ID A0A101XHI7_9CREN Unreviewed; 651 AA.
AC A0A101XHI7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00020262};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=AT710_06340 {ECO:0000313|EMBL:KUO91541.1};
OS Thermocladium sp. ECH_B.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermocladium.
OX NCBI_TaxID=1714261 {ECO:0000313|EMBL:KUO91541.1, ECO:0000313|Proteomes:UP000054381};
RN [1] {ECO:0000313|EMBL:KUO91541.1, ECO:0000313|Proteomes:UP000054381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO91541.1}.
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DR EMBL; LOBW01000044; KUO91541.1; -; Genomic_DNA.
DR STRING; 1714261.AT710_06340; -.
DR Proteomes; UP000054381; 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 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 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|RuleBase:RU363038};
KW Ligase {ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038}.
FT DOMAIN 520..626
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 651 AA; 73554 MW; 7E2F1E4A1574E577 CRC64;
MSYDPEGQVE DEFRGIINEL GAMINEDLSG LEPSRAREGF GFMAVPLHNY IKKNPNILNV
IESLKPRGLI KGIKLINGFL NIDIDYIKYA ELVINSILSN GQRYGWSKQC RSDKIVIEHT
SANPIHQLHT GHGRNMIIGD TLSRLLRFCG GSISTRFYVD DCGPQVMYMA IGYHSVKDLV
NQRIMSGEKP DKVVGAIYSI TYAIGEIQRL TEAEKLAEKD EDKRKIIAER DEWVGVLGKW
STQDQELVNS LASSLGNIDV TEEANRWVRE YEQGNPEIRS KVREGISMVF KGFMETFNEF
GISFDDFDWE SEIALDTGLA KSLVDKLALI GKEYVEKQEG AITIDVGKYA SDHGLFNELS
LPGFLPKAML TRRDGSTLYL TRDLAYAAWC LDKCSPSRVI RVIGSEQTHP XAQLRVLLHM
LGYDASRIMH YSYEMVNMPG AKMSSRRGRM IAMDDLLEEA EERVWKIVEN RLGTEEARKV
VKAVAVGAIR FSFLSISPLK VLEFNWDKLL DLKQNSGPFI QYSYVRASSI LEKAGKPQIS
KATPPSSLNN DEIKLIKDLG GLPKAIAEVS INLRLENLID YVNKMAMDFN VFYERNPVIN
AEPELRDFRL ALVHAFRIAL GNIMNILVNP NNRSHVKIND YFYNSRSPSL S
//
