ID W6QXV8_PENRF Unreviewed; 645 AA.
AC W6QXV8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=PROQFM164_S03g001091 {ECO:0000313|EMBL:CDM34367.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34367.1};
RN [1] {ECO:0000313|EMBL:CDM34367.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM34367.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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 ---------------------------------------------------------------------------
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; HG792017; CDM34367.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QXV8; -.
DR STRING; 1365484.W6QXV8; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 67085at2759; -.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 35..115
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 528..645
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 249..286
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 645 AA; 72296 MW; F418B711A99CD966 CRC64;
MSAASLPASV EALSLQSTAQ KSQFAGCFPT LNPMDIYRQH IAEELGKAAG IDSQKIYPRI
AWTSTLDKGD LSLPVASLQI KQNPVELARD LVAKFPASDL IHPPTQLGPH IQFFCKRQPL
TNNVLGRILK EKAAYGTNGN QGLKDPSDPS KGQKKIIIEF SSPNIAKPFH AGHLRSTIIG
GFLANIYTVM GWNVIKMNYL GDWGKQYGLL ANGFKQFGDE EALIKDPINH LFDVYVKINR
QVSDQEGPIK ELKEQIKAKK EKSEDVAELE AQLAKLVDVS EDEKARRYFK SMEDGDPEAL
ALWRKFRDLS IEKYKQTYAR LNIDFDVYSG ESQIKSESMT DAYKVMEEAG VSEKSEGAVI
VDFTKHGAKK LGKAIIVRKD GTPLYLTRDI GAITERDNEY HFDKMIYVVA AQQDLHLAQL
FKVTELMGHK DLASRCQHIN FGMVRGMSTR KGTVKFLDDI LRDVGDKMHE VMKKNEVKYA
QVEDPVKTAD ILGITSVMVQ DMTGKRVNGY EFNLDAMTSF EGDTGPYLQY AHARLCSMTR
KSELDVNELV NANFDLLTEQ HAVDLIRLLA QWPDVLLQTA KTLEPITVLS YLFKMTHMLS
SSYDVLKVIG SEPDVKQARM ALYASARQVL NNGMRVLGLS PVQRM
//
