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Database: UniProt
Entry: D8G552_9CYAN
LinkDB: D8G552_9CYAN
Original site: D8G552_9CYAN 
ID   D8G552_9CYAN            Unreviewed;       290 AA.
AC   D8G552;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=UBA/THIF-type NAD/FAD binding fold {ECO:0000313|EMBL:CBN57742.1};
GN   ORFNames=OSCI_3510025 {ECO:0000313|EMBL:CBN57742.1};
OS   Kamptonema sp. PCC 6506.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Kamptonema.
OX   NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN57742.1, ECO:0000313|Proteomes:UP000004532};
RN   [1] {ECO:0000313|EMBL:CBN57742.1, ECO:0000313|Proteomes:UP000004532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6506 {ECO:0000313|EMBL:CBN57742.1,
RC   ECO:0000313|Proteomes:UP000004532};
RX   PubMed=20675499; DOI=10.1128/JB.00704-10;
RA   Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT   "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT   reveals several gene clusters responsible for the biosynthesis of toxins
RT   and secondary metabolites.";
RL   J. Bacteriol. 192:5264-5265(2010).
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:CBN57742.1}.
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DR   EMBL; CACA01000315; CBN57742.1; -; Genomic_DNA.
DR   RefSeq; WP_007356934.1; NZ_CACA01000315.1.
DR   AlphaFoldDB; D8G552; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000004532; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..243
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   REGION          252..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  31836 MW;  7D2187362282FF8B CRC64;
     MLHLTPTELE RYRRQIMLPG FGEEAQKRLK SSTVLVTGVG GLGGTAALYL AVAGVGRLIL
     VRGGELRLDD MNRQILMTDD WVGKPRVFKA KETLEEINPD VQVDAIFEYV TPENVDTLVQ
     AADIVLDCAH NFIERDLLNA ACVQWDKPMV EAAMNDMEAY LTTIVPGETP CLSCIFPEKP
     DWDKRGFGVI GAVSGTLACL TALEAIKLLA GIGKPLLSQL LTMDLGSLEF AKRRPYHDPN
     CPVCSHKSRD KLESKLNQKF PTPNPSRSSA TKREKPGIPL PQNSLPIAIS
//
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