ID Q2GRB7_CHAGB Unreviewed; 610 AA.
AC Q2GRB7;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=CHGG_09487 {ECO:0000313|EMBL:EAQ85473.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ85473.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408034; EAQ85473.1; -; Genomic_DNA.
DR RefSeq; XP_001227414.1; XM_001227413.1.
DR AlphaFoldDB; Q2GRB7; -.
DR STRING; 306901.Q2GRB7; -.
DR GeneID; 4395915; -.
DR VEuPathDB; FungiDB:CHGG_09487; -.
DR eggNOG; KOG1075; Eukaryota.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_447580_0_0_1; -.
DR InParanoid; Q2GRB7; -.
DR OrthoDB; 2642889at2759; -.
DR Proteomes; UP000001056; 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 Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR000477; RT_dom.
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; PF00078; RVT_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 2.
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; 2.
DR PROSITE; PS50878; RT_POL; 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:UP000001056};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..610
FT /note="arginine--tRNA ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004208374"
FT DOMAIN 476..610
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
SQ SEQUENCE 610 AA; 66213 MW; 05ECCEC5293166F2 CRC64;
MSRLTLGGLT TLLSGIGAGP IPSIPGDYPV AHPLSRPIDI YCAYLADILA RLAGCEAAVA
YESLQVPGAP ANGDLVLPVP RLRIKGKKSA EQCAELVAAF PKNHPLFREP GAVGIHLPFF
FAPLSLPRLI LPYIFQRQHS YGSDLDAGLR DHALPTQGRK KVVLEFSSPN IAKEFHTGHL
RSTIIGAFIA NLYKTMGWDV VKHGPKGLGV AVVRGRTGTT TYLLRDFAAI LERDEKYAFD
KMIYVVSTEQ DLYFRRVFRT LELMGRSDLA VRLQHVNFGK VLGMYSRLGN VQLLSDILDQ
SREAMHGVMR QNEVKCSQVE DSDAVAEKCP DVTAMTLKTL EPSTILTYLC RLTHQLSSCY
DVLQVVGTEG GRAVVLARAA LDEGARLVLE TGMRLLGLSP VESLPGNTQG SKSIPTFLNN
WDPGFDVSQA VTPAEITRAI GGASPWKAPG EDLLPIGLLK ACGAPLAEVL AVLATRCLEL
GWFPNRFKRA KTVVLPKPGK APPVYQTPGG YTPIALLPTL GKVIESVVAT KVTLAAEANG
LLPDEQMGNR AHRSTELAVR LVVAQVQEAW RQKGAASLLQ LDISGAFDTV NHTRLLATLR
EMGYPRWLVL
//
