ID A0A195BUP9_9HYME Unreviewed; 829 AA.
AC A0A195BUP9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
GN ORFNames=ALC53_00762 {ECO:0000313|EMBL:KYM92307.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM92307.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM92307.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM92307.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM92307.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-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}.
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DR EMBL; KQ976401; KYM92307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195BUP9; -.
DR STRING; 520822.A0A195BUP9; -.
DR Proteomes; UP000078540; 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; 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; 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; PF16044; DUF4796; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 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:UP000078540}.
FT DOMAIN 743..815
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
SQ SEQUENCE 829 AA; 93304 MW; A341BAC51CADC6FF CRC64;
MNNDPGIICF HHCKTKNVFC MQIPAICPVC SSQMQNFIVD PFRVPCPFAN AIHNPTSVVI
RPSRGSFLDD YDMTRDDLHI GIVNSNGGIV EFDKEGLVEN DITKWTDCIV LELVPAAWTA
QWDKALILMS KDIKWKSINY DVINMNCFNF VLEFFNNLGY RDLRFKSKEE LCERLILSKM
YKAMQYVSLY RIQLINTKET KFDVIVVGGG HAGTEASAAA VRMGAKTLLV TQKKSTIGEM
SCNPSFGGIG KGHLMREVDA LDGVCCRICD ISGIYYRVLN KSKGPAVWGL RAQIDRKLYK
KHLQAELFNM PRLHIYESSV EDLILENDSL SCQGVILRDG TKIFGNAVVI TTGTFLKGQI
NIGLEKRPAG RLNDEPSIGL ANTLDRLGFR IGRLKTGTPP RLEKESIDFT KCTAYPPDDS
PIPFSFMSNN VWLPPDKQIL THLTYTNENV AKIIKDNMHC NLHVTEEITG PRYCPSIESK
ILRFKALKHQ IWLEPEGLDS PLIYPSGLSC TLPEEKQVEL VKCIPGLENA RLVKPGYGVE
YDYVDPRELT IQLETRKIPG LFLAGQINGT TGYEEAAAQG IVAGINAAAK VFKKPPLLIS
RTEGYIGVLI DDLTTGGTTE PYRMFTSRSE FRVSLRPDNA DQRLTEKGYA IGCVSRERIE
KTREVFRKMQ EAVQILKSDV RSTSKWRRLL KMKISKDTGH KSAFDMLSVT DESVTFAKLA
KWLPQLGHLD GDPGLARRIE IETKYIFAVA EQQDQVNDIR RNEQMIIPDD IDYNSPDLNL
SNEDREKLTK HLPRTIAAAN KISGVTPSAI LRLLYYIRFH SNENVAKAQ
//
