ID A0A165CB10_9APHY Unreviewed; 505 AA.
AC A0A165CB10;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
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=LAESUDRAFT_716893 {ECO:0000313|EMBL:KZT02486.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT02486.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT02486.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT02486.1,
RC ECO:0000313|Proteomes:UP000076871};
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; KV427652; KZT02486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CB10; -.
DR STRING; 1314785.A0A165CB10; -.
DR InParanoid; A0A165CB10; -.
DR OrthoDB; 239638at2759; -.
DR Proteomes; UP000076871; 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 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; IPR042103; SerRS_1_N_sf.
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; 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 ECO:0000313|EMBL:KZT02486.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 231..491
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..141
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 55489 MW; 034DB097CF7DE03E CRC64;
MSASAHCKST ANATTASKAK GRPSAQHHPQ LADHHVSTGL PRPRLEYRKI SENAVFKSHN
AFNRKAALPI GAIQTIARLY EDQKDVLNSL NTKRHARSTV GERIRASAQD PQLKQAALDE
AKSLKAEIMD LECRLEELEG RLYSLALALP NDTHPDVPIG PESEAVTLST HGPEPIPISA
ERDHLSICRA LNLVDLEAAA TVTGSSWYYL VNEGALLELA LVNYALSIAI KHGFTPVTTP
DVVRSDIASR CGFQPRDQNA DPPVSQMYHI ANLDPEAAKA YHPEFVLAGT AEIPLAGMFA
NKILQAQDLP RKVVGLGHAF RAEAGARGAD TRGLYRVHQF TKLELFVVCE EEQSEKMMEE
IRRLQVEIFG SLGFPFRVLD MPTEELGASA YRKYDMEAWM PGRGGWGEIS STSNCTDYQA
RRLHIRYRRT GSSSTPVASS EVFTSALPFA HTLNGTAAAV PRLIVALLEN GARFDEKGNV
VGFDLPAALR PFWIGGNERK LNRWV
//
