ID B8PKQ0_POSPM Unreviewed; 838 AA.
AC B8PKQ0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=POSPLDRAFT_97570 {ECO:0000313|EMBL:EED78544.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED78544.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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DR EMBL; EQ966432; EED78544.1; -; Genomic_DNA.
DR RefSeq; XP_002476252.1; XM_002476207.1.
DR AlphaFoldDB; B8PKQ0; -.
DR STRING; 561896.B8PKQ0; -.
DR KEGG; ppl:POSPLDRAFT_97570; -.
DR HOGENOM; CLU_339220_0_0_1; -.
DR InParanoid; B8PKQ0; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 10..27
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 94137 MW; D072DDDFCBD8D66B CRC64;
MAKSRKASKR KCGGCGQKGH GSNECTKHNK AGMAIGNARN LTGIYEYHAR IVHKSEIIPK
GVGTSLGLQA NAINCESCGE EEHFRPRFSK SWEARNNKPD PTATYSWYPD NGESTTGYAP
RWYSESVESD NDQETPVVPL AARARAACAT ENFALAVSLF AQAIASDPHV ASHYTERGIA
YAQSKKYACA IGDFQTASSK ADYIPSPLIS FWTAKCRFYL GSHASALFAV RDVLSLDPDY
TDALALKRRL VELQKHIESY HAARKRQHWK LARAAYESCL GIYSEEDCDL PVDIRCWNVE
LRMAEADWKS VVSSVERLMH KEPKSTEVML LRARVLLLTA KLTDALAQTM TVLKLDPDDA
NAKEIRTRLK GIIRSQSEGG VHFRHGRWID AIREWDEALH LVGDKAEEGN GGIIRATLLR
GKAEAELNIG NYSDGIKHVN IALELDATYA EALLTRARIN VSLELYDVAV EGFRAALQLG
KLTMPVLVLS SVQEELDAAE QKAINERRDI NLEILRVEGY RKFCNKIYNA TKFAMLKLDE
QFVPEPTAKP TGNESIVERW ILHKLNVAAR DVNQQLEQRN FMAATNTAYN FWLYELCDVY
IEAMKVMTDE SASPTMRRSA QQTLYTSLDL GLRLLHPFMP FVTEELWQRL PRRPNDPTQS
IMLSAYPVFN SSSVFEDAYR DFELVFSAIK TSRSLAASYN LQSDLQLFVR VQSENEVALF
ESQVPTILAL TKHGKSVKIV RTPEDIPAGC GSAVLTPTVV LHVLVRGQVD LDAEIVKCQK
KLDFARLNLD KILKTESQPD YENVVAANVR LFNEEKRRTL EADIANLELS IQMFEKLK
//
