ID   A0A3B4A3E7_9GOBI        Unreviewed;       514 AA.
AC   A0A3B4A3E7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
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};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000011006.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000011006.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001706};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010728}.
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DR   AlphaFoldDB; A0A3B4A3E7; -.
DR   STRING; 409849.ENSPMGP00000011006; -.
DR   Ensembl; ENSPMGT00000011737.1; ENSPMGP00000011006.1; ENSPMGG00000009119.1.
DR   Proteomes; UP000261520; Unplaced.
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; 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; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          191..471
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          488..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..514
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  57266 MW;  8CAA664B42543843 CRC64;
     MAASFSLAAA RRGCGALCAL TPALRHCPRP VLALTHRHSH GAPRSSLYEH VREGYSDKPD
     LNMSHICADP EAAVANVESR KGELRGDDVR QIVSLWQQLE AVRAEISSLE EQKRAIGDTV
     KALLPAYSAA RQRGREVRRR LSELGPKQND LEEQFYSKAL RLPNGTHPDV PHGDESQARV
     VELVGQKPKF DFKPRGHVEL GERLGLIRQR HLSHVSGHRS YYLRGGGARL QMALQNFTLD
     KLLKRGFIPL TVPDILKGAV FEGCGMQPHA HRSQVYALDP TRSPDLNLAG TGEVGIAGFF
     MDHAVNCTDL PVRTVCSSTC YRAETDTGRE TWGLYRVHHF NKVEMFGVTA DESGLESAQM
     LQEFVNLQKE LFTELELHFR VLDMPTQELG PPAHRKFDIE AWMPGRNSYG EISSGSNCTD
     YQSRRLNILY EREDQSLHYA HTVNATACAV PRMIVSILET HQTKDGSVRV PTALQPYFGS
     DLIQKPSYSP LRYIGPNQPN KPPRPGPRAP PTGP
//