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Database: UniProt
Entry: K0KMQ8_WICCF
LinkDB: K0KMQ8_WICCF
Original site: K0KMQ8_WICCF 
ID   K0KMQ8_WICCF            Unreviewed;      1061 AA.
AC   K0KMQ8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
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   Name=VAS1 {ECO:0000313|EMBL:CCH42403.1};
GN   ORFNames=BN7_1948 {ECO:0000313|EMBL:CCH42403.1};
OS   Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS   3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH42403.1, ECO:0000313|Proteomes:UP000009328};
RN   [1] {ECO:0000313|EMBL:CCH42403.1, ECO:0000313|Proteomes:UP000009328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC   Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX   PubMed=23193139; DOI=10.1128/EC.00258-12;
RA   Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA   Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA   Tauch A., Kohler T., Brinkrolf K.;
RT   "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL   Eukaryot. Cell 11:1582-1583(2012).
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   -!- 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:CCH42403.1}.
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DR   EMBL; CAIF01000043; CCH42403.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0KMQ8; -.
DR   STRING; 1206466.K0KMQ8; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   HOGENOM; CLU_001493_0_1_1; -.
DR   InParanoid; K0KMQ8; -.
DR   Proteomes; UP000009328; 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; IPR010978; tRNA-bd_arm.
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; 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:UP000009328}.
FT   DOMAIN          116..737
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          782..929
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          997..1059
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        28..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1061 AA;  119740 MW;  D61F0CFA5FA36F78 CRC64;
     MSDKIENPAQ PEAAAAQATQ AAPAEGAPKV KTEKELEKER KKAEKLAKFK AKEAKKAEDK
     KKAEANKESK PKKEKKVVEP IPEFVDKTVA GEKKILVNLE DPSLKAYDPK NVESSWYEWW
     VKEGLFEPEF AENGEFKPEG VFCIPAPPPN VTGALHIGHA LTVSIQDTLI RYNRMKGKTV
     LFLPGFDHAG IATQSVVEKQ LARDGISRHT LGREAFIKKV WEWKEVYHAK IKSQFTRLGA
     SYDWNYERFT LDDNLSKSVT EAFVKLHQEG VIYRASRLIN WSVHLNTALS NLEVDNKEIP
     GKTLLSVPGY DEKVEFGVLT SFAYPVENSD EKLVVATTRP ETLFGDTGVA VHPEDPRYKH
     LHGKFVIHPF LGTKIPIVTD AEAVDMEFGT GAVKITPGHD TNDYNTGKRN NLEIVNILTD
     DGVLNENAGE WAGIKRFDAR KKVIEALKEK GLFVEQTENP MTIPICSRSG DVIEPLLKPQ
     WWVSQKDMAA EAIKAVRNGD ITITPKSSEA EYFHWLENIQ DWCISRQLWW GHRCPVYFVQ
     IEGETNDEND DNYWVSGRTL QEAEEQAAQR FAGKTYTLRQ DEDVLDTWFS SGLWPFSTLG
     WPEKTNDLSK FYPWSMLETG WDILFFWVSR MILLGLKMTG EIPFKEVFCH SLVRDAQGRK
     MSKSLGNVVD PLDVITGISL ENLHSKLLGG NLAAKEVEKA KAGQKESYPN GIPQCGTDAL
     RFALCAYTTG GRDINLDILR VEGYRKFCNK IYQATKFALL RLGDDYKPPA TEGLTGQESL
     VEKWILHKLN ETSKIVNESF EKRDFLTSTS AIYEYWYQVC DVYIENSKSL ILEGSEAERK
     SARDTLYTTI DGALRLIHPF MPFLSEEMWQ RLPRRGSDNT KSIVKAAYPT YNKEFDNAKA
     SADYETILDV TKEARSLLAQ YNIIKNGKVF VEASNAEQFE TITAQKESIV ALIKAIDSIE
     VVKSVEEIPQ GVVLQAVSPE INVHLLVKGH VDIDAEISKA QKKLDKVQKS KQSIEKIVNS
     KDYASKANQE AQEQNKTKLE NAAAEIEGFE QTIANLERLK L
//
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