ID   SYI_ANAMM               Reviewed;        1101 AA.
AC   Q5PAL9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Isoleucyl-tRNA synthetase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucine--tRNA ligase;
DE            Short=IleRS;
GN   Name=ileS; OrderedLocusNames=AM684;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the
RT   surface is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile).
CC   -!- COFACTOR: Zinc (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)) (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 2 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000030; AAV86661.1; -; Genomic_DNA.
DR   RefSeq; YP_153916.1; -.
DR   GeneID; 3171286; -.
DR   GenomeReviews; CP000030_GR; AM684.
DR   KEGG; ama:AM684; -.
DR   HOGENOM; Q5PAL9; -.
DR   OMA; Q5PAL9; SNWYVRR.
DR   BioCyc; AMAR234826:AM684-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02003; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002301; Ile-tRNA-synt_Ia.
DR   InterPro; IPR015905; Ile-tRNA-synt_Ia_N.
DR   InterPro; IPR018353; Isoleucyl-tRNA_synthetase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF9; Ile-tRNA-synt_Ia; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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   1101       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_0000098514.
FT   MOTIF        50     60       "HIGH" region.
FT   MOTIF       629    633       "KMSKS" region.
FT   BINDING     632    632       ATP (By similarity).
SQ   SEQUENCE   1101 AA;  125904 MW;  981A2927BF1933CD CRC64;
     MNYYPEVKGN PEFSAIEKEI LQYWNSEKIF EESVNTRSRD RSFVFYDGPP FANGLPHYGH
     LLTGFIKDAV ARYKTMRGFR VERKFGWDCH GLPAEMLAEK ELGVSGKVSI ESFGIDKFND
     YCRSSIMRFT QQWREYVERQ GRWVDFENGY RTMDKSFMES VMWAFHELWH KGLVYESVKV
     VPYSWACQTP LSNFETKMDN AYREKVSKSV TVRFKLSEQV GFVPQGVESC SILAWTTTPW
     TLVSNFALAI NTNMDYVGAV VGAEMLIFSA GYLDHFMRYC ERHSLECAKV VQIPAKELLA
     VKYMPPFPYF ADSKNAFMVL DAEFVAEGAG TGIVHLAPGF GEDDFLLCKQ HGIPNLGEES
     RGMLSVICPI DDAGRFTAAV GDFAGQHVFD VVDAVIRQLK EKGLWFATEQ CTHSYPHCWR
     TDTPLIYRAT SSWYVEVTKL KARMVELNKE VNWVPEHVQS GQFGKWLDGA KDWSVSRHRF
     WGAPVPVWRS DDPKYPRTDV YGSIKKVLPD VKALEEDFGP VEDLHRPYID NLVRPNPDDP
     TGKSMMRRVP DVLDCWFESG SMPYAQMHYP FENKEFFDSH FPADFITEYI AQTRGWFYTL
     FVLSTGLFDR HPFKNCICHG VVLDIKGQKL SKRLNNYPDP MEMFEKYGAD SVRFTMLSHA
     VSIGGDLLLD QDGDVVRDTL KSVVKPIWNS YSFFTVYANS DQMQGRILES LEGITNIMDQ
     YILYECACMV VKVLEAMESS SAGVRDPYNI RLACAAIVQF SDKLNNWYIR GCRGRFWMRD
     KTADKSDAYN TLYTVLYHLA RTIAPFLPFI AESIWLGLSF QREKSVHLAD FPDASSFSAV
     HQYKKNAEYM QLAMDVCSHV LSLRNAHNIR VRQPLRRMVV YPYNCESLLD MPQQYRDIIL
     NEVNVKSLQI ASTIGDMASF ELKLNFALLG QRVPEKVKQI ITLARAGVWE VQSDGSLLLG
     APGCEQCVIQ KDEFSLNLKV HSEYACQIIS GGVPVGVLHI DHELTRELLL EGIARDVMRL
     IQQARKDCGL EMLDHAEVII NTDAAEIIEA ISIWYDFIKQ QTFSHTLEHR PAQAVVEDCS
     KYTKISGKDF DIFLCKSALC S
//