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Database: UniProt
Entry: B9DKG2_STACT
LinkDB: B9DKG2_STACT
Original site: B9DKG2_STACT 
ID   B9DKG2_STACT            Unreviewed;       350 AA.
AC   B9DKG2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Molybdopterin biosynthesis protein MoeB {ECO:0000313|EMBL:CAL28985.1};
GN   OrderedLocusNames=Sca_2080 {ECO:0000313|EMBL:CAL28985.1};
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL28985.1, ECO:0000313|Proteomes:UP000000444};
RN   [1] {ECO:0000313|EMBL:CAL28985.1, ECO:0000313|Proteomes:UP000000444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300 {ECO:0000313|EMBL:CAL28985.1,
RC   ECO:0000313|Proteomes:UP000000444};
RX   PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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DR   EMBL; AM295250; CAL28985.1; -; Genomic_DNA.
DR   RefSeq; WP_015901321.1; NC_012121.1.
DR   AlphaFoldDB; B9DKG2; -.
DR   GeneID; 60544211; -.
DR   KEGG; sca:SCA_2080; -.
DR   eggNOG; COG0476; Bacteria.
DR   HOGENOM; CLU_013325_10_1_9; -.
DR   OrthoDB; 9804286at2; -.
DR   BioCyc; SCAR396513:SCA_RS10500-MONOMER; -.
DR   Proteomes; UP000000444; Chromosome.
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          22..257
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  39350 MW;  E077FC16B6C0A1EA CRC64;
     MIDNAHHSEK NSNNNIRSDE RFSRQTRYTP FGNDGQKALE NAHIMVMGAG ALGSHLAEQL
     VRMGIGKLTI VDMDIVEISN LHRQALYDEN DAIEMQPKVY ALAEKLSQIN SNVEIYPIYQ
     EITPTNIEHM IKDASPDILL DGMDHFAIRF LFNEVCHKLH LPWVYGAAVG GKGSIYAIDF
     TGPCLRCLMQ ETPETAESCA INGVIPPVIM QVVSYQIAEV MRYLSGKRFS GKLITVEPFN
     IKQQSIDVSH LRNPDCPLCG NGEYERLGIA QPKWIEGSCG DTYVFRFKPQ HFENAVLFPG
     NILKSNAFVK LLNIEGHSAT LFKDGRMNVH GIENDNHAEK LYQQLLKSMK
//
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