ID C6HK09_AJECH Unreviewed; 898 AA.
AC C6HK09;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=HCDG_06540 {ECO:0000313|EMBL:EER39435.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER39435.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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}.
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DR EMBL; GG692429; EER39435.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HK09; -.
DR STRING; 544712.C6HK09; -.
DR VEuPathDB; FungiDB:HCDG_06540; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_006406_1_0_1; -.
DR OMA; ASILHIQ; -.
DR Proteomes; UP000002624; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT DOMAIN 35..116
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 529..618
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 243..277
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 898 AA; 99818 MW; E5903D9590A99259 CRC64;
MAADSAPTVA QISIHSTTSE VSKYPNCYPA VNPVDTYRVH VAELVGAALG IDSLSVYPKI
QWTNSLDKGD LVLAVPALQI KGKKPAEVTA QIVENLPPSD LIGTPVVSGT HIQFYFKPEP
LTKTVISSIL KNRATYGTNA NVGLRDPADP SKGKKKIIVE FSSPNIAKPF HAGHLRSTII
GGFLANLYTV MGWDVIKMNY LGDWGKQYGL LANGYEKYGN EEELIKDPIN HLFDVYVKIN
KDVAEQEVPI KELKEKIKQK KENSEDTTEL EKELQAKVDV SYDEKARRYF KSMEDGDEGA
LVLWRRFRDL SIEKYKETYA RLNIDFDRYS GESQVKPESL AKAYEAMAKT GVSEESEGAV
IVDFAKHGAK KLGKAIVVRK DGTPLYLTRD IAAIVERDEE FHFDKMLYVV AAQQDLHLAQ
LFKVTELVGR KDLANRCQHV NFGMVRGMST RKGTVKFLND ILKDVGEKMH EVMKKNTAKY
EQVANPEQTA DILGITSVMV QDMSGKRING YEFNLDDMTS FEGDTGPYLQ YAHARLCSMT
RKAEIDPSEL SSANLSLLTE PHAIDLIRLL ASWPDVVFNT TKTLEPTTVL TYLFRMTHVL
SSGYDVLKVV GSEPELKKAQ CNPPISSAHS WVAISLSEKR KTEAKKCKQT KKHKSVFPPS
RGYQSPRIRS GHVWGTPFLK SCPWVWLILV GTWLDTGHST QALESRKDNV SSGKPLAKRG
AGERILCQPA SQPAKNSGHE KMRNVGECER MLGCRLPGPL VSFLQQFSAI FQLFVKLPCP
PPPTIAAQWR ARSPIPAGCW GVSAGMMTSN SSSDFALREL DLAFLAALGE SHDSSRIPVG
WDGGRGKLKW ASTLPQPFFS LLDASILHIQ LPVIRDLRSK IHSTIQVLVL FMLSSMLT
//
