ID F4WRP4_ACREC Unreviewed; 804 AA.
AC F4WRP4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
DE Flags: Fragment;
GN ORFNames=G5I_08497 {ECO:0000313|EMBL:EGI63051.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI63051.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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}.
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DR EMBL; GL888292; EGI63051.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WRP4; -.
DR STRING; 103372.F4WRP4; -.
DR eggNOG; KOG2311; Eukaryota.
DR InParanoid; F4WRP4; -.
DR Proteomes; UP000007755; 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 InterPro; IPR032016; DUF4796.
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; IPR047001; MnmG_C_subdom.
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; PF16044; DUF4796; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF21680; GIDA_C_1st; 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:UP000007755}.
FT DOMAIN 751..804
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT NON_TER 804
FT /evidence="ECO:0000313|EMBL:EGI63051.1"
SQ SEQUENCE 804 AA; 90733 MW; 31EFBD190BA0A5DC CRC64;
MNNDPGIICF RHCKTKNVFC MQIPAMCPVC SSQMQNFIVD PFRVPCPFAN AIHNPTSVVI
RPSRGSFLDD YDVTRDDLHI GIVNSSGGIV EFDKEGLIEN DITKWTDCIV LELIPTAWTA
QWDEALLLMS KDLKWKSINY DVINMNCFNF VLEFFNNLRY RDLRFESKEE LCERLILSKM
YKAMQYVSLH RTLKDQEYLL QLINMNKTKF DVIVVGGGHA GTEASAAAVR MGAKTLLVTQ
KKSTIGEMSC NPSFGGIGKG HLMREVDALD GVCCRICDIS GIYYRVLNKS KGPAVWGLRA
QIDRKLYKKH LQAELFNMPR LHIYESSVEN LILENDSLSC QGVILRDGTK MFGDAVVITT
GTFLKGQINI GLEKRPAGRL NDEPSIGLAN TLDRLGFRIG RLKTGTPPRL EKESIDFTKC
TAYPPDDSPI PFSFMSDNVW LPPDKQILTH LTYTNEDVAK IVKDNMHCNL HVTEEITGPR
YCPSIESKIL RFKALKHQIW LEPEGLDSPL IYPSGLSCTL PEEKQVELVK CIPGLENARL
VKPGYGVEYD YVDPRELTTQ LETKKVPGLF LAGQINGTTG YEEAAAQGII AGVNAAAKVF
KKPPLLISRT EGYIGVLIDD LTTEGTTEPY RMFTSRSEFR VSLRPDNADQ RLTEKGYAIG
CVSRERIEKT REVFRKMQEV VQILKSDVRS TSKWRQLLKM KISKDTGYKS AFDMLSVTDE
SVTFAKLAKQ LPQLGHLDGD SGLARRIEIE TKYVFAVAKQ QGQVNDIRRN EQMIVPDDID
YNSPDLNLSN EDREKLMKHL PRTV
//
