ID A0A3E2HR83_SCYLI Unreviewed; 1114 AA.
AC A0A3E2HR83;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain domain-containing protein {ECO:0000259|SMART:SM01228};
DE Flags: Fragment;
GN ORFNames=B7463_g523 {ECO:0000313|EMBL:RFU35870.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU35870.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU35870.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU35870.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC {ECO:0000256|ARBA:ARBA00002739}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU35870.1}.
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DR EMBL; NCSJ02000004; RFU35870.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2HR83; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR Pfam; PF15365; PNRC; 1.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT DOMAIN 1015..1086
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU35870.1"
FT NON_TER 1114
FT /evidence="ECO:0000313|EMBL:RFU35870.1"
SQ SEQUENCE 1114 AA; 121587 MW; 918DF36586EA36C6 CRC64;
MSSSIASPQN NRHPQRRNLR GSYQNTQLDM NKLSQPTTPP RTPRRTHQFP QTSQNRAVLS
ADEGGSKQRS RNRNQQRNTM TSPAITKIDQ NTPPANGTQS GTKIIQGKTI NTPTAAFAGA
TFHASPAPSA LPIPSFYSKA DREEKARVRS ASSIHDITVS GSPFAPPSGP VSDGHTSPSS
LSPSRAHKGH YSRNSASGMF ALELDSSGNN DTPFGPAFST PYAERINAAR SANTPRQRFP
PPSQDTQRTV DNAEALKAYL FSGLSLPSST THHSSYNSSS LTPASSPHHR TYPPQAENTR
AAMSQLLQNT NFTGTQENRN LNLPVTSSRM SGLRKELNIT PTRTQNDHDN TYLNSPTPSR
MYSNHISNPN NPTTGFYSHS SSPVQIPSNR TTARSTNADL QGMEESLRRL LKLDPTGNRG
LDNSAIGTVT DPTVTIPNYT GDNDDGRSGW SQVFGYDHNV SASGIGCILF NRHGPYDVIV
IGGGHAXSEA CAGAARTGAR TALITPKLDN IGVCSCNPSF GGIGKGTMLR EIDALDGVAG
RIIDKAGVQF KVLNRKKGPA VWGPRAQIDR SLYKKYMREE LEAYPNLSIL AGSVADIIVS
HDEHTPGSKI TGVRLESGEI IPTNHVVITT GTFLGGEIHI GLQAYPAGRM DEAATFGLSK
SLKDAGFKLG RLKTGTPPRL DKKTINFDIL DAQSGDNPPM PFSFLNEKVA VQDQLLCYAT
YTNRATHDIA KANLDKSIHI RETVKGPRYC PSLESKVIRF SDKDRHIVWL EPEGFDSQII
YPNGISMTVP AEAQEQLLKT IKGLENVTML QPGYGVEYDY VDPRSLKSTL ETKAIRGLFL
AGQINGTTGY EEAAAQGIIA GINAALASQS KAPLVLSRGD GYIGIMVDDL ITKGVSEPYR
MFTSRSEYRM SSRADNADLR LTTKGREVGA VGDKRWASFS DEVAQMDQLR SALLRTQSSS
PGWIAAGFRV GNDSTRRTAF DVLRLSGVTI ENMASQVPEI MSYPERIRKR IEIEAVYAPY
VKQQRAAMKV FEKDEHLKLP VDLDYDQVHG LSMHEKDLLR QTRPESVGQA RRIEGMTPSG
CLRLLAHVQH KSRAAAKAIQ FEEMSLRKAE HVRI
//
