(data stored in ACNUC29543 zone)

SWISSPROT: A5GRD8_SYNR3

ID   A5GRD8_SYNR3            Unreviewed;       202 AA.
AC   A5GRD8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Leucyl/phenylalanyl-tRNA--protein transferase {ECO:0000256|HAMAP-Rule:MF_00688, ECO:0000256|SAAS:SAAS00088489};
DE            EC=2.3.2.6 {ECO:0000256|HAMAP-Rule:MF_00688, ECO:0000256|SAAS:SAAS00384399};
DE   AltName: Full=L/F-transferase {ECO:0000256|HAMAP-Rule:MF_00688};
DE   AltName: Full=Leucyltransferase {ECO:0000256|HAMAP-Rule:MF_00688};
DE   AltName: Full=Phenyalanyltransferase {ECO:0000256|HAMAP-Rule:MF_00688};
GN   Name=aat {ECO:0000256|HAMAP-Rule:MF_00688,
GN   ECO:0000313|EMBL:CAK27447.1};
GN   OrderedLocusNames=SynRCC307_0544 {ECO:0000313|EMBL:CAK27447.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27447.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in the N-end rule pathway of protein
CC       degradation where it conjugates Leu, Phe and, less efficiently,
CC       Met from aminoacyl-tRNAs to the N-termini of proteins containing
CC       an N-terminal arginine or lysine. {ECO:0000256|HAMAP-
CC       Rule:MF_00688, ECO:0000256|SAAS:SAAS00088485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] =
CC         H(+) + N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu);
CC         Xref=Rhea:RHEA:50416, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC         Rhea:RHEA-COMP:12672, Rhea:RHEA-COMP:12673, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64719, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC         ChEBI:CHEBI:133044; EC=2.3.2.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00688, ECO:0000256|SAAS:SAAS01124580};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+)
CC         + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu);
CC         Xref=Rhea:RHEA:12340, Rhea:RHEA-COMP:9613, Rhea:RHEA-COMP:9622,
CC         Rhea:RHEA-COMP:12670, Rhea:RHEA-COMP:12671, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:65249, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC         ChEBI:CHEBI:133043; EC=2.3.2.6; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00688, ECO:0000256|SAAS:SAAS01124578};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a [protein] N-terminus + L-phenylalanyl-tRNA(Phe) = N-
CC         terminal L-phenylalanyl-[protein] + tRNA(Phe);
CC         Xref=Rhea:RHEA:43632, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699,
CC         Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10637, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78531, ChEBI:CHEBI:78597, ChEBI:CHEBI:83561;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00688};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00688,
CC       ECO:0000256|SAAS:SAAS00088483}.
CC   -!- SIMILARITY: Belongs to the L/F-transferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00688, ECO:0000256|SAAS:SAAS00571279}.
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; CT978603; CAK27447.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0544; -.
DR   EnsemblBacteria; CAK27447; CAK27447; SynRCC307_0544.
DR   KEGG; syr:SynRCC307_0544; -.
DR   eggNOG; ENOG4108R4Z; Bacteria.
DR   eggNOG; COG2360; LUCA.
DR   HOGENOM; HOG000102326; -.
DR   KO; K00684; -.
DR   OMA; YRQGIFP; -.
DR   BioCyc; SSP316278:G1GJL-531-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008914; F:leucyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00688; Leu_Phe_trans; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR004616; Leu/Phe-tRNA_Trfase.
DR   PANTHER; PTHR30098; PTHR30098; 1.
DR   Pfam; PF03588; Leu_Phe_trans; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR00667; aat; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRD8.
DR   SWISS-2DPAGE; A5GRD8.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00688,
KW   ECO:0000256|SAAS:SAAS00461224};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00688,
KW   ECO:0000256|SAAS:SAAS00461240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00688,
KW   ECO:0000256|SAAS:SAAS00461218, ECO:0000313|EMBL:CAK27447.1}.
SQ   SEQUENCE   202 AA;  22407 MW;  1A5ECD759533B5EF CRC64;
     MNDLLAAYAA GWFPMAEGPD RALGLFRARN RALIPLDQRF HVPRSLRRQL RPGRFELKLN
     SAFAAVVDGC ADRPSTWISL ELRAIYQELH RLGWAHSIEA WDAHGLAGGQ LGLAIGRCWI
     GESMFHSRPH ASNVVLVQLQ SALRQGGFEL FDVQLSNPHL ERFGCFELSD ADYTSCLAKA
     VQQPARLQIG SSAVSSGAWM PR
//

If you have problems or comments...

PBIL Back to PBIL home page