ID A0A1B9I9I6_9TREE Unreviewed; 1084 AA.
AC A0A1B9I9I6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=I206_01505 {ECO:0000313|EMBL:OCF52219.1};
OS Kwoniella pini CBS 10737.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF52219.1, ECO:0000313|Proteomes:UP000094020};
RN [1] {ECO:0000313|EMBL:OCF52219.1, ECO:0000313|Proteomes:UP000094020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF52219.1,
RC ECO:0000313|Proteomes:UP000094020};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000094020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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}.
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; KI894008; OCF52219.1; -; Genomic_DNA.
DR RefSeq; XP_019013438.1; XM_019153277.1.
DR AlphaFoldDB; A0A1B9I9I6; -.
DR STRING; 1296096.A0A1B9I9I6; -.
DR GeneID; 30169874; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000094020; 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 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:UP000094020}.
FT DOMAIN 119..743
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 798..949
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1021..1083
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 122545 MW; 7D63C00211B7EE8D CRC64;
MSSEERKVAP SAELLPVEQA NPAEGGAAAL APEAPAEGVK EITKSAAKKE AKRLEKLAQK
AAKGPTVAQG PKKDKAEKKE KKAEAPVEEW VNTTPKGEKK DVSGNLPAGY DPIQVEAAHY
DWWKSRGFFK PRYDADGKPL EKGTFCITLP PPNVTGNLHI GHALTISIQD ALIRWKRMQG
HTVLYLPGYD HAGIATQAVV EQRLVKTEGH SRHYYGREKF LEKVWEWKDQ YQAKITNQME
RLGGSYDWDK VAFTMNESLS KAVQETFCIM HEKGLLYRAN RLVNWCVYLN TSLSNLEVDQ
MALTGRTLLN VKGYEAKEKF EFGVITSFAY PIENSDERII VATTRPETML GDTAVAVHPD
DPRYKHLHGK FVIHPFNGRR IPIITDAITV DMEFGTGAVK ITPAHDPNDF ECGQRNNLEF
ISLMNDDGTY NENAAPYQGK KRFHIRNEII AALKEKGLFV EQKDNEMQIP ICSRSGDVVE
QILKPQWWIS CKPMAEEALK RTRAGELEIK PKSSAGDWIR WMENMQDWCI SRQLWWGHRC
PAYLIKYDGE TPDTADDKNW IVARSAEEAE AKAKEQANGR KYTLEQDGDV LDTWFSSGLW
PFSTMGWPEK TADLEHFYPN SVLETGWDIL FFWVARMVFF GNALTGKMPF KEVYCHPMIR
DAYGRKMSKS LGNVIDPLDV ITGQNLQKLH NDLRLGNLPE KEIVKAEEGQ KKLFPKGMPQ
CGTDALRFTL CNYTSGGRDI NMDIGRVEGY RKFCNKLWNA TKFCLFRMDL VDLNGVRQQS
TFVPNASPLP TGQEGLVEKW LFHKYNIASA AISKSLEARE FADATNTAYQ YFLNDLCDVF
IEATKPLFES NASEATRLSA QNTLYTCLEG GLKLLHPFMP YVTEDLWQRL PRRQGDECES
IMLASFPEYI SQQEFPQAAA EFDTVVDCIK AARSIVGLYN LPTNADLKRY ILVIVQAKNQ
QQRQLLESQE PIIIGLTKGC GTAKFISDDS EVPKGCGTEF VTSDINVHIP VAGKINASAE
IDKLQKKEAL AQSNRNKIQK LTEQPNYQTT LKEEVRISNS EKLSSLESEI ETLRLSIERF
KSLL
//
