ID   SYS_ALCBS               Reviewed;         429 AA.
AC   Q0VQ06;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=ABO_1294;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL16742.1; -; Genomic_DNA.
DR   RefSeq; YP_693014.1; -.
DR   GeneID; 4213632; -.
DR   GenomeReviews; AM286690_GR; ABO_1294.
DR   KEGG; abo:ABO_1294; -.
DR   NMPDR; fig|393595.12.peg.1306; -.
DR   HOGENOM; Q0VQ06; -.
DR   OMA; Q0VQ06; LKPYMGG.
DR   BioCyc; ABOR393595:ABO_1294-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    429       Seryl-tRNA synthetase.
FT                                /FTId=PRO_1000019606.
FT   NP_BIND     267    269       ATP (By similarity).
FT   NP_BIND     354    357       ATP (By similarity).
FT   REGION      236    238       Serine binding (By similarity).
FT   BINDING     290    290       Serine (By similarity).
FT   BINDING     390    390       Serine (By similarity).
SQ   SEQUENCE   429 AA;  47944 MW;  2EC992A74F72D5BB CRC64;
     MLDIRALRQD GEAIKAALSK RGYTLDLEEF AALDAKRKQA DMRSQELQAD RKKASKQVGE
     LIKSGMAVDE AKAQVADALQ TIDTELDKEV ASAKAIQDEI REYLMGIPNV PQEAVPAGND
     EDDNVEVRRW GTPKTLPFEP KDHVDIGEAL EGGLDFERAA KLSGARFAVM SGGLARMHRA
     LIDFMLDIHS DEHGYQEVYV PFLVGPEALR GTGQLPKFAE DLFKIEGERE LYLIPTAEVP
     VTNLAADEIL EANTMPRRYT CHTPCFRSEA GSHGRDTRGM IRQHQFEKVE LVQMVRPEES
     DAALEALTGH AEAILQKLDL PYRVVILCGG DLGFSSSKTY DIEVWLPSQQ CYREISSCSN
     FRDYQSRRMQ ARWRNPETGK PELVHTLNGS ALAVGRTLVA ILENYQNDDG SVTVPEALRP
     YMRGLERLK
//