ID A0A093PVE0_PHACA Unreviewed; 575 AA.
AC A0A093PVE0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Protein MTO1 homolog, mitochondrial {ECO:0000256|ARBA:ARBA00013407};
DE Flags: Fragment;
GN ORFNames=N336_00350 {ECO:0000313|EMBL:KFW76032.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW76032.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW76032.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW76032.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL413676; KFW76032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PVE0; -.
DR Proteomes; UP000053238; 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 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 SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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:UP000053238}.
FT DOMAIN 448..520
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT REGION 545..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW76032.1"
FT NON_TER 575
FT /evidence="ECO:0000313|EMBL:KFW76032.1"
SQ SEQUENCE 575 AA; 63883 MW; F8509D7D3F9B797F CRC64;
QKEILNTPLL TVREASVEDL VLAEPDSDRP GKCQVTGVVL GDGSTVHAGS VILTTGTFLR
GMVLIGLEMH PAGRLGDQPA IGLAETLEKL GFAVGRLKTG TPPRLAKDTI DFSGLEERAA
DNPPVPFSFL SEAVWIKPED QLSCYLTRTT AKAQQIIHDN LHLNNHIRET TKGPRYCPSL
ESKVLRFPNR EHQVWLEPEG LESNVIYPQG MSMTLPPELQ EQVIKSIPGL EKAKMLQPGY
GVQYDFLDPR QLTASLESRL VQRLFFAGQI NGTTGYEEAA AQGVIAGINA CLRVHGKPPF
IVSRTESYVG VLIDDLTTLG TSEPYRMFTS RVEFRMSLRP DNADARLTHR GFEEAGCVSQ
QRYEQAVKMR AALEDGIATL KSLQFSISKW SRLMPEVPFS SSRRSPVSAF DILQHPEANM
EVLARAVPDP LGKLAQWREL AERLKIEAAY EWCVANQQQE IEEVRRDEAL QLPEDLDYFA
IDASLSAEVR EKLDSNRPQT IGAVSRIPGI TPAAIVNLLR FVKTSHQKTE KLKALPQTGR
YLPGKMYSEK ATSQQQIPAE FSEEEPESTF VKTPL
//
