ID G9NKM8_HYPAI Unreviewed; 1141 AA.
AC G9NKM8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain domain-containing protein {ECO:0000259|SMART:SM01228};
GN ORFNames=TRIATDRAFT_290147 {ECO:0000313|EMBL:EHK48451.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK48451.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK48451.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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 -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC {ECO:0000256|ARBA:ARBA00009884}.
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:EHK48451.1}.
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DR EMBL; ABDG02000018; EHK48451.1; -; Genomic_DNA.
DR RefSeq; XP_013946620.1; XM_014091145.1.
DR AlphaFoldDB; G9NKM8; -.
DR STRING; 452589.G9NKM8; -.
DR GeneID; 25780025; -.
DR eggNOG; KOG1299; Eukaryota.
DR eggNOG; KOG2311; Eukaryota.
DR HOGENOM; CLU_006656_0_0_1; -.
DR OMA; MHAILRQ; -.
DR OrthoDB; 49088at2759; -.
DR Proteomes; UP000005426; 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 GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 2.
DR Gene3D; 3.40.50.2060; -; 1.
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 InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
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; PF00995; Sec1; 2.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 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:UP000005426}.
FT DOMAIN 1045..1116
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 1141 AA; 125950 MW; 1BCD2227E075F294 CRC64;
MDVSQAVSGY LSKMMLASGD SSSSKMKVLL LDKETISIVS TSITQSALLD YEIYLIDRLD
NAAREKMRHL RCICLVRPSS ETIQLLIDEL RDPKYGEYYL FFTNVAKKSA LERLAEADDH
EVVKVVQEHF ADYIVINPDL FSFNMSLPQQ RIWAGSPDKW NPDSLQRCSE GLIAVLLSLK
KKPLIRYEKS SSLATKLASE VRYLMTKEDQ LFDFRKVDTP PLLLILDRRE DPITPLLTQW
TYQAMVHGLL GIKNGRVDLS DVPDIRPELK EIVLSQDQDP FFKKNMFLNF GDLGGTIKEY
VEQYQSKTKN NANIESISDM KRFIEEYPEF RKLSGNVSNA LPMLMDLLVA AGNVSPRQSD
LVKKVLTYHS SLHTSDARGG ISDIFDSAGI FSGTANRFKG LKGVENVYTQ HSSLLEGTLQ
NLIKGRLKDQ QYPFVEDSVP TRDKPQDIIV FMVGGVTYEE AKMIAGVNAT MPGVRVVLGG
TTVHNTATFL EEVEDAVAFD VVVIGGGHAG AEACAAAARA GARTALVTPK LDNLGTCSCN
PSFGGIGKGT IIREIDALDG LAGRIIDKAG VQFHLLNRRK GPAVWGPRAQ IDRDLYKKYM
RSELESYPNL SIVLESVSDI VLTENKGSAE GSKGAIAGVR LENGEILQTG RVVITTGTFL
GGEIHIGLEA YPAGRIGEAA TTGLSKSLRD AGFQLGRLKT GTPPRLDKAS INFDILQQQF
GDNPPAPFSY LNTEVAVRDQ LTCSITFTND ASHKIVQDNL DKSIHIRETV KGPRYCPSLE
SKVIRFADKE RHIVWLEPEG FDNPIIYPNG LSMTIPAEAQ EQVLRSIRGL EQVKMLQPGY
GVEYDYVDPR GLKSTLETKA IDGLYLAGQI NGTTGYEEAA GQGIIAGMNA GRSALGLPGA
SLSRSDGYIG IMIDDLITKG VTEPYRMFTS RSEFRMAARA DNADLRLTQK GREWGVVSDH
RWSVFSDEKQ QILDLTKSLG AVSLAPEEWN QAGFQVKRSS QRRTGIDMLR LSNTGERIQL
DQLSSVVPEI LNYPARIRER VVIEAAYAPY IKMQAAERGQ FVNDENIRLP LDLDYDGIPG
LALSEKEVLR RTRPETLAQA RRAEGVTPSG CIRLLAYIRR QGSSTGALVG SERSPLEAQL
P
//
