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Database: UniProt
Entry: G9KX46_MUSPF
LinkDB: G9KX46_MUSPF
Original site: G9KX46_MUSPF 
ID   G9KX46_MUSPF            Unreviewed;      1264 AA.
AC   G9KX46;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|ARBA:ARBA00024407};
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=VARS1 {ECO:0000313|Ensembl:ENSMPUP00000010733.1,
GN   ECO:0000313|RefSeq:XP_004780995.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|EMBL:AES09475.1};
RN   [1] {ECO:0000313|EMBL:AES09475.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lungs {ECO:0000313|EMBL:AES09475.1};
RX   PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA   Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA   Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA   Farooqui A., Kelvin D.J.;
RT   "Sequencing, annotation, and characterization of the influenza ferret
RT   infectome.";
RL   J. Virol. 87:1957-1966(2013).
RN   [2] {ECO:0000313|Ensembl:ENSMPUP00000010733.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_004780995.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004780995.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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; AEYP01101422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JP020877; AES09475.1; -; mRNA.
DR   RefSeq; XP_004780995.1; XM_004780938.3.
DR   STRING; 9669.ENSMPUP00000010733; -.
DR   Ensembl; ENSMPUT00000010912.1; ENSMPUP00000010733.1; ENSMPUG00000010821.1.
DR   GeneID; 101671544; -.
DR   CTD; 7407; -.
DR   eggNOG; KOG0432; Eukaryota.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000157775; -.
DR   HOGENOM; CLU_001493_0_1_1; -.
DR   OMA; LDTWMDS; -.
DR   OrthoDB; 5473263at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; cd10294; GST_C_ValRS_N; 1.
DR   CDD; cd00817; ValRS_core; 1.
DR   Gene3D; 1.20.1050.10; -; 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; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004046; GST_C.
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; 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:SF115; VALINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00043; GST_C; 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; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   2: Evidence at transcript level;
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:UP000000715}.
FT   DOMAIN          89..224
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          218..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1201..1263
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        233..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AES09475.1"
FT   NON_TER         1264
FT                   /evidence="ECO:0000313|EMBL:AES09475.1"
SQ   SEQUENCE   1264 AA;  140330 MW;  DDDA3426177ACF0B CRC64;
     MSILYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRA PFPPPRLPAL
     EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG
     LRTSTQDPQA ALGALGRALS PLEEWLRLHT YLAGEAPTLA DLAAVTALLL PFRYVLDPSA
     RRIWGNVTRW FITCVQQPEF RAVLGEVVLY SGARPLSQQP GPEVLVPPKT ATQLKKEAKK
     REKLEKFQQK QKTQQQQPPP AEKKPKPEKR GKRDPGVITY DLPTPAGEKK DVSGTMPDSY
     SPQYVEAAWY PWWEQQGFFK PEYGRSSVSA PNPRGIFMMC IPPPNVTGSL HLGHALTNAI
     QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ GLSRHQLGRE AFLQEVWKWK
     EEKGDRIYHQ LKKLGSSLDW NRACFTMDPK LSTAVTEAFV RLHEEGVIYR STRLVNWSCT
     LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KIQGSDSDEE VVVATTRIET
     MLGDVAVAVH PKDPRYQNLK GRSVIHPFLS RSLPIVFDDF VDMEFGTGAV KITPAHDQND
     YEVGQRHGLE AVSIMDSRGA LVNVPPPFLG LPRFEARKAV LAALKERGLF RGVEDNPMVV
     PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH TWMDNIRDWC
     ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD ERYWVSGRSE AEAREKAAKE FGVSPDKISL
     QQDEDVLDTW FSSGLFPFSI FGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL
     TGKLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIHGV SLQGLHDQLL SSNLDPSEVE
     KAKEGQKADF PAGIPECGTD ALRFGLCAYT SQGRDINLDV NRILGYRHFC NKLWNATKFA
     LRGLGKGFVP SPTSKPGGHE SLVDRWIRSR LTEAVRLSNQ GFQAYDFSAV TTAQYSFWLY
     ELCDVYLECL KPVLNGVDQV VAECARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRTP
     QAPPSLCITP YPEPSECSWK DPDAEAAMEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD
     EATGALASAV SGYVQALASA GVVAVLALGA PVPQGCAVAL ASDRCSVHLQ LQGLVDPARE
     LGKLQAKRSE AQRQAQRLRE RRAASGYPSK VPLDVQEADR TKLQQTEAEL RKVDEAIALF
     QKML
//
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