ID F2L4G5_THEU7 Unreviewed; 453 AA.
AC F2L4G5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 03-APR-2013, entry version 16.
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=TUZN_1938;
OS Thermoproteus uzoniensis (strain 768-20).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC Thermoproteaceae; Thermoproteus.
OX NCBI_TaxID=999630;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-20;
RX PubMed=21478349; DOI=10.1128/JB.00409-11;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL J. Bacteriol. 193:3156-3157(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=768-20;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP002590; AEA13397.1; -; Genomic_DNA.
DR RefSeq; YP_004338709.1; NC_015315.1.
DR EnsemblBacteria; AEA13397; AEA13397; TUZN_1938.
DR GeneID; 10361450; -.
DR KEGG; tuz:TUZN_1938; -.
DR KO; K01875; -.
DR UniPathway; UPA00906; UER00895.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:HAMAP.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA: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; tRNA_binding_arm; 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 281 283 ATP (By similarity).
FT NP_BIND 368 371 ATP (By similarity).
FT REGION 250 252 Serine binding (By similarity).
FT BINDING 297 297 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 304 304 Serine (By similarity).
FT BINDING 403 403 Serine (By similarity).
SQ SEQUENCE 453 AA; 52380 MW; 1BFE8FB51F920FA4 CRC64;
MSWSVLEALR NSPDVVRKTL VARRMDVTLV DRFLDLDSKW RELKREIDEL RHQHNVLSRE
ASKAPPQDRK TIAEKAKELI EKIKGLEDQL KAVEMERERL LFSFPNLIHE SVPVCPEGVD
SIPVRYWGTI KVAREDLEKV LRLDPRPEYV VVDKAPVGHA DEAENVLKMV DTLKAGEVAG
SRFYYMLDDL VWLDFALSLY ALEHLTSKGF RPIVPPYMLK YDVIRRVIDL DTFKDAIYKL
ENEDLYLIAT AEHGIAAYLY GRDLLEEELP QLYVGWSPCF RREAGAGSRD IKGIFRVHIF
HKVEQFVFSL AEESWTWHEE ITKNTEELMQ GLGLPYRVVN ICAHDLGAPA AKKYDVEVWY
PAQGTYRELA SCSNVTDWQS YRLGIRVTRR GMKREYVHTL NCTGLATTRT ITAILENYQR
EDGAVEIPKV LRKYLEPIAT APKDYIVPKN VRR
//
