ID A0A2P6SMY3_ROSCH Unreviewed; 1097 AA.
AC A0A2P6SMY3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=RchiOBHm_Chr1g0376611 {ECO:0000313|EMBL:PRQ60023.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ60023.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ60023.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
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:PRQ60023.1}.
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DR EMBL; PDCK01000039; PRQ60023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6SMY3; -.
DR STRING; 74649.A0A2P6SMY3; -.
DR EnsemblPlants; PRQ60023; PRQ60023; RchiOBHm_Chr1g0376611.
DR Gramene; PRQ60023; PRQ60023; RchiOBHm_Chr1g0376611.
DR OMA; LDTWMDS; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000238479; Chromosome 1.
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:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
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:UP000238479}.
FT DOMAIN 145..766
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 812..952
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 43..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1021..1090
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 53..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 124718 MW; 26E527E2CADC1E68 CRC64;
MLGPYFRVLA KPPSSYQSIG NQIKVAAAPY LLRHFRIRPP LLQSAPAGKA MDAGIEDPEK
KKKKEEKARE KELKKQKALE KAAKFQAQQA NAASKKSEKK SVKRGNEEDE NAADFVDPLT
PVGQKKQMSK QMAKQYSPSA VEKAWYEWWE EVGFFVPDAK SSKPPFVIVF PPPNVTGALH
IGHALTAAIE DTMIRWRRMS GYNALWVPGM DHAGIATQVV VEKKLMRERN LTRHDIGRDE
FVSEVWKWKN NYGGTILKQL RRLGASLDWS RECFTMDEKR SNAVTEAFVR LHKQGLIYRD
NRLVNWDCVL RTAISEIEVD YIDIKERTSL EVPGYKNRVE FGVLTSFAYP LEDNLGEIVV
ATTRVETMLG DTAIAVHPDD DRYKHLHGKH AIHPFNGRRI RIICDAILVD PEFGTGAVKI
TPAHDPNDFN VGKRHNLDFI NVFTDDGKIN QDGGEFAGMP RFKAREEVTE ALKKKGLFKE
ATTNEMRLGI CSRSKDVVEP MIKPQWYVKC SGMAKGALDA AVDDDNRKLD IIPRQYNADW
KRWLENIRDW CVSRQLWWGH RIPAWYAVLD GDKPEDFGSL DDRWVVARNE EEAKALASQR
YEGKEVKLEQ DPDVLDTWFS SGLFPLSVLG WPEDTEDLRA FYPTSVLETG HDIIFFWVSR
MVMLGSTLGG NVPFTKVYLH PMIRDAHGRK MSKSLGNVID PLDVINGVSL EDLHKKLSEG
NLDLREIAIA KEGQKKDFPD GIAECGSDAL HFALVSYTAQ SDKINLDIQR VVGYRQWCNK
LWNAVRFAMS KLGDDYVPLS TVIPDVLPFS CRWILSVLNK AISKTILSLD SYEFSDAATA
VYAWWQYQLC DVFIEAIKPY FAGNNPKFAS ERGFAQDTLW LCLDTGLRLL HPFMPFVTEE
LWQRLPSSKH HNRAASIMIC DYPSIVECWT NERVESEMSL IDSIVRSLRS LSQESRERRP
AFVLCRSMSD REILCRQQLE IETLANLSSL TVISENEAAP TGCAVSVVNE NLSVYLKVLG
SRSAEIDLEK IRKKMEDIKL QQEKITKVMN AAGYKEKVPE KIQKANADKL ESLEKEKLSL
EEASQHMEAQ ISSNKQD
//
