ID A0A166LEM0_9PEZI Unreviewed; 690 AA.
AC A0A166LEM0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glucose inhibited division protein A {ECO:0000313|EMBL:KZL63431.1};
GN ORFNames=CT0861_01211 {ECO:0000313|EMBL:KZL63431.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL63431.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL63431.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL63431.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL63431.1}.
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DR EMBL; LFIV01000393; KZL63431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166LEM0; -.
DR STRING; 708197.A0A166LEM0; -.
DR OrthoDB; 5486689at2759; -.
DR Proteomes; UP000076552; 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 PRINTS; PR00411; PNDRDTASEI.
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:UP000076552}.
FT DOMAIN 585..656
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 666..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 75388 MW; 98F7762C52E0629B CRC64;
MRSLPAALKL RPRNAARGLR YLHPSRTLGR RGFADVAEGA RPFDVVVVGG GHAGAEACAA
AARAGARTAL VTPKIENLGT CSCNPSFGGV GKGIILREID ALDGLAGRVI DKAGVQFRVL
NRAKGPAVWG PRAQIDRKLY QKHMREELET YPNLSIVLGS VSDIVTGANP DTTGSAPTKI
TGVRLESGEV LPTSAVIITT GTFLSAEIHI GMKAYPAGRI GEDASFGLSK SLKDAGFRLG
RLKTGTPPRI AKDSIDYTHL ERQPGDDPPM PFSFLNDRVA VEEQMSCHVS YTNEATHAIV
RDNLDKTIHI RETIRGPRYC PSLEAKIVRF SDKDRHIVWL EPEGFDSDLV YPNGLSMTVP
PEAQERILRS IPGLENCVMT QVGYGVEYDY IDPRSLKATL ETKNIAGLFL AGQINGTTGY
EEAAGQGIIA GINAGRSALG LAPAAVSRAD GYIGIMIDDL ITKGVTEPYR MFTTRSEYRL
TSRADNADLR LTEQGREWGV VSDKRWTAFN DEKQQMNHLM ALLSSTNKSS PEWSRQGFQV
KEDTTRRDAT DMLRLRNVTM DQVAAAVPGV ERFPERIKSR VHIEATYAPF IRRQLAERKV
FARDESLRLP ASIDYDKVPG LAMAEKAVLK ATMPETLAQA RRLEGITPSG CIRLLGYVQR
QQRSTAMASV SRPWRTKKEA PGGEGVSPLP
//
