ID   SYP_ANAPZ               Reviewed;         426 AA.
AC   Q2GK70;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Prolyl-tRNA synthetase;
DE            EC=6.1.1.15;
DE   AltName: Full=Proline--tRNA ligase;
DE            Short=ProRS;
GN   Name=proS; OrderedLocusNames=APH_0647;
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 proline to tRNA(Pro) in a
CC       two-step reaction: proline is first activated by ATP to form Pro-
CC       AMP and then transferred to the acceptor end of tRNA(Pro) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC       diphosphate + L-prolyl-tRNA(Pro).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 2 subfamily.
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DR   EMBL; CP000235; ABD43602.1; -; Genomic_DNA.
DR   RefSeq; YP_505231.1; -.
DR   GeneID; 3930859; -.
DR   GenomeReviews; CP000235_GR; APH_0647.
DR   KEGG; aph:APH_0647; -.
DR   NMPDR; fig|212042.5.peg.632; -.
DR   TIGR; APH_0647; -.
DR   HOGENOM; Q2GK70; -.
DR   OMA; Q2GK70; VVSHQLM.
DR   BioCyc; APHA212042:APH_0647-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_01570; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac.
DR   InterPro; IPR002316; Pro-tRNA-synth_IIa_cons-reg.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 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    426       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000248888.
SQ   SEQUENCE   426 AA;  48223 MW;  28B518077C79FDC2 CRC64;
     MRLSEFYSPT VKNVSSDVVS ASHKYSIRAG IVSQTASGIY TLLPLGLMVL RKVENIIREE
     INAVGFSEIL MPTMQPADLW KESQRYDSYG QELIRIHDRG GREMVLGPTH EEVVTDLVRS
     SLKSYRDLPV NLYQIQWKFR DELRPRNGIL RSREFLMMDA YSFDTDFEKA MKTYDAVFRA
     YRKAFKRMNL QTIALKADMG AIGGSVSHEF HVLTPTGEST VYYDERALEL SEMNDYGIEE
     LKEVYAATDD MHDEKSCGIA PEDLKTARGI EVGHIFYLDD RYSRTMNVKF CNTDGHSGTH
     VKMGCYGIGI SRLIGALIEV FHDDAGIKWP LSVAPFKVGI VNLFSKNEEC KRVSERIHSV
     LPNDSLYDDR DDTPGVKLSR MDLIGLPWQV IVGNSFIKDG VLELKNRATG DIELLSVDDV
     VSRISV
//