ID   SYS_ANADE               Reviewed;         435 AA.
AC   Q2IGB1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=Adeh_3853;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
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., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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; CP000251; ABC83619.1; -; Genomic_DNA.
DR   RefSeq; YP_467056.1; -.
DR   GeneID; 3887795; -.
DR   GenomeReviews; CP000251_GR; Adeh_3853.
DR   KEGG; ade:Adeh_3853; -.
DR   HOGENOM; Q2IGB1; -.
DR   OMA; Q2IGB1; LKPYMGG.
DR   BioCyc; ADEH290397:ADEH_3853-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    435       Seryl-tRNA synthetase.
FT                                /FTId=PRO_1000019608.
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     386    386       Serine (By similarity).
SQ   SEQUENCE   435 AA;  48325 MW;  5FF67C5F2903210C CRC64;
     MLDLKAVAAD FESFERRLAR RGEGAVQALA PVKPLAARRR ELNVLLEKQK KEQADANARI
     RELARTDKGA VEGARASLRA LGDEVKKTEA ELGEVEAELT RLLMLVPNPP HDSVPDGKDE
     HDNVVVKTWG EQKAYGFTPK PHWEVGEALG VLEWQQAAKL SGSRFTILKG AAARLERAIV
     SFFIDVHTSR GYTEILPPYL VTGETMTGTG QLPKFEEDLF KTTNEPPMYL IPTAEVPVTN
     MHRDEIFEAS AMPVSYCAFS PCFRAEAGSA GRDTRGIMRQ HQFHKVELVK LSKAEESYAE
     HEKMLDDACE VLRRLGLHHR VSLLCTGDMG FSSAKTYDIE VWCPGQGAYR EISSVSNCED
     FQARRIRVRY RGENGKPRLA HTLNGSGVAV GRTIVAILEQ CQEADGTVVI PEPLRPYMGG
     LERIAAETFP RGVER
//