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Database: UniProt
Entry: A0A1V3NRI8_9GAMM
LinkDB: A0A1V3NRI8_9GAMM
Original site: A0A1V3NRI8_9GAMM 
ID   A0A1V3NRI8_9GAMM        Unreviewed;       660 AA.
AC   A0A1V3NRI8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-JUN-2019, entry version 15.
DE   RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000256|HAMAP-Rule:MF_01102};
DE            Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000256|HAMAP-Rule:MF_01102};
DE   Includes:
DE     RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102};
DE              EC=2.1.1.61 {ECO:0000256|HAMAP-Rule:MF_01102};
DE   Includes:
DE     RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102};
DE              EC=1.5.-.- {ECO:0000256|HAMAP-Rule:MF_01102};
GN   Name=mnmC {ECO:0000256|HAMAP-Rule:MF_01102};
GN   ORFNames=B1C78_03140 {ECO:0000313|EMBL:OOG27661.1};
OS   Thioalkalivibrio denitrificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=108003 {ECO:0000313|EMBL:OOG27661.1, ECO:0000313|Proteomes:UP000189462};
RN   [1] {ECO:0000313|EMBL:OOG27661.1, ECO:0000313|Proteomes:UP000189462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALJD {ECO:0000313|EMBL:OOG27661.1,
RC   ECO:0000313|Proteomes:UP000189462};
RA   Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA   Sorokin D.Y., Muyzer G.;
RT   "Genomic diversity within the haloalkaliphilic genus
RT   Thioalkalivibrio.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5-
CC       methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble
CC       position (U34) in tRNA. Catalyzes the FAD-dependent demodification
CC       of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a
CC       methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form
CC       mnm(5)s(2)U34. {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00015108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC         methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569,
CC         Rhea:RHEA-COMP:10195, Rhea:RHEA-COMP:10197, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74454,
CC         ChEBI:CHEBI:74455; EC=2.1.1.61; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01102, ECO:0000256|SAAS:SAAS01118306};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01102, ECO:0000256|SAAS:SAAS00179145};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00015101}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC       {ECO:0000256|HAMAP-Rule:MF_01102, ECO:0000256|SAAS:SAAS00540894}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-
CC       methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00540888}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OOG27661.1}.
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DR   EMBL; MVBK01000018; OOG27661.1; -; Genomic_DNA.
DR   BioCyc; GCF_002000365:B1C78_RS03095-MONOMER; -.
DR   Proteomes; UP000189462; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro.
DR   GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_01102; MnmC; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR008471; MnmC-like_methylTransf.
DR   InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05430; Methyltransf_30; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000189462};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423465};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01102, ECO:0000256|SAAS:SAAS00015112};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423462};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00015105, ECO:0000313|EMBL:OOG27661.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423464};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00015110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189462};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423457};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423476, ECO:0000313|EMBL:OOG27661.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423459}.
FT   DOMAIN      121    239       Methyltransf_30. {ECO:0000259|Pfam:
FT                                PF05430}.
FT   DOMAIN      267    630       DAO. {ECO:0000259|Pfam:PF01266}.
FT   REGION        1    241       tRNA (mnm(5)s(2)U34)-methyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01102}.
FT   REGION      270    660       FAD-dependent cmnm(5)s(2)U34
FT                                oxidoreductase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01102}.
SQ   SEQUENCE   660 AA;  70720 MW;  CBB59BE1EE4FB353 CRC64;
     MASATDSPAG FRPLDPAPLT LRDGSPWCAR YGDVYYSPGE GAQESAQVFL AANGLPERWR
     DGERFTVGET GFGTGLNFLL TWDLWRSRPG RGWLHYLSTE LHPFTPPDMA RLMGALPAGL
     RRLGEQLLAQ YPEPVSGYHR LVFPDDRVSL TLLFGDATET LAGCHARVDA WYLDGFAPAR
     NPGLWNEALY AQLARLTPPG GTLASFTAAG HVRRGLEAAG FRIVRQPGFG AKRERITGVC
     ESLPQSVDVR PPWLRWPEGA DVSERRAAVI GAGLAGTSTA LALSRRGWDV TVLDSGPGPA
     AGASGNPAGI IMAHLSADHG VVSRFTLQAA EFAWRWIESV AACGHPIPRD RCGALWLADG
     ERLRLRLDRI AERLALPHTL MQRVDAPQAA ELAGVPLTLG GLYLPRAGWV DPSALCRGQL
     EAASARLVTG VQVSSLRRTG DAWHVLDANG KSVVEAPQVV LANGLGLPAL HPGIETRPLR
     GQLGIMSPAP STQGLRRILC YEGYVTPATP AGHVFGATYV RGDTGTDLRA GEHARNLSDL
     ARVWPAALSN GAPANAGRAA VRYNAAGRLP LVGPLPRMDA FEAAYADLHH GRSWDHYPDA
     PCLPGVYATL AHGSRGLTTT PLAAEVLASL MHGDPLPLSL DLVEALHTAR ERVRQLKRRP
//
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