ID A0A194SCP4_RHOGW Unreviewed; 967 AA.
AC A0A194SCP4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=RHOBADRAFT_23546 {ECO:0000313|EMBL:KPV78503.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV78503.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV78503.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV78503.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001624};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; KQ474073; KPV78503.1; -; Genomic_DNA.
DR RefSeq; XP_018274552.1; XM_018412603.1.
DR AlphaFoldDB; A0A194SCP4; -.
DR STRING; 578459.A0A194SCP4; -.
DR GeneID; 28973052; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT DOMAIN 14..639
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 685..834
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 924..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 109502 MW; 5E70FF0AE7DFECC9 CRC64;
MAAGYNPDVV EKAWYSWWRQ CSFFVPALDW SKVNPDKVFV IPAPPPNVTG SLHIGHALAF
GLQDTLIRWR VLLHRMRGYT TLFVPGYDHA GISTQSVVEK RLAKLEGLSR HDLGREKFLE
RCMAWKEEYQ SRITNQIQRL GVSCDWDRVA FTMNPALSKA VAETFVRLHD DGIIYRANRL
VNWCVAMNTT LSNLEVDQKV LTGRTMLNVP GYDLKDKFEF GVITSFAYPL EGSDDKIVIA
TTRPETILGD TAIAVHPDDE RYKHLHGKFA IHPFLGRRIP IITDSIAVDM SFGTGAVKMT
PAHDPNDYEV GMRHQLEFIN ILNDDGTLNS NAGPEFEGMK RFHARVKVVE DMKKKGLYVG
DAENPMSIPV CAKSGDFIES VMKPQWWVSC KSLAEKAIER TRAGELKIRP ATSEGDWYRW
LEGIQDWCIS RQLWWGHRAP AYFVKIEGEE QDSNDFWVTG RNADEAHERA VAKFPGKKFT
LEQDDDVLDT WFSSGLWPFS IQGWPEQTPD LKHFYPSSLL ETGWDILFFW VARMVLLGIY
LTGQVPFNEV FCHAMIRDAH GRKMSKSLGN VIDPIDVIEG ATLEALHAQL RMGNLAAKEV
ELAEKGQKKD FPSGIPQCGT DALRFALANY SSTGRDINLE ILRVEGYRKF CNKLWNATRF
AMLKLEGDFV PTASEKPTGD ESLVEKWILH KLDLASDKVN HALEDRNFMQ ATSEAYSFWL
YEICDVYIEA IKLTTDPAAP DAKARRSAQN TLYTVLDNGL RMLHPFMPFV TEELWQRLPR
RPTDQTKSIM LARFPEKKPE RDFAQEEKEF DLAFGAVRAS RSISTSYGIN SKLQVFFLAR
TPALAATLRA NTDALSVLIK GCAAFRIVES EDELPEGCVG ETVSSELSAF LLLKGVIDAE
AEIAKSQKRL AFAQQALDKL EKQRAAPTYA DKRPADVQQR EGQKVDEWKS EIGELEKAIA
KFEQLKV
//
