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YGFZ_PHOPR
ID   YGFZ_PHOPR              Reviewed;         329 AA.
AC   Q6LMR1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=PBPRA3100;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- FUNCTION: Folate-binding protein involved in regulating the level of
CC       ATP-DnaA and in the modification of some tRNAs. It is probably a key
CC       factor in regulatory networks that act via tRNA modification, such as
CC       initiation of chromosomal replication. {ECO:0000255|HAMAP-
CC       Rule:MF_01175}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01175}.
CC   -!- SIMILARITY: Belongs to the tRNA-modifying YgfZ family.
CC       {ECO:0000255|HAMAP-Rule:MF_01175}.
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DR   EMBL; CR378673; CAG21416.1; -; Genomic_DNA.
DR   RefSeq; WP_011219674.1; NC_006370.1.
DR   AlphaFoldDB; Q6LMR1; -.
DR   SMR; Q6LMR1; -.
DR   STRING; 298386.PBPRA3100; -.
DR   EnsemblBacteria; CAG21416; CAG21416; PBPRA3100.
DR   KEGG; ppr:PBPRA3100; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   OrthoDB; 1984573at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01175; tRNA_modifying_YgfZ; 1.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR023758; tRNA-modifying_YgfZ.
DR   InterPro; IPR045179; YgfZ/GcvT.
DR   InterPro; IPR017703; YgfZ/GcvT_CS.
DR   PANTHER; PTHR22602; PTHR22602; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR03317; ygfZ_signature; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Folate-binding; Reference proteome; tRNA processing.
FT   CHAIN           1..329
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262893"
FT   BINDING         32
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         190
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   329 AA;  36410 MW;  9664C98F48ED871E CRC64;
     MSIEFNALNF KKVALAAQDK LPKLALINLD DWGLITLIGD DKKSYLQGQV TCDVVSLPIN
     ASIFGAHCDA KGKMRTIFRL FNHNEGYGFL QRKSVMEIQL PELKKYAVFS KVDIEASSDV
     LLGLSGEQAQ AVVEQHFPGD GDVRVITAGT AIKVDDDRWL FAIAPEQAEQ LINTLVETHN
     NVQLSDSTLW DLYDVLYAIP RIDAVTALEF IPQAVNLQAV DGISFKKGCY TGQETVARAK
     YRGINKRAMY IVTGEATQFP FTGDALERSV GDNWRKGGTL LASYLYADGQ AIALVVLPND
     LDEATQFRLA DQPEAIWTQL DLPYSLDDK
 
 
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