ID W9WND6_9EURO Unreviewed; 1055 AA.
AC W9WND6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=A1O7_04051 {ECO:0000313|EMBL:EXJ59904.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ59904.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ59904.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ59904.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) 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}.
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:EXJ59904.1}.
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DR EMBL; AMGW01000003; EXJ59904.1; -; Genomic_DNA.
DR RefSeq; XP_007756257.1; XM_007758067.1.
DR AlphaFoldDB; W9WND6; -.
DR STRING; 1182544.W9WND6; -.
DR GeneID; 19178642; -.
DR VEuPathDB; FungiDB:A1O7_04051; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_010126_0_0_1; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000019473; 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; 1.
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; 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; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000019473}.
FT DOMAIN 543..674
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 613..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 114727 MW; 031BD8B5E9E07998 CRC64;
MATLDADSLQ VLLDGLGVDD TGRSFPAADV LTRPLDIYRT HLAQVLVKLT DCEPQLAYDS
IQEPNDYGDL EVVIPRLRLK GSDPKELALN LAEKFPETPL FDQPFEDGIH VRLYISPETL
ARILLPYILD RGKFYGSCLF PGLTSGDVHR GAGRRVIVDF SSPNLGKEFD GTHLRSTVIG
ASIASLYEGM GWDVRRLNFL GDWGKHIGLL AVGWHRFGSD ELLEEEPLRH LLDVYAKIDE
LSKAEASANQ ENNTEVDTAG EAPLTENVPI STQLDNAFKK MEDGDADAVA LWKRLREACV
TRYADLYAEL NINFDDYSGE SEVSKATMSE VEAILTENGV YEDSNGAWII DFKKHGAKGL
PTVTARHPNG TTSYLLRDVG AVLERRKKYN FDKMIYVVSA KQDVHFQQLF RTLELMGDEY
HNLAQSLQHV SFGPVRGLSP QSASSGLLLG DILTQCQEVM QESLKAEGND DFFQSYGING
DGALTDASEF ARLALISQEL STKRSATLNF TLGTDEKIGA LADNYPGLRV QRWLDNLRSK
AKLQGGEARR SLEHEGLDYT LFTEEESYSY ADMLKLLARF PICVKHAFDK LEPAIILSYL
VQVIDMLPSV WDEEENNPHS EDTGIEPDNE GEGSSSAVRP ARNHDALRTI FCECVRTVVE
NGMNLIGLVP IKERKRESLE VSESTPAVLP EEVSEGAPPM VQSQEAGTEQ APTVRPQGNC
GEPSAPAMPQ EVNEELTPTA NPQDNHEATD VAEVHVAIEE LALPTVPPEL IDEVTEDAAE
VPAATDSSLP KEVDAVADPT GVLQGVNEET GPAVLQENSD ESADVGQLQE SNEETTLPAL
PKVTEQTTLP AFVPEDNDGA TEVALAGEIA EVANPWITPQ ESRGDDAPMT ISQVINAEAA
VPAMPQDRED PGSTAVGQEV NEAAPVAIPQ DINEDAGPLP MPVEVIVEAA VPEEINDAAS
AGVSKGDNED PLLSAISEEA HEPIGTPQPV NEDLPAPIPE ETNVEAISTS IPSRANATES
LDTLQGQNEE NSAPEMKEVD VEPTTTASPE DEGRR
//
