ID R0KTZ3_NOSB1 Unreviewed; 909 AA.
AC R0KTZ3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
DE Flags: Fragment;
GN Name=SYVC {ECO:0000313|EMBL:EOB14276.1};
GN ORFNames=NBO_32g0051 {ECO:0000313|EMBL:EOB14276.1};
OS Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS (Pebrine of silkworm).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB14276.1, ECO:0000313|Proteomes:UP000016927};
RN [1] {ECO:0000313|EMBL:EOB14276.1, ECO:0000313|Proteomes:UP000016927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT "Comparative genomics of parasitic silkworm microsporidia reveal an
RT association between genome expansion and host adaptation.";
RL BMC Genomics 14:186-186(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB908940; EOB14276.1; -; Genomic_DNA.
DR AlphaFoldDB; R0KTZ3; -.
DR STRING; 578461.R0KTZ3; -.
DR EnsemblFungi; EOB14276; EOB14276; NBO_32g0051.
DR VEuPathDB; MicrosporidiaDB:NBO_32g0051; -.
DR HOGENOM; CLU_001493_0_2_1; -.
DR OMA; TIMPPIC; -.
DR Proteomes; UP000016927; 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 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:UP000016927}.
FT DOMAIN 51..677
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 726..869
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB14276.1"
FT NON_TER 909
FT /evidence="ECO:0000313|EMBL:EOB14276.1"
SQ SEQUENCE 909 AA; 104645 MW; BA7809086B910F01 CRC64;
KMDRKQLKEE KKRQKMEKFL SKKTETLSVS KKKVIISLGD GYNPSEIESK WFKIWEENGY
FKPSYIVKDR ERQSNELTLE SSPEQSSLPF VITMPPPNVT GSLHIGHSMM IAIQDCLARY
KRMKGFEVLY LPGTDHAGIA TQSVVSKQLA KEGKEVDREG FLKAAWEWKN KYGERIFEQF
KRLGTSADFS KAKFTLDQGM SEAVIEAFVR LYEKGLIYRE AKIVNWCAKL KTTLSDLEVN
HEIVKPNTFI KVDGGNYEFG VIYQIKYLTS DGNFVEIQTT RPETIVGDVA LCANPKDERY
NKMKDLTFIN PLTGKEIPLI FDEHSVMDFG TGLLKITPAH DPVDFEIGKR HGLEKLIIFD
NENKICVEGP FFGLKRFEAR IKTIEFLKDK GLFVKKVPYE QTLPICSRSG DIIEPTIKEQ
WWCRCQEMGE KALNAVKNGL IEIHPPEAGK IWSRWLENIR DWCLSRQLWW GHRIPAYKSP
NGEWCIGRTK EEAISNYYKE RKCVNKQEDT FLYEESDFVQ DEDVLDTWFS SGLWPFATMG
WPKDTPDLQK YFPGSILETG SDILFFWVAR MVMMSLELTG FIPFKQILLH GIVRDAHGRK
MSKSLGNVID PLFVIDGSSL ENLIEVMKSG NLALSEIKLA EKNLKKDFAH GIAKCGADAL
RFTLLSYTLG MKDINLDISR VEGYRRLCNK LWNANKFCKM ISGDKNLSIY SKTDLKFLSN
YSSLIKWILI GRNKAVKNSI LNLEKFNFMM ATQTIHQFFL YDFCDVFIEV VKNVKEESEK
GLNENLNISA ANESSSVIYS KLLRTIFLDI LKILHPYLPF ITEELYSEYV SDTIMYSAYP
EEVEGMDEET TFGRVLDVIK ILRTKKAKII NILEGTLEES DLIYLRSLVK KTEINLVDDL
KGEVHEDEG
//
