ID   SYSC_MACFA              Reviewed;         514 AA.
AC   Q4R4U9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Seryl-tRNA synthetase, cytoplasmic;
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=SARS; ORFNames=QccE-14020;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (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; AB169795; BAE01876.1; -; mRNA.
DR   HOVERGEN; Q4R4U9; -.
DR   BRENDA; 6.1.1.11; 3438.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
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   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   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    514       Seryl-tRNA synthetase, cytoplasmic.
FT                                /FTId=PRO_0000270763.
FT   NP_BIND     302    304       ATP (By similarity).
FT   NP_BIND     391    394       ATP (By similarity).
FT   REGION      271    273       Serine binding (By similarity).
FT   BINDING     318    318       ATP; via carbonyl oxygen and amide
FT                                nitrogen (By similarity).
FT   BINDING     325    325       Serine (By similarity).
FT   BINDING     429    429       Serine (By similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
SQ   SEQUENCE   514 AA;  58765 MW;  81C2068AF066B393 CRC64;
     MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC
     SKTIGEKMKK KEPVEDDESV PENVLNFDDL TADALANLKV SQIKKVRLLI DEAILKCDAE
     RIKLEAERFE NLREIGNLLH PSVPISNDED ADNKVERIWG DCTVRKKYSH VDLVVMVDGF
     EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY TPIYTPFFMR KEVMQEVAQL
     SQFDEELYKV IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC
     FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE FYQSLGIPYH
     IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV
     EFVHMLNATM CATTRTICAI LENYQTEKGI TVPEKLKEFM PPGLQELIPF VKPAPIDQEP
     SKKQKKQHEG SKKKAAARDV ALESRLQNME VTDA
//