ID A0A1D2IHP3_9ACTN Unreviewed; 425 AA.
AC A0A1D2IHP3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Serine--tRNA ligase {ECO:0000256|ARBA:ARBA00039158};
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/Sec) synthetase {ECO:0000256|ARBA:ARBA00033352};
GN Name=serS_1 {ECO:0000313|EMBL:ODA73997.1};
GN ORFNames=APS67_001923 {ECO:0000313|EMBL:ODA73997.1};
OS Streptomyces sp. AVP053U2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA73997.1, ECO:0000313|Proteomes:UP000054731};
RN [1] {ECO:0000313|EMBL:ODA73997.1, ECO:0000313|Proteomes:UP000054731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA73997.1,
RC ECO:0000313|Proteomes:UP000054731};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005045}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODA73997.1}.
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DR EMBL; LMTQ02000008; ODA73997.1; -; Genomic_DNA.
DR RefSeq; WP_042176037.1; NZ_LMTQ02000008.1.
DR AlphaFoldDB; A0A1D2IHP3; -.
DR OrthoDB; 9804647at2; -.
DR Proteomes; UP000054731; 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; PTHR43697:SF1; SERINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43697; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ODA73997.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054731}.
FT DOMAIN 167..406
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46212 MW; 494153A7D7E34671 CRC64;
MHDPQELLKD GPQAVRRLAR RRHDLDLAAL ADALRERNGA QAEVTRLRTE VNRTARARRS
GPPTEEEKAS ARALRTEVQG AEAAARTAAA HLTELLLSVP NIPLDAVPDG DSEKETVEIR
RGGPAPRPAD GARHHADIGE SLGILDGPAA ARLSGARFSV ARGAGARLER ALRDFLLDLH
TREHGYTEQS VPFLVDRDTM TGTGQLPKFE DDLFRTQVGE RELFLIPTAE VPLTNLVAGR
LLDSRSLPLA FTACTPCFRA EAGAYGRDTR GILRLHQFEK VELVRVCAPE DAPAQLELMV
NHAEECLKRL ELAHRVVLLP AGDLGFSARM TYDVEVWLPG SGSYREISSV SDCGTFQARR
ADIRIKRPDG SRTPAVTLNG SALPIGRTVA ALLEQGARED GSVVLPEVLV PYTGFRRILP
GGDTA
//
