(data stored in ACNUC7421 zone)

SWISSPROT: A0LFC7_SYNFM

ID   A0LFC7_SYNFM            Unreviewed;       800 AA.
AC   A0LFC7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00283};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00283};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00283};
GN   Name=pheT {ECO:0000256|HAMAP-Rule:MF_00283};
GN   OrderedLocusNames=Sfum_0429 {ECO:0000313|EMBL:ABK16129.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16129.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16129.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate +
CC         H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413,
CC         Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215;
CC         EC=6.1.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00283,
CC         ECO:0000256|SAAS:SAAS01124689};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00283};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00283};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00283, ECO:0000256|SAAS:SAAS01133281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283,
CC       ECO:0000256|SAAS:SAAS00710994}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC       subunit family. Type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00283, ECO:0000256|SAAS:SAAS00570605}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000478; ABK16129.1; -; Genomic_DNA.
DR   RefSeq; WP_011697302.1; NC_008554.1.
DR   STRING; 335543.Sfum_0429; -.
DR   EnsemblBacteria; ABK16129; ABK16129; Sfum_0429.
DR   KEGG; sfu:Sfum_0429; -.
DR   eggNOG; ENOG4105C6A; Bacteria.
DR   eggNOG; COG0072; LUCA.
DR   eggNOG; COG0073; LUCA.
DR   HOGENOM; HOG000292087; -.
DR   KO; K01890; -.
DR   OMA; LTPNRSD; -.
DR   OrthoDB; 53568at2; -.
DR   BioCyc; SFUM335543:G1G7I-437-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00769; PheRS_beta_core; 1.
DR   CDD; cd02796; tRNA_bind_bactPheRS; 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_sf.
DR   InterPro; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
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; IPR041616; PheRS_beta_core.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR033714; tRNA_bind_bactPheRS.
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   Pfam; PF17759; tRNA_synthFbeta; 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   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;
DR   PRODOM; A0LFC7.
DR   SWISS-2DPAGE; A0LFC7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00461971, ECO:0000313|EMBL:ABK16129.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00461962};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00710959};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00461946, ECO:0000313|EMBL:ABK16129.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00244536};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00244576};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00089649};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00283,
KW   ECO:0000256|SAAS:SAAS00462106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209,
KW   ECO:0000256|SAAS:SAAS00104020};
KW   tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209,
KW   ECO:0000256|SAAS:SAAS00469761}.
FT   DOMAIN       39    147       TRNA-binding. {ECO:0000259|PROSITE:
FT                                PS50886}.
FT   DOMAIN      401    476       B5. {ECO:0000259|PROSITE:PS51483}.
FT   DOMAIN      707    800       FDX-ACB. {ECO:0000259|PROSITE:PS51447}.
FT   METAL       454    454       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00283}.
FT   METAL       460    460       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00283}.
FT   METAL       463    463       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00283}.
FT   METAL       464    464       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00283}.
SQ   SEQUENCE   800 AA;  87637 MW;  FA9B36673E083C48 CRC64;
     MIVSLKWLRD YVETSLSVEE LTHRLTMVGL EIDGCHPLHP CLGRVVTARV EKVEPHPRAD
     RLSVCEVSDG HGRYSVVCGA PNVKAGQIVP LALPGAELAS GVKIGQATIR GVASLGMLCS
     QKELGLGEDA SGIWPLPGEV PVGVPLSEAL DLDDTILDVA VTPNRGDCLS IVGIAREIAA
     ISGVRLRYPA VACRETGPEV DSLASVRIDA PDGCPRYAAR VIEGITVGPS PQWLKDRLEA
     VGLRSINNIV DVTNYILMEL GQPLHAFDFD LLREQRIVVR YAREGERFTT LDGTERILFG
     DTLMICDGVG PVAVAGIMGG LDSEIGARTR RVLIESACFE PRCIRRSSRK LGLRTESSYR
     FERGVDPEGV IRALDRAAQL MVEVGGGDLA TGRVDAYPRP AEKPVLVLRT DRVNRFLGTD
     LTPAEMAGAL RSIEMQVEEN GGGLEVIPPT FRPDITREVD LAEEIARLAG YDRVPVTYPE
     VRMEAASLDR HLQARMDIKG YLEGAGFFEA INYSFVSMES LRKLKFPAGD RRLNPVQIRN
     PLSEEQAVMR TTLVPSLLQT ARYNFDHKND DLKLFELSKV FLPVEGAPLP EEVHEVAGIL
     AGKRSLNLLY GGDDDVDYAD AKGIVEGILE LLHIEGVRFD SEAPPPYLDA ACAATIMHGE
     LNLGAVGRVA ADVRAAFDLK KPVFVFDLDF ERLFGIARPP AFFSSLPKFP SVSRDMALVV
     DESVPVQGPF DFIRSQGEAL LEHIDIFDIY RDPQLGAGRK SIGYRLVYRA ADRSLTDEEV
     NRLHEGLVSK VLVEFDARLR
//

If you have problems or comments...

PBIL Back to PBIL home page