ID A0A066Y0Y7_COLSU Unreviewed; 542 AA.
AC A0A066Y0Y7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
DE Flags: Fragment;
GN ORFNames=CSUB01_09830 {ECO:0000313|EMBL:KDN71890.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71890.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(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 -!- 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:KDN71890.1}.
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DR EMBL; JMSE01000101; KDN71890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066Y0Y7; -.
DR STRING; 1173701.A0A066Y0Y7; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_006406_6_2_1; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
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; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 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; 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:UP000027238}.
FT DOMAIN 426..542
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KDN71890.1"
SQ SEQUENCE 542 AA; 61229 MW; D6EB78B9156BEB69 CRC64;
FPESPLIEKP VSLQNGSFLQ FWFKTGPLSQ LLIPQVRNRG QTFGKNPNNG LKNPEDPSQG
KKKIIVEFSS PNIAKPFHAG HLRSTIIGGF IANLYDGAGW DVTRINYLGD WGKQYGLLAL
GFERFGSEEA LKEDPINHLY EVYVKINAAM SDEKEQITAK EQAGEDVTAL KDNSLDEQAR
KYFKAMVAGD EAAVAQWKRF RDLSITRYKE TYARLNIHFD EYSGESQVSE QDMEAAAKKL
ADMNISEESE GAVIIDFSKH IPGKAGKSLE RPIIRKKDGT ALYLTRDISE LLHREKKYNF
DHMIYVVASQ QDLHLKQLFK IIELMGYPET AKKCQHINFG MVLGMSTRKG TVKFLDDILR
DVGDKMHEVM KKNEAKYSQV ENPEATADIL GISSVMVQDM SGKRINNYKF DMDTMTSFEG
DTGPYLQYAH ARLCSIFRKA GIPEEDVVKA DLSLLTEKHA IELIRVVSQY PDVVQNTLKT
LEPTTVLTYL FRLTHVVSSS YDVLRIVGSE PEIQKARLAL YSSARTVLYN GMRLLGLSPV
ER
//
