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Database: UniProt
Entry: A0A0W1KKP6_9ACTO
LinkDB: A0A0W1KKP6_9ACTO
Original site: A0A0W1KKP6_9ACTO 
ID   A0A0W1KKP6_9ACTO        Unreviewed;       427 AA.
AC   A0A0W1KKP6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000256|HAMAP-Rule:MF_00176,
GN   ECO:0000313|EMBL:KTF04597.1};
GN   ORFNames=AQZ59_00584 {ECO:0000313|EMBL:KTF04597.1};
OS   Trueperella bernardiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Trueperella.
OX   NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04597.1, ECO:0000313|Proteomes:UP000054404};
RN   [1] {ECO:0000313|EMBL:KTF04597.1, ECO:0000313|Proteomes:UP000054404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04597.1,
RC   ECO:0000313|Proteomes:UP000054404};
RA   Bernier A.-M., Bernard K.;
RT   "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT   0504T, Isolated from Blood Culture.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}.
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|HAMAP-Rule:MF_00176};
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|HAMAP-Rule:MF_00176};
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|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is involved in tRNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00176}.
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:KTF04597.1}.
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DR   EMBL; LNIZ01000002; KTF04597.1; -; Genomic_DNA.
DR   RefSeq; WP_062612981.1; NZ_PKHY01000003.1.
DR   AlphaFoldDB; A0A0W1KKP6; -.
DR   STRING; 59561.AQZ59_00584; -.
DR   PATRIC; fig|59561.3.peg.575; -.
DR   OrthoDB; 9804647at2; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000054404; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 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; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00176};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00176}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00176};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00176};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00176}; Reference proteome {ECO:0000313|Proteomes:UP000054404}.
FT   DOMAIN          139..406
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         230..232
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         261..263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         284
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         348..351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         382
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   427 AA;  46768 MW;  9C6D1791BAA9F644 CRC64;
     MIDIRTIRDN PEQVKASQRA RGAAESDVDS VLAADEARRS SLQEFEDLRA EQKALSRTVG
     KASPEERPAI LAKAKEMAEQ VKALEAKSDS AAAAFQEAML KLQNIIVDGV PAGGEDDYVV
     LREVGKIRDF AAEGVQVKDH LDVAEGIDAL DMERGAKVSG ARFYYLTGIG ARLELALLTM
     AADQAEANGF KLMNTPTLVK PEVMGGTGFL GAHSDEIYYL PADDLYLTGT SEVALAGYHE
     NEILDLTAGP KRYAGWSTCY RREAGSHGKD TRGIIRVHQF NKVEMFSFCD AADAEAEHAR
     FLGWEEDMLA KVELPYRVID TAAGDLGASA ARKFDCEAWL PSQNRFMEVT STSNCTTFQA
     RRLKIRQRGE DGMEAVATIN GTLATTRWLV AMFENHQQAD GSLYVPHALR PYLGGREVIE
     PVRGLQA
//
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