YGFZ_PECAS
ID YGFZ_PECAS Reviewed; 333 AA.
AC Q6D961;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN OrderedLocusNames=ECA0758;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73672.1; -; Genomic_DNA.
DR RefSeq; WP_011092365.1; NC_004547.2.
DR AlphaFoldDB; Q6D961; -.
DR SMR; Q6D961; -.
DR STRING; 218491.ECA0758; -.
DR EnsemblBacteria; CAG73672; CAG73672; ECA0758.
DR KEGG; eca:ECA0758; -.
DR PATRIC; fig|218491.5.peg.756; -.
DR eggNOG; COG0354; Bacteria.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR OrthoDB; 1984573at2; -.
DR Proteomes; UP000007966; Chromosome.
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..333
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_0000262888"
FT BINDING 33
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT BINDING 195
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ SEQUENCE 333 AA; 36320 MW; C712CD298C27CDB1 CRC64;
MVNQHTAHQL PFASQLPFAS TQLAATLISL DDWALATLVG PDTVKYLQGQ VTADVGALPD
NGHILCAHCD AKGKMWSNLR LFHHGEGFAF IERRNLRDVQ LSELKKYAVF SKTAIAPDDN
TILLGAAGAG IRELLASVFS QLPDAEHPVV QHEGATLLHF AHPAERFLLV LSPEPSASLL
EQLGDKVSLN DSRQWLTLDI EAGQPIIDSA NSAQFIPQAT NLQALNGISF SKGCYTGQEM
VARAKYRGAN KRALYWLAGK ANKVPQAGDD LELQLGENWR RTGTVLAASQ LQNGDVWVQA
VLNNDLNAEN TLRVRDDADS QLTVQPLPYE ITD