ID   D9Q038_ACIS3            Unreviewed;       459 AA.
AC   D9Q038;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   14-MAY-2014, entry version 25.
DE   RecName: Full=Serine--tRNA ligase;
DE            EC=6.1.1.11;
DE   AltName: Full=Seryl-tRNA synthetase;
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN   Name=serS; OrderedLocusNames=ASAC_0269;
OS   Acidilobus saccharovorans (strain DSM 16705 / VKM B-2471 / 345-15).
OC   Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / VKM B-2471 / 345-15;
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
RT   supports a new order, Acidilobales, and suggests an important
RT   ecological role in terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC       able to aminoacylate tRNA(Sec) with serine, to form the
CC       misacylated tRNA L-seryl-tRNA(Sec), which will be further
CC       converted into selenocysteinyl-tRNA(Sec) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC       + L-seryl-tRNA(Sec).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC       + L-seryl-tRNA(Ser).
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
CC       1/1.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC       N-terminal extension that is involved in tRNA binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Type-1 seryl-tRNA synthetase subfamily.
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DR   EMBL; CP001742; ADL18676.1; -; Genomic_DNA.
DR   RefSeq; YP_003815707.1; NC_014374.1.
DR   EnsemblBacteria; ADL18676; ADL18676; ASAC_0269.
DR   GeneID; 9498492; -.
DR   KEGG; asc:ASAC_0269; -.
DR   HOGENOM; HOG000035937; -.
DR   KO; K01875; -.
DR   OMA; KAAPKDY; -.
DR   BioCyc; ASAC666510:GH9G-281-MONOMER; -.
DR   UniPathway; UPA00906; UER00895.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.287.40; -; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
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; 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; 1.
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; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   NP_BIND     284    286       ATP (By similarity).
FT   NP_BIND     371    374       ATP (By similarity).
FT   REGION      253    255       Serine binding (By similarity).
FT   BINDING     300    300       ATP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     307    307       Serine (By similarity).
FT   BINDING     408    408       Serine (By similarity).
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
//