ID A0A0D0BLN1_9AGAR Unreviewed; 963 AA.
AC A0A0D0BLN1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=GYMLUDRAFT_205313 {ECO:0000313|EMBL:KIK55696.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK55696.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK55696.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK55696.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KN834804; KIK55696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BLN1; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000053593; 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; 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; 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:UP000053593}.
FT DOMAIN 14..637
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 683..829
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 963 AA; 108997 MW; C133B4B283A2D27B CRC64;
MANSYNPIAV ESAWYDWWNA QGFFAPQLTE DGKVRPEGLF VIPAPPPNVT GNLHIGHALT
TAIQDGLIRW NRMLGKTTLF IPGFDHAGIS TQSVVEKRLF KSSGKTRHDL GREKFVDTVM
DWKNEYQARI TNQLTRLGGS YDWERTAFTM NPSLSKAVIE NFCRLHEDGI LYRANRLVNW
CVRLNTTLSN LEVEQKQLTG RTLLNVPGYD AKEKFEFGVI TSFAYPIEGS DEKLVVATTR
PETMLGDTAI AVHPDDTRYK HLHGKFAVHP FVDRQLRIIP DTMVDMEFGT GAVKITPAHD
PNDYEVGVRH KLEFINILND DGTFNANAGE TFAGMKRFHA RVAVVKALQE KGLYIEAKDN
PMQIPICSKS GDIIEPILKP QWWVNCKPLA EEAIKRTRAG ELEINPKQSE NEWYRWLEGI
QDWCVSRQLW WGHRCPAYFV DIEGQEQDRN EGKNWVVGRD IAQATERAAS LAGGAKFTLH
QDEDVLDTWF SSALWPFSIL GWPDNTSDLQ TFYPTSLLET GWDILFFWVA RMVMLGLKLT
DQMPFKEVYC HAMIRDAHGR KMSKSLGNVI DPIDVIQGLE LEKLHEKLNE GNLDDKEIQK
AKAGQKKDFP KGIPQCGTDA LRFALCAYSA GGRDINLEIL RVEGYRKFCN KVFNATKFAM
LKLEESFVPE PIAKPTGNES LVEQWIFHKL NVAATEVNAH LAERNFMLAT TDVHNFWLYE
LCDVYIEAMK PMTDESASAA TRQSAQQTLY TCLDYGLRLL HPFMPFVTEE LWQRLPRRPN
DSTPSIMVSR FPVNDPSFVF KEADKQFDLV FNVLRAGRSL AASYSLQSNI QFFIHAKTEE
EASLFESQIP TIVTLTKGCT GATVVRDTKD IPAGCGSAVV TSTVVIHTLV RGNVDLDVEI
AKCEKKLDVV RMNLQKIVKQ ESQADYATTV PENVRLANDE KRRTLEAEIA TLESSKAMFA
DLK
//
