YGFZ_ALISL
ID YGFZ_ALISL Reviewed; 318 AA.
AC B6EKN9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN OrderedLocusNames=VSAL_I2535;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ80219.1; -; Genomic_DNA.
DR RefSeq; WP_012551007.1; NC_011312.1.
DR AlphaFoldDB; B6EKN9; -.
DR SMR; B6EKN9; -.
DR STRING; 316275.VSAL_I2535; -.
DR EnsemblBacteria; CAQ80219; CAQ80219; VSAL_I2535.
DR KEGG; vsa:VSAL_I2535; -.
DR eggNOG; COG0354; Bacteria.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR OrthoDB; 1984573at2; -.
DR Proteomes; UP000001730; 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; tRNA processing.
FT CHAIN 1..318
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_1000138068"
FT BINDING 28
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT BINDING 182
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ SEQUENCE 318 AA; 35204 MW; 7467DC034F2FC4EE CRC64;
MMSTLFPKLS IKKEDTLPAL AISELNDWAL ITMIGNDKKS YLQGQVTADV VTLPQDDITF
GGHCDAKGKL WSIFQLFNHN DGYALFQRRS AIETELTEIK KYSVFSKVDI AVGDDVLLGI
SGKKATDWVN KHTTTDANVR ACELGTFAKI SETQWLLVTT PEHKKNIINQ ESNTVLCDES
LWSLHTIQHG LPQLDNALSN AHIPQAMNLQ AVGGISFAKG CYTGQETVAR AKYRGINKRA
MYLLSGQSNS IPVAGDAIER SVGENWRKGG TIVSAYRFED GYTLALAILP NDLEEGTQFK
LQDSIWNKGN QPYSLDEE