ID   SYV_COLP3               Reviewed;         973 AA.
AC   Q488M6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Valyl-tRNA synthetase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valine--tRNA ligase;
DE            Short=ValRS;
GN   Name=valS; OrderedLocusNames=CPS_0738;
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   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As
CC       ValRS can inadvertently accommodate and process structurally
CC       similar amino acids such as threonine, to avoid such errors, it
CC       has a "posttransfer" editing activity that hydrolyzes mischarged
CC       Thr-tRNA(Val) in a tRNA-dependent manner (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: ValRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site (By
CC       similarity).
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 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; CP000083; AAZ27693.1; -; Genomic_DNA.
DR   RefSeq; YP_267488.1; -.
DR   GeneID; 3521952; -.
DR   GenomeReviews; CP000083_GR; CPS_0738.
DR   KEGG; cps:CPS_0738; -.
DR   NMPDR; fig|167879.3.peg.512; -.
DR   TIGR; CPS_0738; -.
DR   HOGENOM; Q488M6; -.
DR   OMA; Q488M6; TDQWYVS.
DR   BioCyc; CPSY167879:CPS_0738-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02004; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR002303; Val-tRNA_synth_Ia.
DR   InterPro; IPR011321; Val-tRNA_synth_Ia_C.
DR   InterPro; IPR019754; Val-tRNA_synth_Ia_N.
DR   InterPro; IPR019499; Val-tRNA_synth_Ia_tRNA-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.287.380; Val-tRNA_synth_Ia_C; 1.
DR   PANTHER; PTHR11946:SF5; tRNA-synt_val; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    973       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000224464.
FT   COILED      901    970       Potential.
FT   MOTIF        57     67       "HIGH" region.
FT   MOTIF       569    573       "KMSKS" region.
FT   BINDING     572    572       ATP (By similarity).
SQ   SEQUENCE   973 AA;  110937 MW;  F2650EE687C39838 CRC64;
     MLQQNNEQLL NLLPDKMMEK TFNPTDIEQS LYTSWEEQGY FSPTGEGDSY SIAIPPPNVT
     GSLHMGHAFQ QTIMDTLIRY QRMQGKNTLW QTGCDHAGIA TQMVVERKIA AEEDKTRHDY
     GREGFIDKIW EWKEESGGTI GKQMRRLGNS IDWSRERFTM DDGMSEAVQE VFVRLFEDDL
     IYRGKRLVNW DPKFHTAISD LEVENKDKKG HMWHLRYPLA NGAKTAEGLD YLVVATTRPE
     TMLGDTGVAV NPEDPRYKDL IGKQVLLPLV NRLIPIVGDD HADMEKGTGC VKITPGHDFN
     DNEVGKRHAL PQINILDKDA AILATAEVYD TKGEVCNAYD TGLPSEFAGM DRFVARKAIV
     AKFDELGLLV EVKDHDLVAP YGDRSGVIIE PLLTDQWYVR VEKLAGPAVD AVKDGQIEFV
     PKQYENMYFS WMNNIQDWCI SRQLWWGHRI PAWYDENEKV YVGRTEEEVR ANNDIAADMK
     LRQDDDVLDT WFSSALWTFS TLGWPKDTED LKTFHPTDVL VTGFDIIFFW VARMIMMTMH
     FNKDENGKAQ IPFKKIYMTG LIRDENGDKM SKSKGNVVDP LDMIDGISLE DLLQKRTGNM
     MQPKLAKKIE KLTRKEYPEG IEAHGTDALR FTLTSVATTG RDISWDMKRL EGYRNFTNKL
     WNASRYVMMN TEEFDCGQSS PEGKAGDMEL SLADRWIIGQ FEQTVKTVHE AFDTYRFDLA
     SQALYEFTWN QFCDWYLELT KPVLFKENEA QQRGTRHTLV NVLEALLRLM HPIMPFITET
     IWQRVQPLSD FSKNGDSIMV QAFPQFDESK CDQQAIDDLE WVKQFIIAIR NIRGEMDISP
     SKELPVLLKN VNDNDQRRLD ENEQFLSSLA KLESITVLAD DEQGPASASA VVGDLSVLIP
     MAGLIDKEAE LARLDKAIEK LEKEAGRVRG KLGNENFVSK APAAVIEKEQ AKLADAESTL
     AKILEQKIQI AAL
//