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Database: UniProt
Entry: C4XFX9_MYCFP
LinkDB: C4XFX9_MYCFP
Original site: C4XFX9_MYCFP 
ID   C4XFX9_MYCFP            Unreviewed;       553 AA.
AC   C4XFX9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   OrderedLocusNames=MBIO_0786 {ECO:0000313|EMBL:BAH70051.1};
OS   Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS   PG18) (Mycoplasma fermentans).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=496833 {ECO:0000313|EMBL:BAH70051.1, ECO:0000313|Proteomes:UP000006810};
RN   [1] {ECO:0000313|EMBL:BAH70051.1, ECO:0000313|Proteomes:UP000006810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18
RC   {ECO:0000313|Proteomes:UP000006810};
RX   PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA   Ishida N., Irikura D., Matsuda K., Sato S., Asano K.;
RT   "Molecular cloning and expression of a novel cholinephosphotransferase
RT   involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT   fermentans.";
RL   Curr. Microbiol. 58:535-540(2009).
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; AP009608; BAH70051.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4XFX9; -.
DR   KEGG; mfp:MBIO_0786; -.
DR   PATRIC; fig|496833.3.peg.379; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_501365_0_0_14; -.
DR   Proteomes; UP000006810; Chromosome.
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; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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   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   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363038};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
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|RuleBase:RU363038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006810}.
FT   DOMAIN          122..409
FT                   /note="Arginyl-tRNA synthetase catalytic core"
FT                   /evidence="ECO:0000259|Pfam:PF00750"
FT   DOMAIN          451..551
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   553 AA;  65077 MW;  F8522F5639CF0C63 CRC64;
     MYLKIYSGSN MVIVHKLNKL IKNIVNELKA ENKIFSSFKF LDGEKKFSLK MARKTKGHNN
     NINHIECDIV FQLKKFSFIP YIELAEEIKK RLIKDSMVKD VTIDRYGLLH IVLNEKDLVS
     VVNEVIKKAY KYGQEKKNNI KVNIEYTSAS PLNSLTLMNA RNALVGETIA RILEYLGYQV
     TREFLVYPGL KKMEKVSQIV HEQYVNLFEL NDNSIKVDKD ILECAKNIKA QNGDLYLDIN
     DTIKRNKFDL AIVFYFLNKS KKQLKNLGVF FDIVSYFEDI LVKEKIDKVL ELLSPFIYDN
     DSNLILNTNL DDSKERILVH RNGTSSYLLL DIIYHLEKLK RADWIIDILD ANHTQYSHSL
     ISALKFLNAY NNNIDIAFCE NFQIKENNEV KSMTEKNQNV IFIDELVKKV NLNEIKFFFL
     EKSTKHQITI EKEILNQKKI SHNFDFILNT YNKINKLLDE SKNNKCYCNK MNQNNFLSKL
     ILRLDYFPYV LRKVIKTLNP FYLTKYLKEM CYLINQNLKD KLKKDYRNFY PILEAVKNVF
     DNGLNLLGID FKN
//
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