ID   SYL2_SULAC              Reviewed;         942 AA.
AC   Q4J8J7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Leucyl-tRNA synthetase 2;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucine--tRNA ligase 2;
DE            Short=LeuRS 2;
GN   Name=leuS2; OrderedLocusNames=Saci_1572;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000077; AAY80885.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_256178.1; -.
DR   GeneID; 3474607; -.
DR   GenomeReviews; CP000077_GR; Saci_1572.
DR   KEGG; sai:Saci_1572; -.
DR   NMPDR; fig|330779.3.peg.378; -.
DR   HOGENOM; Q4J8J7; -.
DR   BioCyc; SACI330779:SACI_1572-MON; -.
DR   BRENDA; 6.1.1.4; 434.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00049; -; 1.
DR   InterPro; IPR015413; aa-tRNA-synt_I.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   TIGRFAMs; TIGR00395; leuS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    942       Leucyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000152143.
FT   MOTIF        35     45       "HIGH" region.
FT   MOTIF       619    623       "KMSKS" region.
FT   BINDING     622    622       ATP (By similarity).
SQ   SEQUENCE   942 AA;  109179 MW;  4DD802C8C8C861C4 CRC64;
     MKISEKWQKE WENKRVFDAT PDPNKKKFFT TIAFPYPNSP FHLGHGRTYV TGDIYARYMR
     MRGYNVLFPM AFHYTGTPII AMADDVAKGD KELIDIFKSI YEIPDDVISK LVDPLFMANY
     FKEEIKQAMK EIGLSIDWRR EFTTIDPEFS SFIIWQFRKL QEKGFIVRDT HPVGWCPVHH
     IPVGMHDTKG DMEPEIGEFV LIYFDSDMGI LPVATLRPET VFGAIAVWVN PHESYSIVEI
     DGKKYVMSEK ASSKLSFQID NLKVITVVKG SELVKHSAVN PITGKEVPII GANFVDPLTG
     TGVVMSVPAH APFDYFYLKK TKSELSIISV IRVEGMGETL AKDLVEKSNP QNDNDLKKLT
     EQVYRIEYNK GVMIDITKLV KPEYVEELKP LVNLPVPAAR QKITEFITQK GLGRKIYEIM
     NRPVYCRCGN EVVVKILKDQ WFLDYGNQEW KDLARKSIES IRFIPPEIKK DFEFVVDWLQ
     KRACARTRGL GTPLPWDKKW IIESLSDSTI YMAFYTIAHR LKEHKLKPSQ LTYEFWEYIM
     LGNGNPDEIS KISGIPVEVI KAMRDEFLYW YPLDVRHSGK DLVPNHLSFF IFNHAAIFPH
     QLWPKGIAVN GFVLYDGKKM SKSLRNIVPL RKAIRMYSPD VIRIALTTNA DIGSDVNFSD
     SYAKSIIDTL KNYYDLLEKL KEFKGEDEGF PEKWLKSKFY QMVINVTQYM DSLDLRSSSN
     EILYNFSSYI NEYFELVRSE GREPNGKLLS QILQIWIKLL SPFAPHFAEE LWHKIGKNTL
     VSLESWPIID QSNVDLFIDL THTYHRKLLN DIQAILSVYK DTPKSIKIFV ANKEFLNVLR
     DAINIVQKGG QLRQLMEIHK PKGKQDARLY QKIYEEAREI DDDMKKLVTN FDFDEKDLLD
     KGLKYLSYKL GIKEIRILDA SEMDRTKYNK DALPLRPAII IE
//