ID A0A165LF00_9APHY Unreviewed; 452 AA.
AC A0A165LF00;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=serine--tRNA ligase {ECO:0000256|ARBA:ARBA00012840};
DE EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE AltName: Full=Seryl-tRNA(Ser) synthetase {ECO:0000256|ARBA:ARBA00034892};
GN ORFNames=DAEQUDRAFT_759986 {ECO:0000313|EMBL:KZT64329.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT64329.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT64329.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT64329.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429132; KZT64329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165LF00; -.
DR STRING; 1314783.A0A165LF00; -.
DR OrthoDB; 239638at2759; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR NCBIfam; TIGR00414; serS; 1.
DR PANTHER; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11778; SERYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KZT64329.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 146..424
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 57..87
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 452 AA; 51774 MW; 807FF053D7173DAA CRC64;
MTLDILHFID NKGGNAEEIR ESQRKRGLSV ELVDEVIQMY ADWVKMDFDS NNINKQVNAI
QKEIAAKKKA KENADELVAK KKELDALVIA KKAETREFEQ KMRQKASTVG NIVGPNVPVS
MTEDDNKTVK TWHPKGEGVE VEKRTDIMPH HEVLLRLDAM DLERGTKITG HRGYFLTNDG
IDLNQALISY GLDFLRKRGY KKIQPPFMMN KDMMGKTAQL DQFDEELYKV IAAEDEKYLI
ATSEQPISAF HSDEWFDSPE TQLPIRYAGY STCFRKEAGS AGRDMWGIFR VHQFEKIEQF
CVTEPDKSWQ MLDAMLANSE EFYQSLGLPY RVVAIVSGAL NLAAAQKYDL EAWFPFQGAH
KELVSCSNCT DYQSRKLEVR CGLKTKDQTR KVYVHMLNGT LCATERALCC LVENHQTPEG
VVIPEVLRPY MQGRDFLPWV KELPKNLQRK QA
//
