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Database: UniProt/TrEMBL
Entry: A1KSZ0_NEIMF
LinkDB: A1KSZ0_NEIMF
Original site: A1KSZ0_NEIMF 
ID   A1KSZ0_NEIMF            Unreviewed;       787 AA.
AC   A1KSZ0;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   11-JUN-2014, entry version 61.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
GN   Name=pheT; OrderedLocusNames=NMC0681;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 /
OS   DSM 15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C.,
RA   Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E.,
RA   Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S.,
RA   Unwin L., Whitehead S., Quail M.A., Achtman M., Barrell B.G.,
RA   Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 B5 domain.
CC   -!- SIMILARITY: Contains 1 FDX-ACB domain.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
CC   -!- SIMILARITY: Contains B5 domain.
CC   -!- SIMILARITY: Contains Bdomain.
CC   -!- SIMILARITY: Contains FDX-ACB domain.
CC   -!- SIMILARITY: Contains tRNA-binding domain.
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DR   EMBL; AM421808; CAM09971.1; -; Genomic_DNA.
DR   RefSeq; YP_974770.1; NC_008767.1.
DR   ProteinModelPortal; A1KSZ0; -.
DR   STRING; 272831.NMC0681; -.
DR   EnsemblBacteria; CAM09971; CAM09971; NMC0681.
DR   GeneID; 4675727; -.
DR   KEGG; nmc:NMC0681; -.
DR   PATRIC; 20351151; VBINeiMen17609_0830.
DR   eggNOG; COG0073; -.
DR   HOGENOM; HOG000292085; -.
DR   KO; K01890; -.
DR   OMA; NYVMIEL; -.
DR   OrthoDB; EOG6CCH1J; -.
DR   BioCyc; NMEN272831:GJDX-665-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.56.20; -; 1.
DR   Gene3D; 3.30.70.380; -; 1.
DR   Gene3D; 3.50.40.10; -; 1.
DR   HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu.
DR   InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR   InterPro; IPR005121; PheS_beta_Fdx_antiC-bd.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR005147; tRNA_synthase_B5-dom.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF03484; B5; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00874; B5; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54991; SSF54991; 1.
DR   SUPFAM; SSF56037; SSF56037; 1.
DR   TIGRFAMs; TIGR00472; pheT_bact; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; RNA-binding; tRNA-binding.
FT   DOMAIN       39    149       tRNA-binding (By similarity).
FT   DOMAIN      400    475       B5 (By similarity).
FT   DOMAIN      694    786       FDX-ACB (By similarity).
FT   METAL       453    453       Magnesium (By similarity){EA2}.
FT   METAL       459    459       Magnesium; via carbonyl oxygen (By
FT                                similarity){EA2}.
FT   METAL       462    462       Magnesium (By similarity){EA2}.
FT   METAL       463    463       Magnesium (By similarity){EA2}.
SQ   SEQUENCE   787 AA;  86038 MW;  0F5E0847C696C4D0 CRC64;
     MQFSYSWLKT QADTELSADK LEHLLTMSGL EVEEAETAAP AFAGVVVAEV KSVEKHPDAD
     RLNVTRVDAG TGELVQIVCG APNVKAGIKV PCSLPGAVLP GNFKIKPTKM RGVPSNGMLC
     STNELGLPDD GVNGLHILPE DAPVGINIRE YLDLDDTLFT LKITPNRADC LSVKGIAREV
     SALTGCAFRQ PEIHTAPITG SRKQPVQINA PADCGRFISR VIENVNAKAA TPDWMKQRLE
     RSGIRSISVL VDIGNYVMLE IGQPMHVFDA DKLSGSLHIR RAREGETLEC LNEKTVSLSE
     NTLVVADEKG ALSLAGLMGG AASAVSDGTQ NIVLEAAWFA PEIIAGKSRQ YGFGSDSSFR
     FERGVDYRLQ ADAIERATEL VLQICGGAAG EMVEAQGELP EAKQVGLRLD RLKTVLGVDI
     PAEQVETILQ HLGLQPEKTA EGFRVTAPSF RFDIEIEADL IEEIGRVYGY ENIPDDYTSG
     RLKMLELPET RRSRFAVYNE MAARGYREVV SYAFVDEQWE QDFAANADPI RLQNPLAAQY
     AVMRSTLIGG LVEILQNNLN RKQNRVRVFE IARVFGKGSD GRFVQNERIG GLWYGAAMPE
     QWGGKTRNAD FYDIKADVEN LLKNKAVEFV KTGYPALHPG RAANIVSDGK VIGFVGELHP
     KWLQKYDLPQ APLVFEIDMA AVLECGKTRY RAVSKFQPVR RDLAFVMPEA MSHDDLLLVL
     KGAANKLVQE ISVFDVYRGM GLPEGMKSVA VKVILQDMEN TLTDEAVEPL IGKLIGAATA
     AGARLRS
//
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