KJY49106.1}.
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; JXBZ01000005; KJY49106.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4KV58; -.
DR   STRING; 1218508.JG29_05550; -.
DR   PATRIC; fig|1218508.4.peg.570; -.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   Proteomes; UP000033695; 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; cd07956; Anticodon_Ia_Arg; 1.
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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000033695}.
FT   DOMAIN          8..91
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          456..571
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           129..139
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   571 AA;  64504 MW;  42F207E299F77561 CRC64;
     MKINQARQLV QQAVYEALKN LDEITISPEQ VQQMVEIPKN SQLGDFAFPT FRLAKQLHQA
     PVKIAQNLAK EVDSSQFAQV CAQGPYVNFF LQRKDIAATT IEEVIKQKNN FGNSTVGANS
     VVTIDMSSPN IAKPMSMGHL RSTVIGNSIA LILDKLNYHP VKINHLGDWG TQFGKLMVAY
     KKWGSEADVK KDPITNLQKY YVKFHKLDKE HPELDEEARE WFKKLENGDE EATQLWQWFR
     SESLKSFMKV YDELGIKFDS YNGEAFYNDK MDEILDLLEH KGLLQESKGA EIVDLGSDLP
     PALIKKSDGA TLYITRDLAA ALYRKRTYHF KKSLYVVGSE QSIHFEQLKA VLAKMGFTWA
     QDIEHIKFGL ITANGKKLST REGRVILLEN VLHDSVQLAQ EQIAEKNPTL ANKDQVAHAV
     GVGAVIFHDL KNNRTDNFDF NLEEVVRFEG ETGPYVQYTH ARAMSILRKA GPQAQDEAAV
     FDTDVDDVTW DILKHLANFP ETVQQAAQLR EPSVIAKYAL HLAKSFNHYY AQTKVLVDDD
     QLAARLNLVQ AVAIVLKEAL RLLGVQAPDE M
//
DBGET integrated database retrieval system