(data stored in SCRATCH zone)

HOGENOM: PROM1_1_PE1006

ID   PROM1_1_PE1006                       STANDARD;      PRT;   824 AA.
AC   PROM1_1_PE1006; A2C259;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phenylalanyl-tRNA synthetase beta chain; EC=6.1.1
DE   20;AltName: Full=Phenylalanine--tRNA ligase beta chain; (PROM1_1.PE1006).
GN   Name=pheT; OrderedLocusNames=NATL1_10111;
OS   PROCHLOROCOCCUS MARINUS STR. NATL1A.
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROM1_1.PE1006.
CC       Prochlorococcus marinus str. NATL1A, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:A2C259_PROM1
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 chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta chain
CC       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   -!- GENE_FAMILY: HOG000292087 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A2C259; -.
DR   EMBL; CP000553; ABM75569.1; -; Genomic_DNA.
DR   RefSeq; YP_001014834.1; NC_008819.1.
DR   ProteinModelPortal; A2C259; -.
DR   STRING; A2C259; -.
DR   GeneID; 4780615; -.
DR   GenomeReviews; CP000553_GR; NATL1_10111.
DR   KEGG; pme:NATL1_10111; -.
DR   eggNOG; COG0072; -.
DR   OMA; ADKLRVC; -.
DR   ProtClustDB; PRK00629; -.
DR   BioCyc; PMAR167555:NATL1_10111-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
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; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR004532; Phe-tRNA-synth_IIc_bsu_bac.
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   Gene3D; G3DSA:3.50.40.10; B3_4; 1.
DR   Gene3D; G3DSA:3.30.56.20; B5; 1.
DR   Gene3D; G3DSA:3.30.70.380; Fdx_AntiC_bd; 1.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
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; SSF56037; B3_4; 1.
DR   SUPFAM; SSF54991; Fdx_AntiC_bd; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   SUPFAM; SSF46955; Putativ_DNA_bind; 1.
DR   TIGRFAMs; TIGR00472; PheT_bact; 1.
DR   PROSITE; PS51483; B5; 1.
DR   PROSITE; PS51447; FDX_ACB; 1.
DR   PROSITE; PS50886; TRBD; 1.
DR   HOGENOMDNA; PROM1_1.PE1006; -.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; RNA-binding; tRNA-binding.
SQ   SEQUENCE   824 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKVSVSWLKD LVEFNNDIDE LSEKLSMTGF EVESLEDISE QAKNVVIGFV EEITPHPNAE
     KLKVCSVDVG LPKKLSIVCG APNVKAGFHV LVAKVGAYLS SKSLKIKLSN LRGVESEGMI
     CSLEELGIES SNEGIEILEE NEATIPPIGT NAVDYLCLND TIIELAITAN RPDGMSMVGI
     AREISTITNS KLTLPTLNYN EDFNIFEPKI SDKETIGVDC IYSITYIDSI DNTGKTNKNI
     FNKLSSLKQN CINPVVDITN YLMLEQGQPL HAFDADLLDN IIGRKVIPND FGIRNGKEGE
     LFVALDKKEY KINPTIKLIT CDDIPIAIAG VIGGNNSSVS DKTTRIWLEA AVFTPTSIRN
     SSREIGLRTD ASSRYEKGIS SNMTTAVSKR ASDLISVQLG GDNISSYVNT DFKKKSISVN
     LRMDKINSVL GKLSSSDSNI VNNNSTKLRY LNEDEIETLL SKLGLILTSN NSGWNVQVPP
     YRSSDLTREI DLIEEIARLI GYDNFDSNMP DPLEPGVLSP TKLVERRLRN SFIHNGFQEV
     VTSSLVGPEN TDDNAVLIKN PLLSETSRLR TNVWDEHLKI LQRNVSFGAE GCWIFEIAKT
     YKKDKECFVE TNLLSGALTG SKRLSKWGGA SKQLTLDYFE ARGKLKQSLD VLGVETIDKQ
     LTDKDFMHPG RTSELFVEGK SIGFFGQIHP SLSEKFDLIK ETYLFNLDFD SLIKAATRKT
     NWTRIYKDYP TVPYMERDIA LIHSKKYSSL EIMGLIKKTG RPLLEKVELI DRYEGSSMPE
     DAISQAFRIR YRDAKKTLVE EDINPIHEKI RNALKEKIKA ELRS
//

If you have problems or comments...

PBIL Back to PBIL home page