ID C5DTZ2_ZYGRC Unreviewed; 1118 AA.
AC C5DTZ2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=ZYRO0C12474g {ECO:0000313|EMBL:CAR27253.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR27253.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928175; CAR27253.1; -; Genomic_DNA.
DR RefSeq; XP_002496186.1; XM_002496141.1.
DR AlphaFoldDB; C5DTZ2; -.
DR STRING; 559307.C5DTZ2; -.
DR GeneID; 8203405; -.
DR KEGG; zro:ZYRO0C12474g; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; C5DTZ2; -.
DR Proteomes; UP000008536; Chromosome C.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008536}.
FT DOMAIN 171..794
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 839..987
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1049..1113
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 66..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1054..1116
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 73..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 127113 MW; A0AD412FF07C5A8B CRC64;
MHKWFRLVSV KSPFSIYRHF SFNTKSCSLA IASSPLSISR EKKPIQIPVL QTRYFTMSDL
EKLPPVDPKT GEIIINPKKE DGSEKTPKEI EKEKKKAEKL LKFAAKQAKQ NEKKKQAGND
GNSEKKKSKK KEAEPIPEFV DKTVPGEKKV LLSLDDPSLK AYNPANVESS WYSWWEKSGF
FEPEFTADGK IKPEGVFCIP APPPNVTGAL HIGHALTISI QDSLIRFNRM KGKTVLFLPG
FDHAGIATQS VVEKQVWNKE KKTRHDYGRE AFVDKVWDWK TEYHERIKSQ IKKLGASYAW
SREAFTLDPK LSKAVVEAFV RLHDEGIIYR DNRLVNWSVK LNTAISNLEV ENKDVKGRTL
LNVPNYDEKV EFGVLTSLAY PVVDSDEKLI IATTRPETLF GDTGIAVHPD DSRYKHLHGK
FAQHPFLDKK IPIVCDSEAV DMEFGTGAVK ITPAHDQNDY NTGKRHNLEF VNILTDDGLL
NENCGPEWQG MKRFDARKRV IEQLKAKGLF VDQKDNEMTI PTCSRSGDII EPLLKPQWWV
SQSAMAKEAI KVVKEGKITI TPKSSEAEYF HWLENIQDWC ISRQLWWGHR CPVYFIEIEG
QENSKNDDKY WVSGRDIEEA EKKAKAKFPD AKFSLHQDED VLDTWFSSGL WPFSTLGWPE
KTADMENFYP FSMLETGWDI LFFWVSRMIL LGIKMTGSVP FNEVFCHSLV RDAQGRKMSK
SLGNVVDPLD VINGIKLADL HAKLYNGNLD SREVERAKAG QSESYPNGIP QCGTDAMRFA
LCAYTTGGRD INLDIMRVEG YRKFCNKIYQ ATKFALMKLG QDYQPPAKEG LSGNESLVEK
WILHNLSSTA KTVNEAMDKR EFLPATSQIY ELWYLICDVY IENSKYLIQE GTEKEQKSAK
DTLYTLLDNA LRLIHPFMPY ISEEMWQRLP RRAEDSVPTL VKAAYPTFTP EYDNVKAAKD
YDLVLDITKG ARSLLAEYNI LKNGKVFVET NHEESYETAV SQKDSMVSLI KAIDEITVVH
KASEIPEGCV LASVNPEVSV HLLVKGHIDI DAEIEKVQKK LDKATKTRQA IETSISSKDY
ETKASAQVKE ANKARLDSAT AEIEGFDATI ENLKRLKL
//
