ID A0A3P9CQ99_9CICH Unreviewed; 1321 AA.
AC A0A3P9CQ99;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005024525.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005024525.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005024525.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR STRING; 106582.ENSMZEP00005024525; -.
DR Ensembl; ENSMZET00005025328.1; ENSMZEP00005024525.1; ENSMZEG00005018327.1.
DR GeneTree; ENSGT00940000157775; -.
DR Proteomes; UP000265160; LG11.
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; 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: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; SSF46589; tRNA-binding arm; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160}.
FT DOMAIN 126..254
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 262..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1251..1320
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 286..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 149067 MW; 1E568E8020928964 CRC64;
MASVLCRKRR LKPGTRCSFI ASDGHSCGCV CVLTELTSLS VSFKEMTTLY VSPHPDDFRS
LLALLAAEYG PSSRPQIITE DPPASLNARS RPALVLAAAG DGDSLVSGAT AVSWYLAFQG
KRAGLDAKQQ SQVWQWLSFA DNELTPVSCA VVFPLMGVTG VDKKLQQTSR AELMRVLKVL
DQALAPRTYL VGESITLADM AVATAVLLPF KYALEPSDRK AVTNVTRWFT TCINQPQFLK
VLGEIVLCEK MVPVTPKTNA ATNAVNGSPA GDSPGAPANG PPKTEAQLKK EAKKREKLEK
FQQKKEMEAK KKTQPPSEKK AKPEKKELGV ITYNITTPAG EKKDVVSPLP DSYSPQYVEA
AWYPWWEKQG FFKPEYGRKS ISEENAKGIF MMCIPPPNVT GSLHLGHALT NAIQDCLTRW
HRMRGETTLW NPGCDHAGIA TQVVVEKKLM REKGMSRHDL GRENFIREVW KWKNEKGDRI
YHQLKKLGSS LDWDRACFTM DPKLSYAVQE AFIRMHDEGV IYRSKRLVNW SCTLNSAISD
IEVDKKELAG RTLLPVPGYK EKIEFGVLVS FAYKVDGSDE EVIVATTRIE TMLGDTAVAV
HPADARYQHL KGKMVLHPFC DRKMPIVFDD FVDMSFGTGA VKITPAHDHN DYEVGERHNL
AFINILDENG LLINVPPPFL GMKRFEARKA VLQALKDRGQ FKEIKDNPMV VPVCSRSKDI
VEPLLKPQWY VDCRDMGKEA ADAVREGRLK IIPDHHLKTW FNWLDNIKDW CISRQLWWGH
RIPAYFITVN DPSVKPGEDM DGHYWVSGRS EEEAREKAAK RFNVSADKIT LRQDEDVLDT
WFSSGIFPFS IFGWPNENED LQVFYPGTLL ETGHDILFFW VARMVMMGLK LTGKLPFKEV
YLHAVVRDAH GRKMSKSLGN VIDPLDVITG ISLEGLHAQL MDSNLDPVEV ERAQQGQKSD
YPNGIPECGT DALRFALCAY TSQGRDINLD VNRILGYRHF CNKLWNAVKF AMKTLGDNFV
PSEKVQLSGE ESVSDRWILS RLSAAVTLCD AGFKAYDFPT ITTAIYNFWL YELCDIYLES
VKPVFSKAEE DSTSQRQALV CRQTLYTCLE VGLRLLSPLM PFVTEELYQR LPRRKPQSDP
PSICVTSYPT TEEFCWNSEE VDRDMEFIMT IVKTIRSLRA DYNLTKTRAD CYLQCIDSAT
VSLVQKYSLQ IQTLSYSQAV IPLTANQPVP EGCAVAIASD RCTVNLMLKG LIDVEKEVAK
LMTKKGDLEK QMEKLREKMG KNDYKEKVPV KVQEQDAEKL RQSQIELEKV KEAMDNFRKM
I
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