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Database: UniProt
Entry: M9RCI1_9RHOB
LinkDB: M9RCI1_9RHOB
Original site: M9RCI1_9RHOB 
ID   M9RCI1_9RHOB            Unreviewed;       573 AA.
AC   M9RCI1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN   ORFNames=OAN307_c18440 {ECO:0000313|EMBL:AGI67500.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI67500.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI67500.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI67500.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
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DR   EMBL; CP003740; AGI67500.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9RCI1; -.
DR   STRING; 391626.OAN307_c18440; -.
DR   KEGG; oat:OAN307_c18440; -.
DR   eggNOG; COG0476; Bacteria.
DR   HOGENOM; CLU_476376_0_0_5; -.
DR   Proteomes; UP000005307; Chromosome.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
PE   4: Predicted;
FT   DOMAIN          298..430
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   573 AA;  63368 MW;  16EAAB711D6BFB2A CRC64;
     MMADTPKEGR LIQECGELTE LASSSVWIQD AYFSRNSSGL LTWSFMLVSE DRRIPLHLIF
     PALFPDLPPF VLPADDTARL SQHQYGEGGE LCLQYRPDNW HPDCKSTDVV QSAKALLDAT
     PADDFLSEVK SDHPSDLPSM LARYPRRFML TPETASLLRR RLAGHVTELR LTLEHRIGST
     EAQVARVASI GYDAGLTVPS DGPGFGGKVV QGVLYRLRSI QTLPDLTTED VREQLYMFLP
     RWLRGMIAKT EDMLVVLSNG QQEVLFRVQH QATERNMDLF HTFEPPHAKE RRVHGQMFQK
     SSVCIIGAGS LGSKVAASLT REGVGHFMLL DNDVLWSDNL VRNELDEMDV GHHKATSLKH
     RLLRIKPGLR VSALSISLTS QSTVQSIAKL GEIISSCDLV IDTTADSGVF RMAAAICTQK
     KRPIVWARVY AGGIGGLVAR SVPYEDPPPM VAALQLQAWC DAKGKMPPEG HERDYGVQGD
     GQDEPLFASD GDVGAISNRL ARHALDVLSP SEMRVHPEPA YYIGLRKGWI FDHPFDTHPV
     VYSLHGGWGD RGTEEGGLNV EKVLNSLGVK HDS
//
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