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MNMG2_FUSNN
ID   MNMG2_FUSNN             Reviewed;         633 AA.
AC   Q8RI88;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG 2 {ECO:0000255|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A 2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Name=mnmG2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA2 {ECO:0000255|HAMAP-Rule:MF_00129}; OrderedLocusNames=FN1723;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC       certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
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DR   EMBL; AE009951; AAL93838.1; -; Genomic_DNA.
DR   RefSeq; NP_602539.1; NC_003454.1.
DR   AlphaFoldDB; Q8RI88; -.
DR   SMR; Q8RI88; -.
DR   STRING; 190304.FN1723; -.
DR   PRIDE; Q8RI88; -.
DR   EnsemblBacteria; AAL93838; AAL93838; FN1723.
DR   KEGG; fnu:FN1723; -.
DR   PATRIC; fig|190304.8.peg.212; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_0; -.
DR   InParanoid; Q8RI88; -.
DR   OMA; FRPGYAI; -.
DR   BioCyc; FNUC190304:G1FZS-223-MON; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   Gene3D; 1.10.150.570; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR044920; MnmG_C_subdom.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT   CHAIN           1..633
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG 2"
FT                   /id="PRO_0000117104"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         181
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         277..291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         374
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   633 AA;  71318 MW;  2EC1E8EFA5BF3B04 CRC64;
     MQEFDIIVVG GGHAGCEAAL ASARMGMKTA IFTISLDTIG VMSCNPSLGG PAKSHLAREI
     DALGGEMGRN IDKTFIQIRV LNTRKGPAVR SLRAQADKMA YANEMKKTLE HTDNLSVIQG
     MVSELVVEEE NGKKIIKGIK IREGLEYKAK AVIIATGTFL RGLIHIGEIN FSAGRMGELS
     SEELPLSLEK IGLKLERFKT GTPTRIDGRT IDYSVLEEQP GDKSQVLKFS NRTKDEDALS
     RRQISCYIAH TNEKVHEIIR NAKERSPLFN GTIQGLGPRY CPSIEDKIFR YPDKNQHHLF
     LEREGYETNE IYLGGLSSSL PVDVQEEMLK NIKGFENAKI MRYAYAIEYD YVPPEEIKYT
     LESRTVENLF LAGQINGTSG YEEAGAQGLM AGINAVRKLR NEEPVILDRA DSYIGTLIDD
     LVSKGTNEPY RMFTARSEYR LYLREDNADL RLTKLGYELG LVPEEEYQRV EKKRKDVKII
     TEILAKTNVG PSNPRVNEIL LKRGENPIKD GSTLLELLRR PEVSFEDIKY ISEEIRGIDL
     QGYDHDTTYQ VEITVKYEGY INRALKMIEK HKSMENKKIP VDIDYDDLKT IPKEAKDKLK
     RIKPINIGQA SRISGVSPAD IQAILIYLKM RGN
 
 
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