ID U5NCE5_9MOLU Unreviewed; 555 AA.
AC U5NCE5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=PRV_01135 {ECO:0000313|EMBL:AGX88990.1};
OS Mycoplasma parvum str. Indiana.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1403316 {ECO:0000313|EMBL:AGX88990.1, ECO:0000313|Proteomes:UP000017119};
RN [1] {ECO:0000313|EMBL:AGX88990.1, ECO:0000313|Proteomes:UP000017119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indiana {ECO:0000313|EMBL:AGX88990.1,
RC ECO:0000313|Proteomes:UP000017119};
RX PubMed=24285648;
RA do Nascimento N.C., Dos Santos A.P., Chu Y., Guimaraes A.M., Pagliaro A.,
RA Messick J.B.;
RT "Genome Sequence of Mycoplasma parvum (Formerly Eperythrozoon parvum), a
RT Diminutive Hemoplasma of the Pig.";
RL Genome Announc. 1:e00986-13(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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR EMBL; CP006771; AGX88990.1; -; Genomic_DNA.
DR RefSeq; WP_022769385.1; NC_022575.1.
DR AlphaFoldDB; U5NCE5; -.
DR STRING; 1403316.PRV_01135; -.
DR KEGG; mpv:PRV_01135; -.
DR PATRIC; fig|1403316.3.peg.200; -.
DR HOGENOM; CLU_006406_0_1_14; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000017119; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 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|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000017119}.
FT DOMAIN 3..89
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 438..544
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 555 AA; 64598 MW; 8D807DAC5D62423E CRC64;
MILTLKEQLK EALREVLVKK NFTLLLDKIE LEESKNSKFG FFSTNLPFLI SSTYKKNIEE
SEQLLLDSLN KHEEIPKIEA VQGYLNFFIS SNLIKNFYKS SLKRKKIIAF SNNEENKKTK
YFIEIVSANP TGILHIGHIR NGVITDTLSN ILEYNNNSVF RAYLINDAGT QIEELIKSIH
TFYSFISKGA SINLMEHSIK YSGNEIRDCA QAITEKFGHY WELDNEELTQ KIKLFAVEFF
VNLIKKELDS LSIKVDNWDY ESKKCSESAL THLIKKLQDF IYLKDNALWF KTSSFKKEGD
EKDDVIVKSD GNLSYFGQDL IYHLYKLEFL GTNGIIINTL AEDHKGHIDR MKAFFSSINV
PESLVKYKTT KLSRLIVDGK KIVFSKRENI FLSSEELKEH LSKDEIRWFL CSRDEENELD
IDLSKLNNKD YNNPIFYILY AYSRALKITE KINFELDGVE LSFEKLDSEI EQSLINSILA
VEFHFQKAIQ NLKVHIISNY LYSLAKKFHT FYESFSIIND SNRETQLARL ALVQLVLRIF
KEFLPLFRIV PTALA
//
