ID A0A3Q0S4E2_AMPCI Unreviewed; 1250 AA.
AC A0A3Q0S4E2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000017677.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000017677.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q0S4E2; -.
DR STRING; 61819.ENSACIP00000017677; -.
DR Ensembl; ENSACIT00000018153.1; ENSACIP00000017677.1; ENSACIG00000013752.1.
DR GeneTree; ENSGT00940000157775; -.
DR OMA; LDTWMDS; -.
DR Proteomes; UP000261340; Unplaced.
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; 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 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:SF118; 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 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}.
FT DOMAIN 81..204
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 203..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1180..1249
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 213..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 141682 MW; 88623E74B9726D7A CRC64;
MTTLYVTPHP DDFRSLLALI AAEYGPSSRP QVITEDPPAS LNARSRPALV LGDVGEGDSV
VSGATAVSWY LAFQGKRAGL DAKQQSQVWQ WLSFADNELT PVSCAVVFPL IGLQQSSRAE
LMRVLKVLDQ ALAPRTYLVG ESITLADMAV AIAVLLPFKY VRALEPSDRE AVTNVTRWFT
TLINQPQFLK VLGKITLCEK MVPVTPKTSP PKTEAQLKKE AKKREKLEKF QQKKEMEAKK
KTQPPSEKKA KPEKKELGVI SYNIPTPAGE KKDVVSPLPD SYSPQYVEAA WYPWWEKQGF
FKPEYGRKSI SEQNPQGIFM MCIPPPNVTG SLHLGHALTN AIQDCLTRWH RMRGETTLWN
PGCDHAGIAT QVVVEKKMMR EKGMSRHDLG RENFIQEVWK WKNEKGDRIY HQLKKLGSSL
DWDRACFTMD SKLSYAVQEA FIRMHDEGVI YRSKRLVNWS CTLNSAISDI EVDKKELTGR
TLLPVPGYKE KIEFGVLVSF AYKVDGSDEE VIVATTRIET MLGDTGVAVH PADPRYQHLK
GKMVLHPFCD RKMPVVFDDF VDMSFGTGAV KITPAHDHND YEVGERHSLP FINILDENGL
LINVPPPFLG MKRFEARKAV LQALKDRGQF KEIKDNPMVV PVCSRSKDIV EPLLKPQWYV
NCRDMGKEAA DAVREGRLKI IPDHHLKTWF NWLDNIKDWC ISRQLWWGHR IPAYFVTVSD
PSVKPGEDMD GHYWVSGRSE EEAREKAAKR FNVSSDKITL KQDEDVLDTW FSSGIFPFSI
FGWPNESEDL KVFYPGTLLE TGHDILFFWV ARMVMMGLKL TGKLPFKEVY LHAVVRDAHG
RKMSKSLGNV IDPLDVITGI SLEGLHAQLT DSNLDPVEVE KAKQGQKSDY PNGIPECGTD
ALRFALCAYT SQGRDINLDV NRILGYRHFC NKLWNAVKFA MKTLGDNFVP SEKAQLSGEE
SVSDRWILSR LSAAVALCDA GFKVYDFPTI TTAIYNFWLY ELCDVYLESV KPVFSKAEED
STSQRPALVC RQTLYTCLEV GLRLLSPLMP FVTEELYQRL PRRNPQSDPP SICVTSYPDS
QEFCWGSEEV DRDMEFIMTI VKTIRSLRAD YNLTKTRADC YLQCIDSATV SLVQKYSLQI
QTLSYSQAVI PLTANQPVPE GCAVAIASDR CTVNLMLKGL IDVEKEVAKL ITKKGDLEKQ
MEKLREKMAK NDYKEKVPVK VQEQDAEKLR QSQTELEKVT EAMDNFRKMM
//
