ID   SYN_COLP3               Reviewed;         466 AA.
AC   Q481G3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Asparaginyl-tRNA synthetase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparagine--tRNA ligase;
DE            Short=AsnRS;
GN   Name=asnS; OrderedLocusNames=CPS_2591;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000083; AAZ27879.1; -; Genomic_DNA.
DR   RefSeq; YP_269306.1; -.
DR   GeneID; 3522138; -.
DR   GenomeReviews; CP000083_GR; CPS_2591.
DR   KEGG; cps:CPS_2591; -.
DR   NMPDR; fig|167879.3.peg.2872; -.
DR   TIGR; CPS_2591; -.
DR   HOGENOM; Q481G3; -.
DR   OMA; Q481G3; LQKKRHS.
DR   BioCyc; CPSY167879:CPS_2591-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:HAMAP.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00534; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004522; Asn-tRNA-synth_IIb.
DR   InterPro; IPR002312; Asp-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA_bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   TIGRFAMs; TIGR00457; asnS; 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    466       Asparaginyl-tRNA synthetase.
FT                                /FTId=PRO_1000051388.
SQ   SEQUENCE   466 AA;  52401 MW;  D2D1030A3F062DD7 CRC64;
     MSVISITDVL AGNFPVNESI TIHGWIRTRR DSKAGISFLA LHDGSCFDAI QAIVPNELDN
     YESDVLKLTT GCSVKVTGIL VESPGKGQAF EIQATEVEVL GFVEDPDTYP MAAKRHSIEF
     LREQAHLRPR TNIGGAVTRV RNCLAQAVHR FLHSKGYFWI STPLITGSDC EGAGEMFRVS
     TLDMENLPRN DEGKVDYNKD FFGKETFLTV SGQLNVETYC NALSKVYTFG PTFRAENSNT
     TRHLAEFWMV EPEIAFADLS DAADLAEEML KYVFKAVLEE RPDDMAFFQQ RVDKTVLDRL
     NSVINTDFVR LDYTDAITIL ENCGKKFENQ VSWGVDLNSE HERYLAEEHF NGPVVLQNYP
     KDIKSFYMRL NDDGKTVAAM DILAPGIGEI IGGSQREERL DVLDSRLEEM GLDIADYGWY
     RDLRRYGTVP HSGFGLGFER LVAYATGMQN VRDVIPFPRT PNNAAF
//