ID   A0A3Q2ZDI4_KRYMA        Unreviewed;      1101 AA.
AC   A0A3Q2ZDI4;
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:ARBA00013169};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000001751.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000001751.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q2ZDI4; -.
DR   STRING; 37003.ENSKMAP00000001751; -.
DR   Ensembl; ENSKMAT00000001797.1; ENSKMAP00000001751.1; ENSKMAG00000001393.1.
DR   GeneTree; ENSGT00940000159890; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 2.
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:SF116; 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   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:UP000264800}.
FT   DOMAIN          109..729
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          776..944
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1101 AA;  125411 MW;  7D5D2E7A92026732 CRC64;
     MWRAGYSPSL RMPGKMAARL CSNKPPGAQS PVSSQLSSSP RPQAEKQRRR REREMAILSK
     QHTSAGEETV NWSEKPKIVY TAQTPPGTKK DTSLPFPSSY SPEYVESCWY QWWEKEGFFS
     PEQHERLSHG VDQTFSLCIP PPNVTGTLHV GHALTVAVQD ALARWKRMQG YRVLWVPGCD
     HAGIATQTVV ERRLLRDQGK HRQDFTREEF LQEVWKWKNE KGEEIYHQLR KLGASLDWSR
     ACFTMDPGFS RAVTAAFVRL CDSDLIYRSE GLVNWSCALQ SAISDIEVDS VEVSGQTMLS
     VPGYENKVEF GALYTFAYPV EGHDGRVAVS TTRPETMLGD VAVAVHPDDP RYQSFHGKQC
     RHPFTNRLIP VITSTTVDME LGTGAVKVTP AHDHKDFLLS RRHTLPHVSV ILGDGTMAPS
     CGRWLEGKKR FDARQLVLDA LAEKKLFVGK QNHPMTLPVC SRSGDVIEPL LKKQWFVRCG
     KMAEKAIQAV EDGQLELIPQ HYSKTWKNWM SSISDWCISR QLWWGHQIPA YQVELPESTT
     RPEEQWVWGH SLDEARQRAA VKYGVKPEDV TLKRDPDVLD TWFSSGLFPF AMFGWPEQTS
     DLQRFYPNSI LETGSDLIFF WVARMVMLGT ELTGQLPFRQ VLFHSLVRDK YGRKMSKSLG
     NVIDPLDVIH GVSLQRLQEK VKEGNFDRRE QLVAMEAQRK DFPKGIPQCG TDALRFALCS
     HRIQGDDISL SVAQVLSCRH FCNKMWQTLR FTLGVLGENT QPLGTIEETT PLGSMERWIC
     SRLYSTVAQC EQAFDAYELH AVTSALHSFW LHSLCDVYIE YVKPVLLRED EGAEVQADAD
     DSDTTTVRQV ARTVLYHCVS LSLALLSPFM PFITEELWQR LQPFRPRPPG APTPTSLCLQ
     PYPRSTHLAH WHFPEEEKDF LMVQEVIRVA RSLRTQCGLR KEKPVMWAVC SPSQAQVLLH
     FRSAVWTLSR ISSLQLHCPD RPDWLPSVQS GPPPKESLVG LVDHTCQLHL YNQSGVNVDK
     QILQLSQRRD RLVPKLEKIL RRLQGSNDSA NVPDHDRQQM EIKVSTEQEM FDSLLKVFKD
     YSLHQGGYVF SDICLSVDMI T
//