ID F8H002_PSEUT Unreviewed; 426 AA.
AC F8H002;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 29-MAY-2013, entry version 15.
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=PSTAB_2173;
OS Pseudomonas stutzeri (strain ATCC 17588 / DSM 5190 / CCUG 11256 / JCM
OS 5965 / LMG 11199 / NCIMB 11358 / Stanier 221).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=96563;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 17588;
RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.;
RT "Complete Genome Sequence of Pseudomonas stutzeri Strain CGMCC
RT 1.1803.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 /
RC NCIMB 11358 / Stanier 221;
RA Yan Y., Chen M., Lu W., Zhang W., Ping S., Lin M.;
RT "Complete genome sequence of Pseudomonas stutzeri strain CGMCC
RT 1.1803.";
RL Submitted (JUN-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.
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DR EMBL; CP002881; AEJ05454.1; -; Genomic_DNA.
DR RefSeq; YP_004714543.1; NC_015740.1.
DR EnsemblBacteria; AEJ05454; AEJ05454; PSTAB_2173.
DR GeneID; 10943216; -.
DR KEGG; psz:PSTAB_2173; -.
DR KO; K01875; -.
DR BioCyc; PSTU96563:GHIN-2221-MONOMER; -.
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 264 266 ATP (By similarity).
FT NP_BIND 351 354 ATP (By similarity).
FT REGION 233 235 Serine binding (By similarity).
FT BINDING 287 287 Serine (By similarity).
FT BINDING 387 387 Serine (By similarity).
SQ SEQUENCE 426 AA; 47575 MW; 659BAA93AA7F9362 CRC64;
MLDSKLVRTQ LQDVAARLAT RGYQLDVARI EALEAQRKTV QTRTEQLQAE RNARSKSIGQ
AKQRGEDIAP LLADVDRMGS ELESGKQELD RIQSELDQLM LSIPNLPHES VPVGADEEEN
VEVRRWGTPK AFDFPVQDHV ALGEQHGWLD FETAAKLSGA RFALMRGPIA RLHRALAQFM
IDLHTREHGY EEAYTPYLVQ APALQGTGQL PKFEEDLFKI SREGEADFYL IPTAEVSLTN
IVAGEILDAK QLPLKFVAHT PCFRSEAGAS GRDTRGMIRQ HQFDKVEMVQ IVEPSKSFEA
LEELTGNAEK VLQLLELPYR VLSLCTGDMG FGATKTYDLE VWVPSQDKYR EISSCSNCGD
FQARRMQARY RNPETGKPEL VHTLNGSGLA VGRTLVAVLE NYQQADGRIL VPEVLKPYMG
GIEVIG
//
