ID   SYS2_METBU              Reviewed;         502 AA.
AC   Q12TN5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Type-2 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=Mbur_2337;
OS   Methanococcoides burtonii (strain DSM 6242).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcoides burtonii DSM 6242.";
RL   Submitted (MAR-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   -!- COFACTOR: Binds 1 Zn(2+) ion per subunit. This ion is coordinated
CC       with 2 cysteines, 1 glutamate and a water molecule that
CC       dissociates from the zinc ion to allow the coordination of the
CC       amino group of the serine substrate, which is essential for
CC       catalysis (By similarity).
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 (By 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 presumably involved in tRNA binding
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Type-2 seryl-tRNA synthetase subfamily.
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DR   EMBL; CP000300; ABE53191.1; -; Genomic_DNA.
DR   RefSeq; YP_566941.1; -.
DR   SMR; Q12TN5; 1-502.
DR   GeneID; 3998918; -.
DR   GenomeReviews; CP000300_GR; Mbur_2337.
DR   KEGG; mbu:Mbur_2337; -.
DR   NMPDR; fig|259564.8.peg.2241; -.
DR   HOGENOM; Q12TN5; -.
DR   OMA; Q12TN5; PAQCEPF.
DR   BioCyc; MBUR259564:MBUR_2337-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:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_01278; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; FALSE_NEG.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    502       Type-2 seryl-tRNA synthetase.
FT                                /FTId=PRO_0000286168.
FT   NP_BIND     336    338       ATP (By similarity).
FT   NP_BIND     347    348       ATP (By similarity).
FT   REGION      353    355       Serine binding (By similarity).
FT   METAL       306    306       Zinc; catalytic (By similarity).
FT   METAL       355    355       Zinc; catalytic (By similarity).
FT   METAL       461    461       Zinc; catalytic (By similarity).
FT   BINDING     304    304       Serine; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     336    336       Serine (By similarity).
FT   BINDING     400    400       Serine (By similarity).
FT   BINDING     432    432       ATP (By similarity).
FT   BINDING     435    435       Serine (By similarity).
FT   BINDING     468    468       ATP (By similarity).
SQ   SEQUENCE   502 AA;  57388 MW;  E3DA16D5AC8FDF58 CRC64;
     MELKFNLKGA FKTSTDPTGA KEVIAQYFDE ANNTILKKGA PEGQGAKITQ WDIVDGSIEL
     TIESGRYVRA HDAIMRLKKP LAAKLGKEFR IGIRGVDVKK FTISMPAEGE IGNMNIPHVS
     NISKVEGGLI LELNVGESEL ERRIPDRILT LMEEKVRAKD YGGKAEHWQI LWESDKKEHT
     FAGDPTQEMM KHGWIKRGAS RGQWIHGPQS TKMFRTFEKI VYDELLEPLG YREMIFPKLV
     PWEVWQKSGH AKGVYPEIYY VCPPKTRDPA YWEEVSDHYK VTHEVPTELI KSKIGDPIGG
     LCYAQCPPFW MYLQGETIPT DEFPIKVFDK SGTSHRYESG GIHGIERVDE FHRVEIVWLG
     TKEQVIETAR KLHERYMHIF NEILDLEWRK AWVTPWFMAQ EGLTGLSEQG EAGTTDYEAP
     LPYRGDDGEW LEFQNVSING NKYPSGFNVK SQTGEELWSG CSGVGLERWA SAFFAQKGLD
     PENWPEEFRK RVGEVPKGIR FL
//