ID YGFZ_VIBVY Reviewed; 324 AA.
AC Q7MHM7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN OrderedLocusNames=VV2842;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC95606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC95606.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043877319.1; NC_005139.1.
DR AlphaFoldDB; Q7MHM7; -.
DR SMR; Q7MHM7; -.
DR STRING; 672.VV93_v1c25500; -.
DR KEGG; vvy:VV2842; -.
DR PATRIC; fig|196600.6.peg.2830; -.
DR eggNOG; COG0354; Bacteria.
DR HOGENOM; CLU_007884_6_1_6; -.
DR Proteomes; UP000002675; Chromosome I.
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 Gene3D; 2.40.30.160; -; 1.
DR Gene3D; 3.30.70.1630; -; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
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 InterPro; IPR048451; YgfZ_barrel.
DR NCBIfam; TIGR03317; ygfZ_signature; 1.
DR PANTHER; PTHR22602:SF0; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22602; UNCHARACTERIZED; 1.
DR Pfam; PF21130; YgfZ_barrel; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Folate-binding; tRNA processing.
FT CHAIN 1..324
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_0000262907"
FT BINDING 184
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ SEQUENCE 324 AA; 35527 MW; 496561680F2B5C76 CRC64;
MQSTQPIQRC ALGSQQALPE LAVSLLDNLG LITMTGNDKK SYLQGQVTCD VVSLEADQVT
WGGHCDAKGK LWSAFRLFHY GDGYAMLQDK SAIDVELREL KKYAVFAKVE INVSDAILLG
VCGVQAEQAI AKLTNNAEAA VATFAQGTAV KISPQRWLLV VDANQQDEVL AMLATAPLCD
HALWDLYDIL EVSPRIPAFA QNEHIPQAVN LQAVNGISFK KGCYTGQETV ARAKYRGINK
RALYRLSGAI EPSAPETTIS LERSVGDNWR AAGEALVSYH FDDGRATGLF VLPNDLEPET
QFRLAGQSEQ LWQREPLPYS LDDE
//
