ID   SYS_ANAPZ               Reviewed;         428 AA.
AC   Q2GKS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=APH_0427;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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; CP000235; ABD44439.1; -; Genomic_DNA.
DR   RefSeq; YP_505030.1; -.
DR   GeneID; 3931299; -.
DR   GenomeReviews; CP000235_GR; APH_0427.
DR   KEGG; aph:APH_0427; -.
DR   NMPDR; fig|212042.5.peg.414; -.
DR   TIGR; APH_0427; -.
DR   HOGENOM; Q2GKS1; -.
DR   OMA; Q2GKS1; EHFEIGE.
DR   BioCyc; APHA212042:APH_0427-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    428       Seryl-tRNA synthetase.
FT                                /FTId=PRO_1000019609.
FT   NP_BIND     259    261       ATP (By similarity).
FT   NP_BIND     346    349       ATP (By similarity).
FT   REGION      228    230       Serine binding (By similarity).
FT   BINDING     282    282       Serine (By similarity).
FT   BINDING     384    384       Serine (By similarity).
SQ   SEQUENCE   428 AA;  48221 MW;  5AC1A7A4F94FC1DF CRC64;
     MHDIEFIKNN PELFDKAMLS RGLESQAAKI IELDLQKRKL LTELYALREQ RNAITKEVTV
     LKQSGADCSS HVETSKKLAH EISELEERIK RDTGLSYLLC SLPNIPDDAV PFGKSADDNV
     EVRSYGQKRS FSFEIKPHYV LGEMLNLMDF RRAAFLSGSR FSILSGQLAA LERGLASFML
     EMHTKEFGYT EVFHPSLVND LAMFNVGQLP KFTHDSFQTT DAMRLVPTSE VVLTNLVANT
     NLHRNSLPLR FTAYSQCFRS EAGSAGQDTR GMIRQHQFSK VELVSITDAS QSNVELERML
     SVAEEVLKRL ELPYRVVLLC TGDMGFSASI SYDIEVWMPA QNKYREISSC SNCKDFQARR
     MGAKCFYLEK QNKRSSFVHT LNGSALALGR TIAAIMENYQ NSDGTITIPD ALRKFMSADY
     IRPGTALP
//