ID   SYS_ANAVT               Reviewed;         426 AA.
AC   Q3MCE0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Seryl-tRNA synthetase;
DE            EC=6.1.1.11;
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
DE   AltName: Full=Serine--tRNA ligase;
DE            Short=SerRS;
GN   Name=serS; OrderedLocusNames=Ava_1724;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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(Ser) = AMP + diphosphate
CC       + L-seryl-tRNA(Ser).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC       + L-seryl-tRNA(Sec).
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; CP000117; ABA21346.1; -; Genomic_DNA.
DR   RefSeq; YP_322241.1; -.
DR   GeneID; 3682145; -.
DR   GenomeReviews; CP000117_GR; Ava_1724.
DR   KEGG; ava:Ava_1724; -.
DR   NMPDR; fig|240292.3.peg.2804; -.
DR   HOGENOM; Q3MCE0; -.
DR   OMA; Q3MCE0; EHFEIGE.
DR   BioCyc; AVAR240292:AVA_1724-MON; -.
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:0006434; P:seryl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00176; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR002317; Ser-tRNA-synth_IIa.
DR   InterPro; IPR018156; Ser-tRNA-synth_IIa_C.
DR   InterPro; IPR015866; Ser-tRNA-synth_IIa_N.
DR   Gene3D; G3DSA:1.10.287.40; Ser-tRNA-synth_IIa_N; 1.
DR   PANTHER; PTHR11778; tRNA-synt_ser; 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   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   CHAIN         1    426       Seryl-tRNA synthetase.
FT                                /FTId=PRO_1000019610.
FT   NP_BIND     266    268       ATP (By similarity).
FT   NP_BIND     353    356       ATP (By similarity).
FT   REGION      235    237       Serine binding (By similarity).
FT   BINDING     289    289       Serine (By similarity).
FT   BINDING     389    389       Serine (By similarity).
SQ   SEQUENCE   426 AA;  47740 MW;  D9F2509398315C22 CRC64;
     MLDIKQIREN PQLIQERLNS RSGTYDIQPI LQLDKQQREL EATRSQIQAR SNEIGKIVGQ
     KIKSGINPQD PEIQALRDEG NSIKAQLSEL EPREKELKAE IEQLILALPN LPSDSTPIGK
     SEEENVEVRR WGDEYLPQNP NIIPHWEIGE KLGILNFERA VKVAQSRFVN LIGAGAALER
     ALINFMLKTQ TVAGYVEVSP PLLVNTDSLT GTGQLPKFAE ESFKCADDEL WLIPTAEVPV
     TNLYRGEILA AENLPIYHCA YTPCFRREAG SYGRDMRGLI RLHQFNKVEL VKVVHPSTSF
     DELEKLVGNA EAILQALKLP YRVINLCTGD LGFGATKTYD LEVWLPSSGK YREISSCSNC
     FDFQARRADI RFKEAGKKGT QFVHTLNGSG LAVGRTMAAI LENYQQPDGT ILIPEVLQVY
     LGREVL
//