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Database: UniProt
Entry: A0A1F4ZU14_9BACT
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Original site: A0A1F4ZU14_9BACT 
ID   A0A1F4ZU14_9BACT        Unreviewed;       240 AA.
AC   A0A1F4ZU14;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN   ORFNames=A2Y86_00415 {ECO:0000313|EMBL:OGD09929.1};
OS   Candidatus Aminicenantes bacterium RBG_13_62_12.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1797269 {ECO:0000313|EMBL:OGD09929.1, ECO:0000313|Proteomes:UP000178836};
RN   [1] {ECO:0000313|EMBL:OGD09929.1, ECO:0000313|Proteomes:UP000178836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGD09929.1}.
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DR   EMBL; MEXX01000072; OGD09929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4ZU14; -.
DR   STRING; 1797269.A2Y86_00415; -.
DR   Proteomes; UP000178836; Unassembled WGS sequence.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
FT   DOMAIN          11..236
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   240 AA;  25715 MW;  F861BA44DB3340F9 CRC64;
     MSDERRRYLR QLTLSGWDQE RLDKSCVLVA GVGGLGSASS LYLAAAGVGR LRLCDADRVE
     ISDLNRQVLF SMSSLGKPKV EEAARRLAGL NPETSVEIFE ERLTGENIDR LAAECDIIVD
     GMDNMEGRFV LNGYSVRKGI PYVYGAVHGW EGMAALIHPP ETGCLSCLIP SIPPRPESPV
     PVAGFVPGAI GLIQAAEALK QLMNLGGALA GRLLIYDGRS MSFDLVAWGR NPGCPVCGSP
//
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