ID A0A0F4ZG42_9PEZI Unreviewed; 1221 AA.
AC A0A0F4ZG42;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme C-terminal subdomain domain-containing protein {ECO:0000259|SMART:SM01228};
GN ORFNames=TD95_001591 {ECO:0000313|EMBL:KKA29497.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29497.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29497.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29497.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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 -!- 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:KKA29497.1}.
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DR EMBL; LAEV01000801; KKA29497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZG42; -.
DR OrthoDB; 49088at2759; -.
DR Proteomes; UP000033483; 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; 1.25.40.60; -; 1.
DR Gene3D; 3.40.50.1910; -; 1.
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; 1.
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:UP000033483}.
FT DOMAIN 1116..1187
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 1221 AA; 134972 MW; 302670614E28EFF2 CRC64;
MDIWQAMAGY LANVVTAGEK TGGGSSASSK MKVLLLDSDT ISIVSTATTQ SALLNHEIYL
IDRLDNPNRE KMRHLRCICL VRPSPDSIQM LIEELREPKY GEYFLFFTNV VKKSSLERLA
EADDHEIVKQ VQEQFADFVV INPDLFSFDL SAPSHRIWGG GAEHWNPDTL QRCSEGLTAV
LLALKKKPLI RYTKTSGMAK KLATEVRYRM TQEEQLFDFR RVDTPPILLI LDRREDPVTP
LLTQWTYQAM VHHMLGIKNG RVDLSNVPDI RPELKEVVLS QDQDPFFKKN MYLNFGDLGG
NIKDYVEQYQ SKTKSSADLE SIDDMKRFIE EYPEFRKLAG NVSKHVTLVS ELSRRVGTEN
LLEVSELEQS LACNDSHNSD LRSIQALIPN PQVSSESKVA LVALYALRYS KSPNSAVPVL
TDLLVAAGGV SPYRAAIVER VLRYQGSLSQ PQTQAGITDL FEGGGILGSR GLRGLKGVEN
VYTQHNPILE STLQNLIKGR LRDQQYPFLE GSTRDKPQDI IVFIVGGATY EEAKTVASIN
ANSPGVRVVL GGTTIHNAGT FMDEVEEAVS GWPSRFDVVV IGGGHAGAEA SAAAARSGAK
TALVTPKIDN LGVCSCNPSF GGIGKGIIIR EIDALDGVAG RIIDKAGVQF KVLNKVKGPA
VWGPRAQIDR KLYNRYMTEE LTNYTNLDVV TGKAADIIVD HSSPSGSYGA ITGIRLESGE
VIHTRSVVIT TGTFLGGEIH IGLEAYPSGR IGEAATFGLS KSLKNAGFAL GRLKTGTPPR
LQRQSIKFDV LQEQLGDDPP MPFSFMNERV AVTDQLSCFM TYTNQRSHDV VRENLDKTIH
IRETVKGPRY CPSLESKVIK FAEKDRHLVW IEPEGFDTDV FYPNGLSMTI PAEAQERLLK
TIFGLEDVVM LQPGYGVEYD YVDPRSLKAT LETKAISGLF LAGQINGTTG YEEAAGQGII
AGTNAGRAAQ NLTQLTLSRS DGYIGVMIDD LITKGVSEPY RMFTTRSEYR ISSRADNADQ
RLTALGRAHG IVGDARWDRF SRDRADIDAL LGVLDGFRLS APEWIRRGFR VRHDTQRRSA
LEVLRTPDSG LAQLEELVPQ ITTYSTDVQR RVGIEAVYAP YMDSQVSWRR SLEREENMKL
PLDLDYNSVC GLSFHEREIL KATRPESIAQ ARRLEGMTPS GSLRLLKHVM VGVKREAAFK
DVQANLVREQ GLQSDSSAGL V
//
