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Database: UniProt
Entry: A0A0D8HJ23_9ACTN
LinkDB: A0A0D8HJ23_9ACTN
Original site: A0A0D8HJ23_9ACTN 
ID   A0A0D8HJ23_9ACTN        Unreviewed;       436 AA.
AC   A0A0D8HJ23;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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 {ECO:0000313|EMBL:KJF17923.1};
GN   ORFNames=AXFE_12080 {ECO:0000313|EMBL:KJF17923.1};
OS   Acidithrix ferrooxidans.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidithrix.
OX   NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF17923.1, ECO:0000313|Proteomes:UP000032360};
RN   [1] {ECO:0000313|EMBL:KJF17923.1, ECO:0000313|Proteomes:UP000032360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Py-F3 {ECO:0000313|EMBL:KJF17923.1,
RC   ECO:0000313|Proteomes:UP000032360};
RA   Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT   "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT   strain Py-F3.";
RL   Submitted (JAN-2015) 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:KJF17923.1}.
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DR   EMBL; JXYS01000027; KJF17923.1; -; Genomic_DNA.
DR   RefSeq; WP_052604971.1; NZ_JXYS01000027.1.
DR   AlphaFoldDB; A0A0D8HJ23; -.
DR   STRING; 1280514.AXFE_12080; -.
DR   PATRIC; fig|1280514.3.peg.1577; -.
DR   OrthoDB; 9804647at2; -.
DR   Proteomes; UP000032360; 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; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KJF17923.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032360}.
FT   DOMAIN          184..420
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          52..101
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   436 AA;  48860 MW;  2925CFA3DE9E084A CRC64;
     MIDIRALREN PNETKELLSR RGIDTAVVDE LLEIDLRLRS SVSKRDSLRA VINDLSRSVA
     EAYRQKETAL AQELKEKSKA HGEALEELSK EVSELENARR DLWLVIPNVP SLDTPIGQGE
     KDNVILRYWS PKTGHSTVEV DLDYEPAQKV PHWEIGAALG ILDLERAAKL SGSMFPMYKG
     AGARMLRALT SFALDAHSDA FLEVRPPTFV KRETMVSTGH LPKFAEDAYQ MERDDLWAIP
     TAEVPLTSMA RDEILPSEEL PIRMTAATPC FRREAGSAGR DTRGLLRLHE FDKVELMVYS
     NPKDSQGVFM DMLRRAEGIL QSLGLTYRVL DLCTGDIGAS AKRTFDLEAY SPGVGRWLEV
     SSVSWFGDYQ ARRANIRFRD ASTNEVSYVD TLNGSALAWA RVFAVLIETY RNQDESVTIP
     LVLVPYMGGI QNIVPK
//
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