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Database: UniProt
Entry: A0A0H3J2I8_CLOPA
LinkDB: A0A0H3J2I8_CLOPA
Original site: A0A0H3J2I8_CLOPA 
ID   A0A0H3J2I8_CLOPA        Unreviewed;       563 AA.
AC   A0A0H3J2I8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:AJA51642.1};
GN   ORFNames=CLPA_c15790 {ECO:0000313|EMBL:AJA51642.1}, CP6013_01598
GN   {ECO:0000313|EMBL:KRU12351.1};
OS   Clostridium pasteurianum DSM 525 = ATCC 6013.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA51642.1, ECO:0000313|Proteomes:UP000030905};
RN   [1] {ECO:0000313|EMBL:AJA51642.1, ECO:0000313|Proteomes:UP000030905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 525 {ECO:0000313|EMBL:AJA51642.1}, and DSM 525 / ATCC 6013
RC   {ECO:0000313|Proteomes:UP000030905};
RX   PubMed=25700415;
RA   Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT   "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT   Clostridium pasteurianum DSM 525.";
RL   Genome Announc. 3:e01591-e01514(2015).
RN   [2] {ECO:0000313|EMBL:KRU12351.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU12351.1};
RA   Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT   "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT   6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KRU12351.1, ECO:0000313|Proteomes:UP000028042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU12351.1,
RC   ECO:0000313|Proteomes:UP000028042};
RX   PubMed=25103768;
RA   Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT   "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT   6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL   Genome Announc. 2:0-0(0).
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; CP009268; AJA51642.1; -; Genomic_DNA.
DR   EMBL; JPGY02000001; KRU12351.1; -; Genomic_DNA.
DR   RefSeq; WP_003447138.1; NZ_JPGY02000001.1.
DR   AlphaFoldDB; A0A0H3J2I8; -.
DR   GeneID; 76626003; -.
DR   KEGG; cpae:CPAST_c15790; -.
DR   KEGG; cpat:CLPA_c15790; -.
DR   PATRIC; fig|1262449.3.peg.3337; -.
DR   eggNOG; COG0018; Bacteria.
DR   Proteomes; UP000028042; Unassembled WGS sequence.
DR   Proteomes; UP000030905; 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   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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030905}.
FT   DOMAIN          1..82
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          448..563
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           120..130
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   563 AA;  64653 MW;  A41D34CC56761CCB CRC64;
     MDYKKIITAR IKDTVDLELE TIERLIEIPP KSEMGDYAFP CFSLAKALRK APNIIAEDMA
     KNIYKEGFEK IENLGPYLNF FVDKAVFMKN TIETVLTEKD SYGSSEVGKG KNITIDFSSP
     NIAKPFHVGH LFSTAIGNSL YRILSFEGYN CIGINHLGDW GTQFGKLICA YKRWCDKEKL
     EKEPIKELLR IYVKFHDEAD RDSSIEDEAR MYFKKLEDGE KEEIELWEKF RELSLKEFQK
     VYYLLNVKFD SYAGESFYND KMDAVVEEID KKGLLVDSNG AKVVMLDEFN MPPCIIKKSD
     GATIYATRDL TAAEYRKNTY NFYKSIYVVG GEQKLHFKQV FKTLELMGYD WAKDCNHVSF
     GLVKFADKKL STRKGEVIFL EDLLNESISK TLEIINEKNP ELENKEEVAK KVGVGAMVFT
     YLKNSREKDI VFDWKDMLSF DGETGPYVQY TYARAKSILR KLGNGSGEID YSKLNTSEEF
     ELVKYIESFQ NAILAAIDKL EPSILTRHII EIAKAFNKFY NLHKIATEED KEIKNARLKL
     VEATAQVIKN GLNLLGISVV ESM
//
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