ID E9FMX3_9STRE Unreviewed; 377 AA.
AC E9FMX3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=ThiF family protein {ECO:0000313|EMBL:EFX58563.1};
GN ORFNames=HMPREF0851_01146 {ECO:0000313|EMBL:EFX58563.1};
OS Streptococcus sp. M334.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563038 {ECO:0000313|EMBL:EFX58563.1, ECO:0000313|Proteomes:UP000003840};
RN [1] {ECO:0000313|EMBL:EFX58563.1, ECO:0000313|Proteomes:UP000003840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M334 {ECO:0000313|EMBL:EFX58563.1,
RC ECO:0000313|Proteomes:UP000003840};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. M334.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GL732488; EFX58563.1; -; Genomic_DNA.
DR RefSeq; WP_000675234.1; NZ_GL732488.1.
DR AlphaFoldDB; E9FMX3; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_8_1_9; -.
DR OrthoDB; 9804286at2; -.
DR Proteomes; UP000003840; Unassembled WGS sequence.
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 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 117..340
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 377 AA; 43117 MW; 22536E5640A34DB7 CRC64;
MKFYHPRIKE IYPVYKLHKN LFRIGLQIGI TTEIKDDNNK MWNLVNILDG RPFQDILNIM
LTKYDDLTEE DITGALELLD NEGVLEEAGE IQDIKERYHS NIYYFSRYLN SFQDSIATQK
KIHQSTILLL GLGGGGSNIL TLLAGLGPKK IKIVDFDIVE QSNLGRQFLY KEDDIGLSKV
QIAHREVTKM NSDIEVETHN IRITSVSDLI PLLDDVDITI CVIDKPQYDI QRIVNKAIVT
KNIPCIFGAS QVSRGRVYSV IPYQTGCFDC LNIHYTKIDT LFLEQFHGVR TITKTIPTIA
YGPAIFQLTS AIVDETIRLL TQYTEPISLN HQYEINYENG ASFTHDSWGR YLDECPTCGT
GKEDDWEIFS KYGELKL
//
