ID   D9Q038_ACIS3            Unreviewed;       459 AA.
AC   D9Q038;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   07-APR-2021, entry version 65.
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   OrderedLocusNames=ASAC_0269 {ECO:0000313|EMBL:ADL18676.1};
OS   Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS   345-15).
OC   Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18676.1, ECO:0000313|Proteomes:UP000000346};
RN   [1] {ECO:0000313|EMBL:ADL18676.1, ECO:0000313|Proteomes:UP000000346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC   {ECO:0000313|Proteomes:UP000000346};
RX   PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA   Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT   a new order, Acidilobales, and suggests an important ecological role in
RT   terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
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|ARBA:ARBA00001032, ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00001706, ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP001742; ADL18676.1; -; Genomic_DNA.
DR   RefSeq; WP_013266188.1; NC_014374.1.
DR   STRING; 666510.ASAC_0269; -.
DR   EnsemblBacteria; ADL18676; ADL18676; ASAC_0269.
DR   GeneID; 9498492; -.
DR   KEGG; asc:ASAC_0269; -.
DR   eggNOG; arCOG00403; Archaea.
DR   HOGENOM; CLU_023797_0_1_2; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; 16385at2157; -.
DR   BioCyc; ASAC666510:G1GMD-285-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000000346; Chromosome.
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:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; -; 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; 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   PANTHER; PTHR11778; PTHR11778; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 2.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   TIGRFAMs; TIGR00414; serS; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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:UP000000346}.
FT   DOMAIN          164..433
FT                   /note="AA_TRNA_LIGASE_II"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NP_BIND         284..286
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   NP_BIND         371..374
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   REGION          253..255
FT                   /note="Serine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   COILED          33..53
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          69..103
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         300
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         307
FT                   /note="Serine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT   BINDING         408
FT                   /note="Serine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   459 AA;  52780 MW;  D59E1563610261A4 CRC64;
     MPWSILNLLR TNPEALREVA RKRQIDVKII DEAVQLDEQW RKVQAEINEL RHQHNVISAA
     IPKAKGEERE KLLAQAKELS RELEDAERRL SELEAKREEA LWRLPNVVLD DVPVGGEEAT
     RPVRFWGTPR VYHEYLDAFK AQTEAYGFNV PYELIDWKPV GHADMLENVL KLGDTEKASE
     VAGSRFYYLF DDLVWLDFAL LLYAIDKLTS KGYTLVLPPY MLRYKVINSV IDLATFQDAI
     YKIENDDLYL IATAEHSLAA MYYNEELYDD ELPKKFVGIS PAFRREAGAA NKDLKGIFRV
     HQFHKVEQFV FSKPEESQKI HEELISNAEG LFQGLGIPYR VVNIASGDLG ACAVKKYDLE
     AWMPAQGKYR EMVSASNCTD WQAYRLNIRL IRRKGMERGE YVHTLNSTGI ASTRTITAIL
     ENFQEPDGTV IIPKVLRKYL EPFDAAPKDF IKPRPRKAI
//