ID A0A0W4ZW12_PNEJ7 Unreviewed; 646 AA.
AC A0A0W4ZW12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN ORFNames=T551_00041 {ECO:0000313|EMBL:KTW32556.1};
OS Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW32556.1, ECO:0000313|Proteomes:UP000053447};
RN [1] {ECO:0000313|Proteomes:UP000053447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
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}.
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:KTW32556.1}.
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DR EMBL; LFWA01000001; KTW32556.1; -; Genomic_DNA.
DR RefSeq; XP_018231248.1; XM_018372308.1.
DR AlphaFoldDB; A0A0W4ZW12; -.
DR STRING; 1408657.A0A0W4ZW12; -.
DR GeneID; 28938563; -.
DR VEuPathDB; FungiDB:T551_00041; -.
DR eggNOG; KOG1195; Eukaryota.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000053447; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 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; 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|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|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000053447}.
FT DOMAIN 521..638
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 646 AA; 74770 MW; E3FAA6D8425861FD CRC64;
MLRTTCLLRA IITRFYRINR QKNTVFKSFY SRNMKNIDTF DDLSKNLKEI GISEDILSLE
GTDPFKNPID IFRTYISYHL SKITSISVKI LLPMLEQVSK LENGDLMLPV ARLRLQEKPD
ILAEKWAQKF PQTIVRAKNQ GSFIQFFFSP ELLTDLVISY IYRDDHKYGS NDSGKGKKIL
VEFGSPNIAK PFHAGHLRST IIGSFVSNIH ELCSWEVIRF NYLGDWGKQF GLLAIGFELY
GSEEELERDP IQHLYDVYVK INTIASQKDN PEADNVNEKA REYFKKMEEG NENFLKLWKR
FRDFSIEKYK TTYSRLNIHY DEYGGESKVS QQNIEDVMRV LKKKNLLKED KGAILIDLSK
FSKKLGNAML KKSDGTTLYL TRDIGEAIQR YEHYKFDKMI YVVSSQQELH LAQLFKILEL
LDLPWAKSCS HISYGLVLGM STRKGTAVFL DSILETAQEN MHEIMKKNQK KYIQIENPKF
VSDIVGISAI LIQDMSSKRI NNYSFLWSRI LSFEGDTGPY LQYAHSRLAS IIRHSNISIE
NIKKAELNCL TESNAIDLIR VLAKYPDVIN TTIRTLEPST IITYLFKLTH IISGCYDILW
VMNQPENIAT ARLSLYLACK KVLNNGMRLL GLTPLERYIL FINYLS
//
